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IDPMIDYEARSequenceNameLengthN-ter MODC-ter MODLinear/CyclicChiralityChem-MODOriginNatureIncubation TimeConcentrationHalf LifeUnits Half LifeProteaseAssayTest SampleVivo/VitroReferencePatent No.Activity
4001
389173312024
DHYLSTQTILSKDPNEEK-DBCO-N3-TTAATTCTGGGGGAGCCTTTTGTGGGTAGGGTTTTGTGGGTAGGGCGGGTTGGTTTTCGGGTTGGTTTTGCCCCGGAGGAGGAATT-N3-DBCO-RDHMVLLESVTAAGIT 
Aptamer-split peptide conjugate34DBCO modified S10 at C terminusDBCO modified S11 peptide at N terminusLinearLAzide-modified aptamer fragments (5 SSA and 3 SSA) "TTAATTCTGGGGGAGCCTTTTGTGGGTAGGGTTTTGTGGGTAGGGCGGGTTGGTTTTCGGGTTGGTTTTGCCCCGGAGGAGGAATT" are conjugated with DBCO-modified peptides (S10 and S11) , DBCO = DibenzocyclooctyneAptamer-peptide complexHetero modulator for split GFP in response to ATPSamples were collected every 24 h for 7 days1 μM4C57Bl/6N Mice serum proteaseSerum stability assayC57BL/6N Mice serumIn VitroNoneNoneA shorter antisense DNA of 11 nucleotides (aptamer) showed an EC50 value of 238 μM
4002
388071462024
HAEGTFTSDVSSYLEGQAAKEFIAWLVKGRGHAEGTFTSDVSSYLEGQAAKEFIAWLVKGRG
TG10362FreeFc region of IgG joined through (CH2-CH3) IgD LinearLGLP-1 dimerizationGLP-1 analogsAntiobesityBlood sampling time points:(1) Within 2 h before dosing on day 1 and day 8,(2) 6, 12, 24, 36, 48, 72, 96, 144 and 168 h (before dosing on day 15) after dosing on day 8 (3)Within 2 h before dosing on day 64, day 71 and day 78 (4)6, 12, 24, 36, 48, 72, 96, 144, 168, 336 and 504 h after dosing on day 78.15.0 mg116  ± 10.8 (Terminal Half Life)Human serum protease Double-antibody sandwich assayHuman serumIn VivoNoneNoneN.A.
4003
388071462024
HAEGTFTSDVSSYLEGQAAKEFIAWLVKGRGHAEGTFTSDVSSYLEGQAAKEFIAWLVKGRG
TG10362FreeFc region of IgG joined through (CH2-CH3) IgD LinearLGLP-1 dimerizationGLP-1 analogsAntiobesityBlood sampling time points:(1) Within 2 h before dosing on day 1, day 8 and day 15, (2) 6, 12, 24, 36, 48, 72, 96, 144 and 168 h (before dosing on day 22) after dosing on day 15 (3)Within 2 h before dosing on day 64, day 71 and day 78 (4) 6, 12, 24, 36, 48, 72, 96, 144, 168, 336 and 504 h after dosing on day 78.22.5 mg110  ± 11.9 (Terminal Half Life)Human serum protease Double-antibody sandwich assayHuman serumIn VivoNoneNoneN.A.
4004
388071462024
HAEGTFTSDVSSYLEGQAAKEFIAWLVKGRGHAEGTFTSDVSSYLEGQAAKEFIAWLVKGRG
TG10362FreeFc region of IgG joined through (CH2-CH3) IgD LinearLGLP-1 dimerizationGLP-1 analogsAntiobesityBlood sampling time points: (1) Within 2 h before dosing on day 1, day 8, day 15 and day 22, (2)6, 12, 24, 36, 48, 72, 96, 144 and 168 h (before dosing on day 29) after dosing on day 22,(3)Within 2 h before dosing on day 64, day 71 and day 78 (4) 6, 12, 24, 36, 48, 72, 96, 144, 168, 336 and 504 h after dosing on day 78.30.0 mg116  ± 9.34 (Terminal Half Life)Human serum protease Double-antibody sandwich assayHuman serumIn VivoNoneNoneN.A.
4005
387890612024
HAEGTFTSDVSSYLEGQAAKEFIAWLVKGRG
Liraglutide31FreeFreeLinearLLys-30 is replaced by Arg and Lys-20 is acylated with a C16 palmitic acid linkd with γGluGLP-1 analogsAntidiabetesBlood sample was collected for IV-dosed rats, time points were pre-dose, 1 min, 5 min, 15 min, 30 min, 1 hr, 2 hr, 4 hr, 8 hr, 10 hr, and 24 hr1 mg/kg5.3 ± 1.5 Male SD rats plasma proteaseUHPLCMale SD rats plasmaIn VivoNoneNoneN.A.
4006
387890612024
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
Exenatide39FreeAmidationLinearLNoneExendin-4 analogsAntidiabetesBlood sample was collected for IV-dosed rats, time points were pre-dose, 1 min, 5 min, 15 min, 30 min, 1 hr, 2 hr, 4 hr, 8 hr, 10 hr, and 24 hr1 mg/kg0.5 ± 0.1Male SD rats plasma proteaseUHPLCMale SD rats plasmaIn VivoPDB id: 7MLLNoneN.A.
4007
387890612024
HAEGTFTSDVSSYLEGQAAKEFIAWLVKGRG
Liraglutide31FreeFreeLinearLLys-30 is replaced by Arg and Lys-20 is acylated with a C16 palmitic acid linkd with γGluGLP-1 analogsAntidiabetesBlood samples (250 μL) were collected at predetermined time points. For SC-dosed rats, time points included pre-dose, 15 min, 30 min, 1 hr, 2 hr, 3 hr, 4 hr, 8 hr, 10 hr, 24 hr, and 30 hr1 mg/kg9.1 ± 2.9 Male SD rats plasma proteaseUHPLCMale SD rats plasmaIn VivoNoneNoneN.A.
4008
387890612024
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
Exenatide39FreeAmidationLinearLNoneExendin-4 analogsAntidiabetesBlood sample was collected for IV-dosed rats, time points were pre-dose, 1 min, 5 min, 15 min, 30 min, 1 hr, 2 hr, 4 hr, 8 hr, 10 hr, and 24 hr1 mg/kg1.03 ± 0.10Male SD rats plasma proteaseUHPLCMale SD rats plasmaIn VivoPDB id: 7MLLNoneN.A.
4009
387890612024
HAEGTFTSDVSSYLEGQAAKEFIAWLVKGRG
Liraglutide (Lymph cannulated)31FreeFreeLinearLLys-30 is replaced by Arg and Lys-20 is acylated with a C16 palmitic acid linkd with γGluGLP-1 analogsAntidiabetesLymph was collected continuously into tubes at specified time intervals: predose, 0–15 min, 15–30 min, 30 45 min, 45–60 min, 1–1.5 hr, 1.5–2 hr, 2–3 hr, 3–4 hr, 4–6 hr, 6–8 hr, 8–10 hr, 10–24 hr, and 24–30 hr2 mg/kg12.61 ± 5.45 Male SD rats lymph proteaseUHPLCMale SD rats thoraic lymphIn VivoNoneNoneN.A.
4010
387890612024
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
Exenatide (Lymph cannulated)39FreeAmidationLinearLNoneExendin-4 analogsAntidiabetesLymph was collected continuously into tubes at specified time intervals: predose, 0–15 min, 15–30 min, 30 45 min, 45–60 min, 1–1.5 hr, 1.5–2 hr, 2–3 hr, 3–4 hr, 4–6 hr, 6–8 hr, 8–10 hr, 10–24 hr, and 24–30 hr1 mg/kg10.26 ± 6.51 Male SD rats lymph proteaseUHPLCMale SD rats thoraic lymphIn VivoPDB id: 7MLLNoneN.A.
4011
387853342024
IsoV-DTHFPCIKFEPRSKGCK
Rusfertide (PTG-300)18IsoV = Isovaeryl at position 1AmidationCyclic(C7-C17 Disulfide Linkage)LLys8 conjugation with palmitoyl-Glu(2)-OHSynthetic Provides therapy for PV and HemochromatosisN.A.1 mg17.9 ± 2.1Human plasma proteaseHPLC-MSHuman plasma In VivoNoneNoneN.A.
4012
387853342024
IsoV-DTHFPCIKFEPRSKGCK
Rusfertide (PTG-300)18IsoV = Isovaeryl at position 1AmidationCyclic(C7-C17 Disulfide Linkage)LLys8 conjugation with palmitoyl-Glu(2)-OHSynthetic Provides therapy for PV and HemochromatosisN.A.3 mg21.3 ± 6.2Human plasma proteaseHPLC-MSHuman plasma In VivoNoneNoneN.A.
4013
387853342024
IsoV-DTHFPCIKFEPRSKGCK
Rusfertide (PTG-300)18IsoV = Isovaeryl at position 1AmidationCyclic(C7-C17 Disulfide Linkage)LLys8 conjugation with palmitoyl-Glu(2)-OHSynthetic Provides therapy for PV and HemochromatosisN.A.10 mg26.1 ± 7.0Human plasma proteaseHPLC-MSHuman plasma In VivoNoneNoneN.A.
4014
387853342024
IsoV-DTHFPCIKFEPRSKGCK
Rusfertide (PTG-300)18IsoV = Isovaeryl at position 1AmidationCyclic(C7-C17 Disulfide Linkage)LLys8 conjugation with palmitoyl-Glu(2)-OHSynthetic Provides therapy for PV and HemochromatosisN.A.20 mg35.4 ± 9.6 Human plasma proteaseHPLC-MSHuman plasma In VivoNoneNoneN.A.
4015
387853342024
IsoV-DTHFPCIKFEPRSKGCK
Rusfertide (PTG-300)18IsoV = Isovaeryl at position 1AmidationCyclic(C7-C17 Disulfide Linkage)LLys8 conjugation with palmitoyl-Glu(2)-OHSynthetic Provides therapy for PV and HemochromatosisN.A.40 mg45.0 ± 13Human plasma proteaseHPLC-MSHuman plasma In VivoNoneNoneN.A.
4016
387853342024
IsoV-DTHFPCIKFEPRSKGCK
Rusfertide (PTG-300)18IsoV = Isovaeryl at position 1AmidationCyclic(C7-C17 Disulfide Linkage)LLys8 conjugation with palmitoyl-Glu(2)-OHSynthetic Provides therapy for PV and HemochromatosisN.A.80 mg52.5 ± 17Human plasma proteaseHPLC-MSHuman plasma In VivoNoneNoneN.A.
4017
387853342024
IsoV-DTHFPCIKFEPRSKGCK
Rusfertide (PTG-300)18IsoV = Isovaeryl at position 1AmidationCyclic(C7-C17 Disulfide Linkage)LLys8 conjugation with palmitoyl-Glu(2)-OHSynthetic Provides Therapy For Pv And HemochromatosisN.A.40 mg49.6 ± 18Human Plasma Proteasehigh-performance liquidchromatography–tandem mass spectrometry methodHuman plasma after 2 once weekly repeated doseIn VivoNoneNoneN.A.
4018
387853342024
IsoV-DTHFPCIKFEPRSKGCK
Rusfertide (PTG-300)18IsoV = Isovaeryl at position 1AmidationCyclic(C7-C17 Disulfide Linkage)LLys8 conjugation with palmitoyl-Glu(2)-OHSynthetic Provides Therapy For Pv And HemochromatosisN.A.40 mg36.1 ± 21Human Plasma Proteasehigh-performance liquidchromatography–tandem mass spectrometry methodHuman plasma after 2 once weekly repeated doseIn VivoNoneNoneN.A.
4019
387372832024
LAEAKVLANRELDKYGVSDFYKRLINKAKTVEGVEALKLHILAALP-FRRG-(E5C3)-(GN)
ABD035-immunoGNN.A.P1h3His-tagLinearLHumanized anti-HER2 scFv P1h3, albumin-binding peptides (ABD035 or dAb7h8), cathepsin B-cleavable peptide B2, endosome-disruptive peptide E5C3 fusion protein, GN= Gasdermin-NSynthetic AntitumorBlood samples were promptly collected at 5, 10, 30, 60, 360, and 720 min0.1 μmol/kg35.22BALB/c mice serum proteaseELISABALB/c mice serumIn VivoNoneNoneCytotoxicity of ABD035-immunoGN in N87 cells reached as high as 62 %, compared to 38 % for immunotBid after 24 h of incubation
4020
387372832024
FRRG-(E5C3)-(GN)
immunoGNN.A.P1h3His-tagLinearLHumanized anti-HER2 scFv P1h3, albumin-binding peptides (ABD035 or dAb7h8), cathepsin B-cleavable peptide B2, endosome-disruptive peptide E5C3 fusion protein, GN= Gasdermin-NSynthetic AntitumorBlood samples were promptly collected at 5, 10, 30, 60, 360, and 720 min0.1 μmol/kg4.599BALB/c mice serum proteaseELISABALB/c mice serumIn VivoNoneNoneCytotoxicity of ABD035-immunoGN in N87 cells reached as high as 62 %, compared to 38 % for immunotBid after 24 h of incubation
4021
387372832024
DIQMTQSPSSLSAVGDRVTITCRASQSISSYLNWYQQKPGKAPKLLIYRNSPLQSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQTYRVPPTFGQGTKVEIKR-FRRG-(E5C3)-(GN)
dAb7h8-immunoGNN.A.P1h3His-tagLinearLHumanized anti-HER2 scFv P1h3, albumin-binding peptides (ABD035 or dAb7h8), cathepsin B-cleavable peptide B2, endosome-disruptive peptide E5C3 fusion protein, GN= Gasdermin-NSynthetic AntitumorBlood samples were promptly collected at 5, 10, 30, 60, 360, and 720 min0.1 μmol/kg31.25BALB/c mice serum proteaseELISABALB/c mice serumIn VivoNoneNoneCytotoxicity of ABD035-immunoGN in N87 cells reached as high as 62 %, compared to 38 % for immunotBid after 24 h of incubation
4022
387210432024
SVSEIQLMHNLGKHLNSMERVEWLRKKLQDVHNFC
EXT607 (R=OH)35FreeCys modified PTH-1 linked with VitD3 through (PEG)36LinearLR= OH for Cys35PTH-1 derivativeTreatment of HypoparathyroidismBlood samples were collected at 0 (pre-dose), 0.083 (IV only), 0.25, 0.5, 1, 2, 4, 6, 12, 24, 36, 48, 60, and 72 h post-dose100 µg/kg8.43Rats plasma proteaseELISARats plasmaIn VivoNoneNoneEC50(nM) = 23.7 (Calcium responses of EXT607 in mammalian cells overexpressing human PTHR1)
4023
387210432024
SVSEIQLMHNLGKHLNSMERVEWLRKKLQDVHNFC
EXT607 (R=OH)35FreeCys modified PTH-1 linked with VitD3 through (PEG)36LinearLR= OH for Cys35PTH-1 derivativeTreatment of HypoparathyroidismBlood samples were collected at 0 (pre-dose), 0.083 (IV only), 0.25, 0.5, 1, 2, 4, 6, 12, 24, 36, 48, 60, and 72 h post-dose30 µg/kg 15.4Rats plasma proteaseELISARats plasmaIn VivoNoneNoneEC50(nM) = 23.7 (Calcium responses of EXT607 in mammalian cells overexpressing human PTHR1)
4024
387210432024
SVSEIQLMHNLGKHLNSMERVEWLRKKLQDVHNFC
EXT607 (R=OH)35FreeCys modified PTH-1 linked with VitD3 through (PEG)36LinearLR= OH for Cys35PTH-1 derivativeTreatment of HypoparathyroidismBlood samples were collected at 0 (pre-dose), 0.083 (IV only), 0.25, 0.5, 1, 2, 4, 6, 12, 24, 36, 48, 60, and 72 h post-dose100 µg/kg7.36Rats plasma proteaseELISARats plasmaIn VivoNoneNoneEC50(nM) = 23.7 (Calcium responses of EXT607 in mammalian cells overexpressing human PTHR1)
4025
387210432024
SVSEIQLMHNLGKHLNSMERVEWLRKKLQDVHNFC
EXT607 (R=OH)35FreeCys modified PTH-1 linked with VitD3 through (PEG)36LinearLR= OH for Cys35PTH-1 derivativeTreatment of HypoparathyroidismBlood samples were collected at 0 (pre-dose), 0.083 (IV only), 0.25, 0.5, 1, 2, 4, 6, 12, 24, 36, 48, 60, and 72 h post-dose300 µg/kg9.21Rats plasma proteaseELISARats plasmaIn VivoNoneNoneEC50(nM) = 23.7 (Calcium responses of EXT607 in mammalian cells overexpressing human PTHR1)
4026
387210432024
SVSEIQLMHNLGKHLNSMERVEWLRKKLQDVHNFC
EXT607 (R=OH)35FreeCys modified PTH-1 linked with VitD3 through (PEG)36LinearLR= OH for Cys35PTH-1 derivativeTreatment of HypoparathyroidismBlood samples were collected at 0 (pre-dose), 0.083 (IV only), 0.25, 0.5, 1, 2, 4, 6, 12, 24, 36, 48, 60, and 72 h post-dose0.02 mg/kg32.3Cynomolgus monkeys plasma proteaseELISACynomolgus monkeys plasmaIn VivoNoneNoneEC50(nM) = 23.7 (Calcium responses of EXT607 in mammalian cells overexpressing human PTHR1)
4027
387210432024
SVSEIQLMHNLGKHLNSMERVEWLRKKLQDVHNFC
EXT607 (R=OH)35FreeCys modified PTH-1 linked with VitD3 through (PEG)36LinearLR= OH for Cys35PTH-1 derivativeTreatment of HypoparathyroidismBlood samples were collected at 0 (pre-dose), 0.083 (IV only), 0.25, 0.5, 1, 2, 4, 6, 12, 24, 36, 48, 60, and 72 h post-dose0.007 mg/kg24Cynomolgus monkeys plasma proteaseELISACynomolgus monkeys plasmaIn VivoNoneNoneEC50(nM) = 23.7 (Calcium responses of EXT607 in mammalian cells overexpressing human PTHR1)
4028
387210432024
SVSEIQLMHNLGKHLNSMERVEWLRKKLQDVHNFC
EXT607 (R=OH)35FreeCys modified PTH-1 linked with VitD3 through (PEG)36LinearLR= OH for Cys35PTH-1 derivativeTreatment of HypoparathyroidismBlood samples were collected at 0 (pre-dose), 0.083 (IV only), 0.25, 0.5, 1, 2, 4, 6, 12, 24, 36, 48, 60, and 72 h post-dose0.02 mg/kg24.3Cynomolgus monkeys plasma proteaseELISACynomolgus monkeys plasmaIn VivoNoneNoneEC50(nM) = 23.7 (Calcium responses of EXT607 in mammalian cells overexpressing human PTHR1)
4029
387210432024
SVSEIQLMHNLGKHLNSMERVEWLRKKLQDVHNFC
EXT607 (R=OH)35FreeCys modified PTH-1 linked with VitD3 through (PEG)36LinearLR= OH for Cys35PTH-1 derivativeTreatment of HypoparathyroidismBlood samples were collected at 0 (pre-dose), 0.083 (IV only), 0.25, 0.5, 1, 2, 4, 6, 12, 24, 36, 48, 60, and 72 h post-dose0.07 mg/kg27.7Cynomolgus monkeys plasma proteaseELISACynomolgus monkeys plasmaIn VivoNoneNoneEC50(nM) = 23.7 (Calcium responses of EXT607 in mammalian cells overexpressing human PTHR1)
4030
386425032024
VPALR
VPALR-SUL5FreeSul = SulpirideLinearLNoneDerived from the Ku70 domainAntidepressantBlood samples were collected from the orbital venous plexus at various time points (5 min, 15 min, 30 min, 1 h, 2 h, 3 h, 5 h, 7 h, 9 h, 12 h, 24 hEquivalent of 3 mg/kg of sulpiride17.49 ± 13.50Male SD rats plasma proteaseLC-MS/MSMale SD rats plasmaIn VivoNoneNoneVPALR-SUL showed almost 100% cell viability at all tested concentrations, which indicates excellent biocompatibility with HT22 nerve cells and minimal cytotoxicity
4031
386139962024
AGILKRW
PepH37FreeAmidationLinearLNoneSyntheticAnticancerAt different time points (0, 1, 5, 10, 30, 60, 120, and 360 min), 120 µL aliquots were collected and incubated with equal volume of 96% ethanol for 30 min at 4⁰C1 mM21.00 ± 2.91Human serum proteaseRP-HPLCHuman serumIn VitroNoneNoneIC50 > 100.0 for TNBC MDA-MB-231 Monolayer
4032
386139962024
WRRRYRRWRRRRRWRRRPRR
vCPP231920FreeAmidationLinearLNoneSyntheticAnticancerAt different time points (0, 1, 5, 10, 30, 60, 120, and 360 min), 120 µL aliquots were collected and incubated with equal volume of 96% ethanol for 30 min at 4⁰C1 mM280.40 ± 59.20Human serum proteaseRP-HPLCHuman serumIn VitroNoneNoneIC50 = 4.00±1.03 for TNBC MDA-MB-231 Monolayer
4033
386139962024
AGILKRW-Ahx-WRRRYRRWRRRRRQRRRPRR
PepH3-vCPP2319 527FreeAmidationLinearLAhx links two peptideSynthetic chimeric peptide of PepH3 and vCPP2319AnticancerAt different time points (0, 1, 5, 10, 30, 60, 120, and 360 min), 120 µL aliquots were collected and incubated with equal volume of 96% ethanol for 30 min at 4⁰C1 mM125.20 ± 34.21Human serum proteaseRP-HPLCHuman serumIn VitroNoneNoneIC50 = 5.20±1.04 for TNBC MDA-MB-231 Monolayer
4034
386010382024
YSEGTFTSDKSKYLDSQAAQDFVQWLLAGGPSSGAPPPS
DR10627 39FreeAmidationLinearLA palmitoyl group is conjugated to DR10627 via a -γ-glutamyl-linker connected to the Lys10 positionGLP-1 analogsAntiobesity, AntidiabetesBlood samples were collected at 0 (pre-dose), 0.5, 1, 2, 4, 8, 12, 16, 20, 24, 30, 38 and 48 h after administration1 nmol/kg5.80 ± 1.26Cynomolgus monkeys serum proteaseLC-MS/MSCynomolgus monkeys serumIn VivoNoneNoneThe glucose-lowering effect of 12 nmol/kg DR10627 reached its lowest point at 2 hours post-administration, and the effect lasted for 24 hours, indicating a long-lasting action
4035
386010382024
YSEGTFTSDKSKYLDSQAAQDFVQWLLAGGPSSGAPPPS
DR10627 39FreeAmidationLinearLA palmitoyl group is conjugated to DR10627 via a -γ-glutamyl-linker connected to the Lys10 positionGLP-1 analogsAntiobesity, AntidiabetesBlood samples were collected at 0 (pre-dose), 0.5, 1, 2, 4, 8, 12, 16, 20, 24, 30, 38 and 48 h after administration5 nmol/kg5.05 ± 0.405Cynomolgus monkeys serum proteaseLC-MS/MSCynomolgus monkeys serumIn VivoNoneNoneThe glucose-lowering effect of 12 nmol/kg DR10627 reached its lowest point at 2 hours post-administration, and the effect lasted for 24 hours, indicating a long-lasting action
4036
386010382024
YSEGTFTSDKSKYLDSQAAQDFVQWLLAGGPSSGAPPPS
DR10627 39FreeAmidationLinearLA palmitoyl group is conjugated to DR10627 via a -γ-glutamyl-linker connected to the Lys10 positionGLP-1 analogsAntiobesity, AntidiabetesBlood samples were collected at 0 (pre-dose), 0.5, 1, 2, 4, 8, 12, 16, 20, 24, 30, 38 and 48 h after administration26 nmol/kg4.19 ± 0.957Cynomolgus monkeys serum proteaseLC-MS/MSCynomolgus monkeys serumIn VivoNoneNoneThe glucose-lowering effect of 12 nmol/kg DR10627 reached its lowest point at 2 hours post-administration, and the effect lasted for 24 hours, indicating a long-lasting action
4037
385554442024
CGSNKGAIIGLM
Aβ11/T80@CSs-TGC12FreeLinked with Chol using PEG2k linkerLinearLNoneSyntheticTreating intracranial infections caused by multidrug resistant Acinetobacter BaumanniiBlood samples were collected at predetermined time points (0.25, 0.5, 1, 2, 4, 6, and 8 h),12.5 mg/kg1.26 ± 0.21SD rats plasma proteaseHPLCSD rats plasmaIn VivoNoneNoneBoth free TGC and Aβ11/T80@CSs-TGC displayed potent antimicrobial activity with a minimum inhibitory concentration of 2 μg/mL 
4038
385542472024
CKGKGAKCSRLMYDCCTGSCRSGKC
MVIIA25FreeAmidationCyclic (C1-C16,C8-C20, C15-C25)LNoneDerived from the venom of cone snails (genus Conus)Treatment of Refractory Chronic PainAt 0, 1, 2, 4, 8, and 24 h, aliquots of peptides MVIIA at 37 celsisus100 µM8Human serum proteaseHPLCHuman serumIn VitroNoneNoneN.A.
4039
385542472024
CKGKGAKCSRLMYDCCTGSCRSGKC
K2-MVIIA25FreeAmidationCyclic (C1-C16,C8-C20, C15-C25)LAlkyl chain conjugated with Lys2 side chainDerived from the venom of cone snails (genus Conus)Treatment of Refractory Chronic PainAt 0, 1, 2, 4, 8, and 24 h, aliquots of peptides MVIIA at 37 celsisus100 µMRemained intact for 78.68% after 24 Hours Human serum proteaseHPLCHuman serumIn VitroNoneNoneN.A.
4040
385542472024
CKGKGAKCSRLMYDCCTGSCRSGKC
K2-K4-MVIIA25FreeAmidationCyclic (C1-C16,C8-C20, C15-C25)LAlkyl chain conjugated with Lys2, Lys4 side chainDerived from the venom of cone snails (genus Conus)Treatment of Refractory Chronic PainAt 0, 1, 2, 4, 8, and 24 h, aliquots of peptides MVIIA at 37 celsisus100 µMRemained intact for 75.61% after 24 Hours Human serum proteaseHPLCHuman serumIn VitroNoneNoneN.A.
4041
384936732024
ALWPPNLHAWVP
Peptide ALW12FreeFreeLinearLNoneSyntheticAlleviating Lupus NephritisN.A.12.5 mg/kg0.315 (Elimination Half Life)Cd1 mice plasma proteaseN.A.CD1 mice plasmaIn VivoNoneNoneKD(M) = 1.99*10-4 (Binding affinity of peptides to anti-dsDNA IgG3)
4042
384869972024
HsQGTFTSDKSKYLE-Aib-KAAQDFVEWLKAGGPSSGAPPPS
1907-B40FreeReplacing the amide bond with a C-terminal acidCyclic (Lactam Bridge K17 & D21)MixAt position 10 of the peptide sequence, modifications involving octadecanedioic acid (C18) and a glycine/serine-based linker "GGSGSG" were introduced, Aib modification,D-serineGLP-1 analogsAntidiabetesBlood samples were collected at 0 min (before peptides administration) and 10, 20, 30 min, 1, 2, 4, 6, 8, 24, 36, 48, 72 h, 4, 5, 6 and 7 day after peptides administration0.05 mg/kg∼16.8SD rats plasma proteaseLC-MS/MS SD rats plasmaIn VivoNoneNoneGLP-1R EC50 (nmol/L) = 0.088 (for 1907-B)
4043
384869972024
H-Aib-EGTFTSDVSSYLEGQAAKEFIAWLVRGRG
Semaglutide31FreeFreeLinearLAib modification at position 2, Lys20 side chain conjugated with (ADO-linker-Glu-C18)GLP-1 analogsAttenuates Renal FibrosisBlood samples were collected at 0 min (before peptides administration) and 10, 20, 30 min, 1, 2, 4, 6, 8, 24, 36, 48, 72 h, 4, 5, 6 and 7 day after peptides administration0.05 mg/kg∼8SD rats plasma proteaseLC-MS/MS SD rats plasmaIn VivoNoneNoneN.A.
4044
384869972024
HsQGTFTSDKSKYLE-Aib-KAAQDFVEWLKAGGPSSGAPPPS
1907-B40FreeReplacing the amide bond with a C-terminal acidCyclic (Lactam Bridge K17 & D21)MixAt position 10 of the peptide sequence, modifications involving octadecanedioic acid (C18) and a glycine/serine-based linker "GGSGSG" were introduced, Aib modification,D-serineGLP-1 analogsAntidiabetesBlood samples were collected at 0 min (before peptides administration) and 10, 20, 30 min, 1, 2, 4, 6, 8, 24, 36, 48, 72 h, 4, 5, 6 and 7 day after peptides administration0.05 mg/kg∼20.5SD rats plasma proteaseLC-MS/MS SD rats plasmaIn VivoNoneNoneGLP-1R EC50 (nmol/L) = 0.088 (for 1907-B)
4045
384869972024
H-Aib-EGTFTSDVSSYLEGQAAKEFIAWLVRGRG
Semaglutide31FreeFreeLinearLAib modification at position 2, Lys20 side chain conjugated with (ADO-linker-Glu-C18)GLP-1 analogsAttenuates Renal FibrosisBlood samples were collected at 0 min (before peptides administration) and 10, 20, 30 min, 1, 2, 4, 6, 8, 24, 36, 48, 72 h, 4, 5, 6 and 7 day after peptides administration0.05 mg/kg∼7.95SD rats plasma proteaseLC-MS/MS SD rats plasmaIn VivoNoneNoneN.A.
4046
384869972024
HsQGTFTSDKSKYLE-Aib-KAAQDFVEWLKAGGPSSGAPPPS
1907-B40FreeReplacing the amide bond with a C-terminal acidCyclic (Lactam Bridge K17 & D21)MixAt position 10 of the peptide sequence, modifications involving octadecanedioic acid (C18) and a glycine/serine-based linker "GGSGSG" were introduced, Aib modification,D-serineGLP-1 analogsAntidiabetesN.A.25.0 μg/kg 84Cynomolgus monkeys plasma proteaseHPLC-MS/MSCynomolgus monkeys plasmaIn VivoNoneNoneGLP-1R EC50 (nmol/L) = 0.088 (for 1907-B)
4047
384869972024
HsQGTFTSDKSKYLE-Aib-KAAQDFVEWLKAGGPSSGAPPPS
1907-B40FreeReplacing the amide bond with a C-terminal acidCyclic (Lactam Bridge K17 & D21)MixAt position 10 of the peptide sequence, modifications involving octadecanedioic acid (C18) and a glycine/serine-based linker "GGSGSG" were introduced, Aib modification,D-serineGLP-1 analogsAntidiabetesN.A.25.0 μg/kg N.A.Cynomolgus monkeys plasma proteaseHPLC-MS/MSCynomolgus monkeys plasmaIn VivoNoneNoneGLP-1R EC50 (nmol/L) = 0.088 (for 1907-B)
4048
383994082024
N.A.
BI-XN.A.N.A.N.A.N.A.N.A.N.A.SyntheticTreatment Of Human Ocular Diseaseserial blood samples were taken in EDTA anticoagulant pre-dose and at 1 h, 2 h, 4 h, 24 h, 48 h, 72 h, 96 h, and 168 h and 2, 4, 6, 8, and 10 weeks after dosing or until the last in-life timepoint of the animals.0.25 mg/eye3Cynomolgus Monkeys Plasma ProteaseImmunocapture-LC-MS/MSCynomolgus monkeys plasmaIn VivoNoneNoneAffinity binding site to human albumin (KD = 1.4 nM)
4049
383994082024
N.A.
BI-XN.A.N.A.N.A.N.A.N.A.N.A.SyntheticTreatment Of Human Ocular Diseaseserial blood samples were taken in EDTA anticoagulant pre-dose and at 1 h, 2 h, 4 h, 24 h, 48 h, 72 h, 96 h, and 168 h and 2, 4, 6, 8, and 10 weeks after dosing or until the last in-life timepoint of the animals.0.25 mg/eye13.2Cynomolgus Monkeys Plasma ProteaseImmunocapture-LC-MS/MSCynomolgus monkeys plasmaIn VivoNoneNoneAffinity binding site to human albumin (KD = 1.4 nM)
4050
383994082024
N.A.
BI-XN.A.N.A.N.A.N.A.N.A.N.A.SyntheticTreatment Of Human Ocular Diseaseserial blood samples were taken in EDTA anticoagulant pre-dose and at 1 h, 2 h, 4 h, 24 h, 48 h, 72 h, 96 h, and 168 h and 2, 4, 6, 8, and 10 weeks after dosing or until the last in-life timepoint of the animals.0.25 mg/eye11.8Cynomolgus Monkeys Plasma ProteaseImmunocapture-LC-MS/MSCynomolgus monkeys plasmaIn VivoNoneNoneAffinity binding site to human albumin (KD = 1.4 nM)
4051
383563172024
Y-Aib-EGTFTSDYSI-Aib-LDKIAQKAFVQWLIAGGPSSGAPPPS
Tirzepatide39FreeAmidationLinearLC20 fatty diacid moiety conjugated with Lys20, Aib modification at position 2,13GLP-1 analogsAntidiabetesPK samples were collected after single and multiple doses, up to 109 weeks of continuous tirzepatide treatment2–500 ng/mL.5.4Human plasma proteaseLC-MSHuman plasmaIn VivoNoneNoneN.A.
4052
383407262024
IEEQAKTFLDKFNHEAEDLFYQSSLGGSKGDFRGGGGSGGGGSGGGGSGGGGSGGGGSGGGGSGGGGSDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQ
A1L35HR2m114Conjugation of angiotensin-converting enzyme 2 (ACE2)-derived peptide A1 to the N terminus of the viral HR2-derived peptide HR2m through a long flexible linker,FreeLinearLNonefusion protein of A1 and HR2mAntiviral (Inhibits Coronaviruses)Sera were collected from these mice before (0 h) and 2, 4, 8, 12, 24, 48, 72, 120, 168, 240 and 336 h after injection5 mg/kg2.64Balb/c mice serum proteaseN.A.BALB/c mice serumIn VivoNoneNoneA1L35HR2m was highly potent in inhibiting SARS-CoV-2 infection with an IC50 value of 27 nM
4053
383407262024
IEEQAKTFLDKFNHEAEDLFYQSSLGGSKGDFRGGGGSGGGGSGGGGSGGGGSGGGGSGGGGSGGGGSDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQ
A1L35HR2m-Chol114Conjugation of angiotensin-converting enzyme 2 (ACE2)-derived peptide A1 to the N terminus of the viral HR2-derived peptide HR2m through a long flexible linker,Chol conjugation at C terminalLinearLNonefusion protein of A1 and HR2mAntiviral (Inhibits Coronaviruses)Sera were collected from these mice before (0 h) and 2, 4, 8, 12, 24, 48, 72, 120, 168, 240 and 336 h after injection5 mg/kg81.83Balb/c mice serum proteaseN.A.BALB/c mice serumIn VivoNoneNoneA1L35HR2m was highly potent in inhibiting SARS-CoV-2 infection with an IC50 value of 27 nM
4054
383407262024
IEEQAKTFLDKFNHEAEDLFYQSSLGGSKGDFRGGGGSGGGGSGGGGSGGGGSGGGGSGGGGSGGGGSDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQ
A1L35HR2m-Chol114Conjugation of angiotensin-converting enzyme 2 (ACE2)-derived peptide A1 to the N terminus of the viral HR2-derived peptide HR2m through a long flexible linker,Chol conjugation at C terminalLinearLNonefusion protein of A1 and HR2mAntiviral (Inhibits Coronaviruses)N.A.5 mg/kg89.8Balb/c mice serum proteaseN.A.Balb/c mice lung tissue homogenate In VivoNoneNoneA1L35HR2m was highly potent in inhibiting SARS-CoV-2 infection with an IC50 value of 27 nM
4055
383407262024
IEEQAKTFLDKFNHEAEDLFYQSSLGGSKGDFRGGGGSGGGGSGGGGSGGGGSGGGGSGGGGSGGGGSDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQ
A1L35HR2m-Chol114Conjugation of angiotensin-converting enzyme 2 (ACE2)-derived peptide A1 to the N terminus of the viral HR2-derived peptide HR2m through a long flexible linker,Chol conjugation at C terminalLinearLNonefusion protein of A1 and HR2mAntiviral (Inhibits Coronaviruses)N.A.5 mg/kg10.6Balb/c mice serum proteaseN.A.Balb/c mice trachea tissue homogenate In VivoNoneNoneA1L35HR2m was highly potent in inhibiting SARS-CoV-2 infection with an IC50 value of 27 nM
4056
383407262024
IEEQAKTFLDKFNHEAEDLFYQSSLGGSKGDFRGGGGSGGGGSGGGGSGGGGSGGGGSGGGGSGGGGSDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQ
A1L35HR2m-Chol114Conjugation of angiotensin-converting enzyme 2 (ACE2)-derived peptide A1 to the N terminus of the viral HR2-derived peptide HR2m through a long flexible linker,Chol conjugation at C terminalLinearLNonefusion protein of A1 and HR2mAntiviral (Inhibits Coronaviruses)N.A.5 mg/kg49Balb/c mice serum proteaseN.A.Balb/c mice nose tissue homogenate In VivoNoneNoneA1L35HR2m was highly potent in inhibiting SARS-CoV-2 infection with an IC50 value of 27 nM
4057
383120522024
KXCRGDCFCX
Maraciclatide (99mTc)7AcetylationFreeCyclic(Ac-Cys8 Bond, Cys2-Cys6 Disulfide Bond)LRadiolabelled with technetium, X= Unknown Structure syntheticNovel Diagnostic Imaging Agent For A Range Of Pathological ConditionsBlood and plasma samples were collected at 10 min, 30 min, 1 h, 2 h, 4 h, 8 h, 24 h, 48 h, 72 h, and 7 days post-administrationThe data acquired from all participants who received 99mTc-maraciclatide within the expected clinical range (15, 75 µg, 150) were pooled1 (Terminal Elimination Half Life)Human Plasma ProteaseGamma counterHuman plasmaIn Vivohttps://pubchem.ncbi.nlm.nih.gov/compound/73050806NoneN.A.
4058
382935402024
ENLYFQHGEGTFTSDVSSYLEGQAAKEFIAWLVKGRGGGGSGGGGSGGGGSLAEAKVLANRELDKYGVSDYYKNLINNAKTVEGVKALIDEILAALPGGGGSGGGGSGGGGSHSQGTFTSDYSKYLDSRRAQDFVQWLMNTGGEGGSEGSEGEGSEGSGEGEGGSEGSEGEGSEGSGEGEGGSEGSEGEGGSEGSEGEGGEGSGEGEGSEGSGEGEGSGEGSEGEGGSEGGEGEGSEGGSEGEGSEGGSEGEGGEGSGEGEGGGEGSEGEGSEGSGEGEGSGEGSEG
GLP-ABD-XTEN144257GLP-1 molecule was linked to the N-terminus of ABD via a (GGGGS)3 linker (GLP-ABD), His-tagABD was connected to the N-terminus of the XTEN polypeptide (144 amino acids) through a (GGGGS)3 linkerLinearLNoneFusion protein of GLP-1, ABD, XTEN (either 144 or 288)Antidiabetes, AntiobesityAt 1, 3, 7, 12, 18, 24, 30, 36 h, approximately 30 μL of blood was drawn from the tail vein5 nmol12.9C57Bl/6 mice plasma protease And DPP-4ELISAC57BL/6 mice plasmaIn VivoNoneNoneGLP-ABD-XTEN144 has a Kd value of only 5.50 nM
4059
382935402024
ENLYFQHGEGTFTSDVSSYLEGQAAKEFIAWLVKGRGGGGSGGGGSGGGGSLAEAKVLANRELDKYGVSDYYKNLINNAKTVEGVKALIDEILAALPGGGGSGGGGSGGGGSHSQGTFTSDYSKYLDSRRAQDFVQWLMNTGGEGSGEGSEGEGSEGSGEGEGSEGSGEGEGGSEGSEGEGGSEGSEGEGGSEGSEGEGSGEGSEGEGGSEGSEGEGSGEGSEGEGSEGGSEGEGGSEGSEGEGSGEGSEGEGGEGGSEGEGSEGSGEGEGSGEGSEGEGSEGSGEGEGSGEGSEGEGSEGSGEGEGSEGSGEGEGGSEGSEGEGSEGSGEGEGGEGSGEGEGSGEGSEGEGGGEGSEGEGSGEGGEGEGSEGGSEGEGGSEGGEGEGSEGSGEGEGSEGGSEGEGSEGGSEGEGSEGSGEGEGSEGSGEG
GLP-ABD-XTEN288401GLP-1 molecule was linked to the N-terminus of ABD via a (GGGGS)3 linker (GLP-ABD), His-tagABD was connected to the N-terminus of the XTEN polypeptide (288 amino acids) through a (GGGGS)3 linkerLinearLNoneFusion protein of GLP-1, ABD, XTEN (either 144 or 288)Antidiabetes, AntiobesityAt 1, 3, 7, 12, 18, 24, 30, 36 h, approximately 30 μL of blood was drawn from the tail vein5 nmol7.32C57Bl/6 mice plasma protease And DPP-4ELISAC57BL/6 mice plasmaIn VivoNoneNoneGLP-ABD-XTEN288 showed a Kd value of 27.78 nM
4060
382365612024
HQGTFTSDKSEYLDSERARDFVAWLEAGG
Cotadutide29FreeFreeLinearLpalm-Glu-OH conjugated at Lys9 side chainSyntheticDual GLP-1 and Glucagon (GCG) Receptor agonist N.A.20 to 600 μg13.3N.A.N.A.N.A.In VivoNoneNoneN.A.
4061
381049072024
Y-(d-Dab)-RFFwKTF
[Al18F]NODA-MPAA-HTA8Conjugating 18F nuclide with a modified KE108 peptide, MPAA modification at N terminalThe amino group of KE108 peptide conjugated with the carboxyl group of NODACyclic(d-Dab2-Phe8)MixD-Tryp amino acid substituition, d-Dab = Diaminobutyric acid18F-radiolabeled somatostatin analogueUsed for PET imaging of Neuroendocrine tumors (NETs)Blood samples were collected from the retroorbital plexus into capillary at 5, 10, 15, 30,60 and 120 minN.A.37.63 ± 13.05 (Elimination Half Life)BALB/c mice blood proteaseGamma counterBALB/c mice blood sampleIn VivoNoneNoneAffinity of [Al18F]NODA-MPAA-HTA (Kd = 8.77 ± 1.14 nM, n = 4) 
4062
380069442024
CGKGGGGGIEGPTLRQWLAARAGGGGGGGGIEGPTLRQWLAARA
Fatty Acid Modified TMP108FreeFreeLinearLC41H70O15N4 fatty acid modificationTMP analogueTreatment of ThrombocytopeniaN.A.100 μg/kg128.5Beagle dogs plasma proteaseELISABeagle dogs plasmaIn VivoNoneNoneThe modified TMPs, particularly the C41H70O15N4 group, showed enhanced and prolonged activity, reaching peak platelet counts of 5047 × 10⁹/L at 216 hours (enhanced platelet counts)
4063
378185892024
RCLPAGKPCAGVTQKIPCCGKCSRNKCT
ΔTRTX-Ac128FreeFreeCyclic (C2-C9-C18-C19-C22-C27 form LCK Loop)LNoneFrom venom of the Mexican Blond tarantula spider Aphonopelma chalcodesAntidiabetesBlood withdrawn by cardiac puncture at0, 2, 4, 6, 8 and 12 h post-administration10 mg/kg2.17C57Bl/6 Male Mice Plasma ProteaseMass spectrometryC57BL/6 male mice plasmaIn Vivohttps://dom-pubs.pericles-prod.literatumonline.com/doi/10.1111/dom.15319NoneThe activity value of ΔTRTX-Ac1 alone shows minimal influence on reducing circulating glucose levels, with glucose levels remaining at 23.7 ± 3.1 mmol/L in high-fat-fed/streptozotocin (HFF/STZ) mice
4064
378185892024
RCLPAGKPCAGVTQKIPCCGKCSRNKCT
ΔTRTX-Ac128FreeFreeCyclic (C2-C9-C18-C19-C22-C27 form LCK Loop)LNoneFrom venom of the Mexican Blond tarantula spider Aphonopelma chalcodesAntidiabetesBlood withdrawn by cardiac puncture at 0, 2, 4, 6, 8 and 12 h post-administration10 mg/kg2.16C57Bl/6 Male Mice Pancreas ProteaseMass spectrometryC57BL/6 male mice pancreas In Vivohttps://dom-pubs.pericles-prod.literatumonline.com/doi/10.1111/dom.15319NoneThe activity value of ΔTRTX-Ac1 alone shows minimal influence on reducing circulating glucose levels, with glucose levels remaining at 23.7 ± 3.1 mmol/L in high-fat-fed/streptozotocin (HFF/STZ) mice
4065
N.A.2024
Y-Aib-EGT-aMeF-TSD-4Pal-SI-aMeL-LDOKAQ-Aib-EFIq-aMeY-LIEGGPSSGAPPPS
Compound 143FreeAmidationLinearMixAib2, aMeF(2F)6, 4PallO, aMeL13, Ornl6, K17, Aib20, D-Glu24 aMeY25, and Ser39 substituitions, Lys17 linked with chemical group ((2-[2-(2-Amino-ethoxy)-ethoxy]-acetyl)2-(y-Glu)-CO-(CH2)16-CO2H)Incretin AnalogAntidiabetesBlood sample collected over 36 Hours4.06 nmol/kg68Dogs plasma proteaseLC-MSDogs plasmaIn VivoNoneUS 2023/0072968 WN.A.
4066
N.A.2024
Y-Aib-EGT-aMeF-TSD-4Pal-SI-aMeL-LDOKAQ-Aib-EFIq-aMeY-LIEGGPSSGAPPPS
Compound 143FreeAmidationLinearMixAib2, aMeF(2F)6, 4PallO, aMeL13, Ornl6, K17, Aib20, D-Glu24 aMeY25, and Ser39 substituitions, Lys17 linked with chemical group ((2-[2-(2-Amino-ethoxy)-ethoxy]-acetyl)2-(y-Glu)-CO-(CH2)16-CO2H)Incretin AnalogAntidiabetesBlood sample collected over 168 Hours386.4 nmol/kg64Dogs plasma proteaseLC-MSDogs plasmaIn VivoNoneUS 2023/0072968 WN.A.
4067
N.A.2024
Y-Aib-EGT-aMeF-TSD-4Pal-SI-aMeL-LDOKAQ-Aib-EFIq-aMeY-LIEGGPSSGAPPPS
Compound 143FreeAmidationLinearMixAib2, aMeF(2F)6, 4PallO, aMeL13, Ornl6, K17, Aib20, D-Glu24 aMeY25, and Ser39 substituitions, Lys17 linked with chemical group ((2-[2-(2-Amino-ethoxy)-ethoxy]-acetyl)2-(y-Glu)-CO-(CH2)16-CO2H)Incretin AnalogAntidiabetesBlood sample collected over 168 Hours350.4 nmol/kg77Dogs plasma proteaseLC-MSDogs plasmaIn VivoNoneUS 2023/0072968 WN.A.
4068
N.A.2024
Y-Aib-EGT-aMeF-TSD-4Pal-SI-aMeL-LDOKAQ-Aib-EFIq-aMeY-LIEGGPSSGAPPPS
Compound 143FreeAmidationLinearMixAib2, aMeF(2F)6, 4PallO, aMeL13, Ornl6, K17, Aib20, D-Glu24 aMeY25, and Ser39 substituitions, Lys17 linked with chemical group ((2-[2-(2-Amino-ethoxy)-ethoxy]-acetyl)2-(y-Glu)-CO-(CH2)16-CO2H)Incretin AnalogAntidiabetesBlood sample collected over 168 Hours352.5 nmol/kg76Dogs plasma proteaseLC-MSDogs plasmaIn VivoNoneUS 2023/0072968 WN.A.
4069
N.A.2024
Y-Aib-EGT-aMeF-TSD-4Pal-SI-aMeL-LDOKAQ-Aib-EFIq-aMeY-LIEGGPSSGAPPPS
Compound 143FreeAmidationLinearMixAib2, aMeF(2F)6, 4PallO, aMeL13, Ornl6, K17, Aib20, D-Glu24 aMeY25, and Ser39 substituitions, Lys17 linked with chemical group ((2-[2-(2-Amino-ethoxy)-ethoxy]-acetyl)2-(y-Glu)-CO-(CH2)16-CO2H)Incretin AnalogAntidiabetesBlood sample collected over 168 Hours375.7 nmol/kg46Dogs plasma proteaseLC-MSDogs plasma after food is provided 1 min post doseIn VivoNoneUS 2023/0072968 WN.A.
4070
N.A.2024
Y-Aib-EGT-aMeF-TSD-4Pal-SI-aMeL-LDOKAQ-Aib-EFIq-aMeY-LIEGGPSSGAPPPS
Compound 143FreeAmidationLinearMixAib2, aMeF(2F)6, 4PallO, aMeL13, Ornl6, K17, Aib20, D-Glu24 aMeY25, and Ser39 substituitions, Lys17 linked with chemical group ((2-[2-(2-Amino-ethoxy)-ethoxy]-acetyl)2-(y-Glu)-CO-(CH2)16-CO2H)Incretin AnalogAntidiabetesBlood sample collected over 168 Hours377.1 nmol/kg55Dogs plasma proteaseLC-MSDogs plasma after food is provided 30 min post doseIn VivoNoneUS 2023/0072968 WN.A.
4071
N.A.2024
Y-Aib-EGT-aMeF-TSDYSI-aMeL-LDOKAQ-Aib-EFIqYLIEGGPSSGAPPPS
Compound 240FreeAmidationLinearMixAib2, aMeF(2F)6, aMeL13, Ornl6, K17, Aib20, D-Glu24, and Ser39 substituitions, Lys17 linked with chemical group ((2-[2-(2-Amino-ethoxy)-ethoxy]-acetyl)2-(y-Glu)-CO-(CH2)16-CO2H)Incretin AnalogAntidiabetesBlood sample collected over 336 Hours4.06 nmol/kg105Dogs plasma proteaseLC-MSDogs plasma after food is provided 30 min post doseIn VivoNoneUS 2023/0072968 WN.A.
4072
N.A.2024
Y-Aib-EGT-aMeF-TSDYSI-aMeL-LDOKAQ-Aib-EFIqYLIEGGPSSGAPPPS
Compound 240FreeAmidationLinearMixAib2, aMeF(2F)6, aMeL13, Ornl6, K17, Aib20, D-Glu24, and Ser39 substituitions, Lys17 linked with chemical group ((2-[2-(2-Amino-ethoxy)-ethoxy]-acetyl)2-(y-Glu)-CO-(CH2)16-CO2H)Incretin AnalogAntidiabetesBlood sample collected over 168 Hours389 nmol/kg96Dogs plasma proteaseLC-MSDogs plasma after treatment with Sodium Caprate (C10, 280Mg)In VivoNoneUS 2023/0072968 WN.A.
4073
N.A.2024
Y-Aib-EGTFTSDYSI-Aib-LDKIAQKA-Nal-VQWLIAGGPSSGAPPPS
Compound 340FreeAmidationLinearLAib2, Aibl3 and 1-Nal22 substituitions, Lys20 linked with chemical group ((2-[2-(2-Amino-ethoxy)-ethoxy]-acetyl)2-(y-Glu)-CO-(CH2)18-CO2H)Incretin AnalogAntidiabetesBlood sample collected over 336 Hours4.01 nmol/kg104Dogs plasma proteaseLC-MSDogs plasmaIn VivoNoneUS 2023/0072968 WN.A.
4074
N.A.2024
Y-Aib-EGTFTSDYSI-Aib-LDKIAQKA-Nal-VQWLIAGGPSSGAPPPS
Compound 340FreeAmidationLinearLAib2, Aibl3 and 1-Nal22 substituitions, Lys20 linked with chemical group ((2-[2-(2-Amino-ethoxy)-ethoxy]-acetyl)2-(y-Glu)-CO-(CH2)18-CO2H)Incretin AnalogAntidiabetesBlood sample collected over 336 Hours20 mg111Dogs plasma proteaseLC-MSDogs plasmaIn VivoNoneUS 2023/0072968 WN.A.
4075
N.A.2024
Y-Aib-EGTFTSDYSI-Aib-LDKIAQKA-Nal-VQWLIAGGPSSGAPPPS
Compound 340FreeAmidationLinearLAib2, Aibl3 and 1-Nal22 substituitions, Lys20 linked with chemical group ((2-[2-(2-Amino-ethoxy)-ethoxy]-acetyl)2-(y-Glu)-CO-(CH2)18-CO2H)Incretin AnalogAntidiabetesBlood sample collected over 336 Hours20 mg104Dogs plasma proteaseLC-MSDogs plasmaIn VivoNoneUS 2023/0072968 WN.A.
4076
N.A.2024
Y-Aib-EGTFTSDYSI-Aib-LDKIAQKAFVQWLIAGGPSSGAPPPS
TZP40FreeAmidationLinearLAib2, Aibl3 substituitions, Lys20 linked with chemical group ((2-[2-(2-Amino-ethoxy)-ethoxy]-acetyl)2-(y-Glu)1-CO-(CH2)18-CO2H)Incretin AnalogAntidiabetesBlood sample collected over 336 Hours4.15 nmol/kg70Dogs plasma proteaseLC-MSDogs plasmaIn VivoNoneUS 2023/0072968 WN.A.
4077
N.A.2024
Y-Aib-EGTFTSDYSI-Aib-LDKIAQKAFVQWLIAGGPSSGAPPPS
TZP40FreeAmidationLinearLAib2, Aibl3 substituitions, Lys20 linked with chemical group ((2-[2-(2-Amino-ethoxy)-ethoxy]-acetyl)2-(y-Glu)1-CO-(CH2)18-CO2H)Incretin AnalogAntidiabetesBlood sample collected over 336 Hours4.15 nmol/kg159Dogs plasma proteaseLC-MSDogs plasmaIn VivoNoneUS 2023/0072968 WN.A.
4078
N.A.2024
Y-Aib-EGTFTSDYSI-Aib-LDKIAQKAFVQWLIAGGPSSGAPPPS
TZP40FreeAmidationLinearLAib2, Aibl3 substituitions, Lys20 linked with chemical group ((2-[2-(2-Amino-ethoxy)-ethoxy]-acetyl)2-(y-Glu)1-CO-(CH2)18-CO2H)Incretin AnalogAntidiabetesBlood sample collected over 336 Hours20 mg97Dogs plasma proteaseLC-MSDogs plasmaIn VivoNoneUS 2023/0072968 WN.A.
4079
N.A.2024
AMVSEFLKQAWFIENEEQEYVQTLKSSKGGPGSAVSPYPTFNPSSDV
Peptide 147FreeAmidationLinearLV24L modificationsAnnexin A1 DerivativeAntiinflammatoryBlood sample were collected at 2,5,10,20,40,60 Minutes After Dosing And For Animals Receiving 10 Mg/Kg, Additional Samples Were Taken At 90 And 120 Minutes After Dosing0.1 mg/kg3.49 (Initial Elimination Phase)Male wistar rats plasma proteaseLC-MS/MSMale wistar rat plasmaIn VivoNoneEP 2023067975 WN.A.
4080
N.A.2024
AMVSEFLKQAWFIENEEQEYVQTLKSSKGGPGSAVSPYPTFNPSSDV
Peptide 147FreeAmidationLinearLV24L modificationsAnnexin A1 DerivativeAntiinflammatoryBlood sample were collected at 2,5,10,20,40,60 Minutes After Dosing And For Animals Receiving 10 Mg/Kg, Additional Samples Were Taken At 90 And 120 Minutes After Dosing1 mg/kg3.34 (Initial Elimination Phase)Male wistar rats plasma proteaseLC-MS/MSMale wistar rat plasmaIn VivoNoneEP 2023067975 WN.A.
4081
N.A.2024
AMVSEFLKQAWFIENEEQEYVQTLKSSKGGPGSAVSPYPTFNPSSDV
Peptide 147FreeAmidationLinearLV24L modificationsAnnexin A1 DerivativeAntiinflammatoryBlood sample were collected at 2,5,10,20,40,60 Minutes After Dosing And For Animals Receiving 10 Mg/Kg, Additional Samples Were Taken At 90 And 120 Minutes After Dosing10 mg/kg7.64 (Initial Elimination Phase)Male wistar rats plasma proteaseLC-MS/MSMale wistar rat plasmaIn VivoNoneEP 2023067975 WN.A.
4082
N.A.2024
AMVSEFLKQAWFIENEEQEYVQTLKSSKGGPGSAVSPYPTFNPSSDV
Peptide 147FreeAmidationLinearLV24L modificationsAnnexin A1 DerivativeAntiinflammatoryBlood sample were collected at 2,5,10,20,40,60 Minutes After Dosing And For Animals Receiving 10 Mg/Kg, Additional Samples Were Taken At 90 And 120 Minutes After Dosing0.1 mg/kg18.8 (Terminal Elimination Phase)Male wistar rats plasma proteaseLC-MS/MSMale wistar rat plasmaIn VivoNoneEP 2023067975 WN.A.
4083
N.A.2024
AMVSEFLKQAWFIENEEQEYVQTLKSSKGGPGSAVSPYPTFNPSSDV
Peptide 147FreeAmidationLinearLV24L modificationsAnnexin A1 DerivativeAntiinflammatoryBlood sample were collected at 2,5,10,20,40,60 Minutes After Dosing And For Animals Receiving 10 Mg/Kg, Additional Samples Were Taken At 90 And 120 Minutes After Dosing1 mg/kg10 (Terminal Elimination Phase)Male wistar rats plasma proteaseLC-MS/MSMale wistar rat plasmaIn VivoNoneEP 2023067975 WN.A.
4084
N.A.2024
AMVSEFLKQAWFIENEEQEYVQTLKSSKGGPGSAVSPYPTFNPSSDV
Peptide 147FreeAmidationLinearLV24L modificationsAnnexin A1 DerivativeAntiinflammatoryBlood sample were collected at 2,5,10,20,40,60 Minutes After Dosing And For Animals Receiving 10 Mg/Kg, Additional Samples Were Taken At 90 And 120 Minutes After Dosing10 mg/kg10.2 (Terminal Elimination Phase)Male wistar rats plasma proteaseLC-MS/MSMale wistar rat plasmaIn VivoNoneEP 2023067975 WN.A.
4085
N.A.2024
AMVSEFLKQAWFIENEEQEYVQTLKSSKGGPGSAVSPYPTFNPSSDV
Peptide 147FreeAmidationLinearLV24L modificationsAnnexin A1 DerivativeAntiinflammatorySamples were collected at 2,5,10,20,40 Minutes After Dosing On Days 1 Or 141 mg/kg8.4 (Elimination Half Life)Male wistar rats plasma proteaseLC-MS/MSMale wistar rats plasma after day 1 repeated doseIn VivoNoneEP 2023067975 WN.A.
4086
N.A.2024
AMVSEFLKQAWFIENEEQEYVQTLKSSKGGPGSAVSPYPTFNPSSDV
Peptide 147FreeAmidationLinearLV24L modificationsAnnexin A1 DerivativeAntiinflammatorySamples were collected at 2,5,10,20,40 Minutes After Dosing On Days 1 Or 141 mg/kg7.33 (Elimination Half Life)Female wistar rats plasma proteaseLC-MS/MSFemale wistar rats plasma after day 1 repeated doseIn VivoNoneEP 2023067975 WN.A.
4087
N.A.2024
AMVSEFLKQAWFIENEEQEYVQTLKSSKGGPGSAVSPYPTFNPSSDV
Peptide 147FreeAmidationLinearLV24L modificationsAnnexin A1 DerivativeAntiinflammatorySamples were collected at 2,5,10,20,40 Minutes After Dosing On Days 1 Or 141 mg/kg7.66 (Elimination Half Life)Male wistar rats plasma proteaseLC-MS/MSMale wistar rats plasma after day 14 repeated doseIn VivoNoneEP 2023067975 WN.A.
4088
N.A.2024
AMVSEFLKQAWFIENEEQEYVQTLKSSKGGPGSAVSPYPTFNPSSDV
Peptide 147FreeAmidationLinearLV24L modificationsAnnexin A1 DerivativeAntiinflammatorySamples were collected at 2,5,10,20,40 Minutes After Dosing On Days 1 Or 141 mg/kg7.11 (Elimination Half Life)Female wistar rats plasma proteaseLC-MS/MSFemale wistar rats plasma after day 14 repeated doseIn VivoNoneEP 2023067975 WN.A.
4089
N.A.2024
AMVSEFLKQAWFIENEEQEYVQTLKSSKGGPGSAVSPYPTFNPSSDV
Peptide 147FreeAmidationLinearLV24L modificationsAnnexin A1 DerivativeAntiinflammatorySamples were collected at 2,5,10,20,40 Minutes After Dosing On Days 1 Or 143 mg/kg7 (Elimination Half Life)Male wistar rats plasma proteaseLC-MS/MSMale wistar rats plasma after day 1 repeated doseIn VivoNoneEP 2023067975 WN.A.
4090
N.A.2024
AMVSEFLKQAWFIENEEQEYVQTLKSSKGGPGSAVSPYPTFNPSSDV
Peptide 147FreeAmidationLinearLV24L modificationsAnnexin A1 DerivativeAntiinflammatorySamples were collected at 2,5,10,20,40 Minutes After Dosing On Days 1 Or 143 mg/kg8 (Elimination Half Life)Female wistar rats plasma proteaseLC-MS/MSFemale wistar rats plasma after day 1 repeated doseIn VivoNoneEP 2023067975 WN.A.
4091
N.A.2024
AMVSEFLKQAWFIENEEQEYVQTLKSSKGGPGSAVSPYPTFNPSSDV
Peptide 147FreeAmidationLinearLV24L modificationsAnnexin A1 DerivativeAntiinflammatorySamples were collected at 2,5,10,20,40 Minutes After Dosing On Days 1 Or 143 mg/kg6.67 (Elimination Half Life)Male wistar rats plasma proteaseLC-MS/MSMale wistar rats plasma after Day 14 Repeated DoseIn VivoNoneEP 2023067975 WN.A.
4092
N.A.2024
AMVSEFLKQAWFIENEEQEYVQTLKSSKGGPGSAVSPYPTFNPSSDV
Peptide 147FreeAmidationLinearLV24L modificationsAnnexin A1 DerivativeAntiinflammatorySamples were collected at 2,5,10,20,40 Minutes After Dosing On Days 1 Or 143 mg/kg6.85 (Elimination Half Life)Female wistar rats plasma proteaseLC-MS/MSFemale wistar rats plasma After Day 14 Repeated DoseIn VivoNoneEP 2023067975 WN.A.
4093
N.A.2024
AMVSEFLKQAWFIENEEQEYVQTLKSSKGGPGSAVSPYPTFNPSSDV
Peptide 147FreeAmidationLinearLV24L modificationsAnnexin A1 DerivativeAntiinflammatorySamples Were Collected At 2,5,10,20,40 Minutes After Dosing On Days 1 Or 1410 mg/kg7.8 (Elimination Half Life)Male wistar rats plasma proteaseLC-MS/MSMale wistar rats plasma After Day 1 Repeated DoseIn VivoNoneEP 2023067975 WN.A.
4094
N.A.2024
AMVSEFLKQAWFIENEEQEYVQTLKSSKGGPGSAVSPYPTFNPSSDV
Peptide 147FreeAmidationLinearLV24L modificationsAnnexin A1 DerivativeAntiinflammatorySamples Were Collected At 2,5,10,20,40 Minutes After Dosing On Days 1 Or 1410 mg/kg7.16 (Elimination Half Life)Female wistar rats plasma proteaseLC-MS/MSFemale wistar rats plasma After Day 1 Repeated DoseIn VivoNoneEP 2023067975 WN.A.
4095
N.A.2024
AMVSEFLKQAWFIENEEQEYVQTLKSSKGGPGSAVSPYPTFNPSSDV
Peptide 147FreeAmidationLinearLV24L modificationsAnnexin A1 DerivativeAntiinflammatorySamples Were Collected At 2,5,10,20,40 Minutes After Dosing On Days 1 Or 1410 mg/kg7.31 (Elimination Half Life)Male wistar rats plasma proteaseLC-MS/MSMale wistar rats plasma After Day 14 Repeated DoseIn VivoNoneEP 2023067975 WN.A.
4096
N.A.2024
AMVSEFLKQAWFIENEEQEYVQTLKSSKGGPGSAVSPYPTFNPSSDV
Peptide 147FreeAmidationLinearLV24L modificationsAnnexin A1 DerivativeAntiinflammatorySamples Were Collected At 2,5,10,20,40 Minutes After Dosing On Days 1 Or 1410 mg/kg7.04 (Elimination Half Life)Female wistar rats plasma proteaseLC-MS/MSFemale wistar rats plasma After Day 14 Repeated DoseIn VivoNoneEP 2023067975 WN.A.
4097
N.A.2024
AMVSEFLKQAWFIENEEQEYVQTLKSSKGGPGSAVSPYPTFNPSSDV
Peptide 147FreeAmidationLinearLV24L modificationsAnnexin A1 DerivativeAntiinflammatorySamples Were Collected At 2,5,10,20,40 Minutes After Dosing On Days 1 Or 141 mg/kg4.68 (Elimination Half Life)Male dogs plasma proteaseLC-MS/MSMale dogs plasma After Day 1 Repeated DoseIn VivoNoneEP 2023067975 WN.A.
4098
N.A.2024
AMVSEFLKQAWFIENEEQEYVQTLKSSKGGPGSAVSPYPTFNPSSDV
Peptide 147FreeAmidationLinearLV24L modificationsAnnexin A1 DerivativeAntiinflammatorySamples Were Collected At 2,5,10,20,40 Minutes After Dosing On Days 1 Or 141 mg/kg4.83 (Elimination Half Life)Female dogs plasma proteaseLC-MS/MSFemale dogs plasma After Day 1 Repeated DoseIn VivoNoneEP 2023067975 WN.A.
4099
N.A.2024
AMVSEFLKQAWFIENEEQEYVQTLKSSKGGPGSAVSPYPTFNPSSDV
Peptide 147FreeAmidationLinearLV24L modificationsAnnexin A1 DerivativeAntiinflammatorySamples Were Collected At 2,5,10,20,40 Minutes After Dosing On Days 1 Or 141 mg/kg6.59 (Elimination Half Life)Male dogs plasma proteaseLC-MS/MSMale dogs plasma After Day 1 Repeated DoseIn VivoNoneEP 2023067975 WN.A.
4100
N.A.2024
AMVSEFLKQAWFIENEEQEYVQTLKSSKGGPGSAVSPYPTFNPSSDV
Peptide 147FreeAmidationLinearLV24L modificationsAnnexin A1 DerivativeAntiinflammatorySamples Were Collected At 2,5,10,20,40 Minutes After Dosing On Days 1 Or 141 mg/kg4.66 (Elimination Half Life)Female dogs plasma proteaseLC-MS/MSFemale dogs plasma After Day 1 Repeated DoseIn VivoNoneEP 2023067975 WN.A.
4101
N.A.2024
AMVSEFLKQAWFIENEEQEYVQTLKSSKGGPGSAVSPYPTFNPSSDV
Peptide 147FreeAmidationLinearLV24L modificationsAnnexin A1 DerivativeAntiinflammatorySamples Were Collected At 2,5,10,20,40 Minutes After Dosing On Days 1 Or 143 mg/kg6.01 (Elimination Half Life)Male dogs plasma proteaseLC-MS/MSMale dogs plasma After Day 1 Repeated DoseIn VivoNoneEP 2023067975 WN.A.
4102
N.A.2024
AMVSEFLKQAWFIENEEQEYVQTLKSSKGGPGSAVSPYPTFNPSSDV
Peptide 147FreeAmidationLinearLV24L modificationsAnnexin A1 DerivativeAntiinflammatorySamples Were Collected At 2,5,10,20,40 Minutes After Dosing On Days 1 Or 143 mg/kg5.7(Elimination Half Life)Female dogs plasma proteaseLC-MS/MSFemale dogs plasma After Day 1 Repeated DoseIn VivoNoneEP 2023067975 WN.A.
4103
N.A.2024
AMVSEFLKQAWFIENEEQEYVQTLKSSKGGPGSAVSPYPTFNPSSDV
Peptide 147FreeAmidationLinearLV24L modificationsAnnexin A1 DerivativeAntiinflammatorySamples Were Collected At 2,5,10,20,40 Minutes After Dosing On Days 1 Or 143 mg/kg6.05 (Elimination Half Life)Male dogs plasma proteaseLC-MS/MSMale dogs plasma After Day 1 Repeated DoseIn VivoNoneEP 2023067975 WN.A.
4104
N.A.2024
AMVSEFLKQAWFIENEEQEYVQTLKSSKGGPGSAVSPYPTFNPSSDV
Peptide 147FreeAmidationLinearLV24L modificationsAnnexin A1 DerivativeAntiinflammatorySamples Were Collected At 2,5,10,20,40 Minutes After Dosing On Days 1 Or 143 mg/kg6.13 (Elimination Half Life)Female dogs plasma proteaseLC-MS/MSFemale dogs plasma After Day 1 Repeated DoseIn VivoNoneEP 2023067975 WN.A.
4105
N.A.2024
AMVSEFLKQAWFIENEEQEYVQTLKSSKGGPGSAVSPYPTFNPSSDV
Peptide 147FreeAmidationLinearLV24L modificationsAnnexin A1 DerivativeAntiinflammatorySamples Were Collected At 2,5,10,20,40 Minutes After Dosing On Days 1 Or 1410 mg/kg5.09 (Elimination Half Life)Male dogs plasma proteaseLC-MS/MSMale dogs plasma After Day 1 Repeated DoseIn VivoNoneEP 2023067975 WN.A.
4106
N.A.2024
AMVSEFLKQAWFIENEEQEYVQTLKSSKGGPGSAVSPYPTFNPSSDV
Peptide 147FreeAmidationLinearLV24L modificationsAnnexin A1 DerivativeAntiinflammatorySamples Were Collected At 2,5,10,20,40 Minutes After Dosing On Days 1 Or 1410 mg/kg5.41 (Elimination Half Life)Female dogs plasma proteaseLC-MS/MSFemale dogs plasma After Day 1 Repeated DoseIn VivoNoneEP 2023067975 WN.A.
4107
N.A.2024
AMVSEFLKQAWFIENEEQEYVQTLKSSKGGPGSAVSPYPTFNPSSDV
Peptide 147FreeAmidationLinearLV24L modificationsAnnexin A1 DerivativeAntiinflammatorySamples Were Collected At 2,5,10,20,40 Minutes After Dosing On Days 1 Or 1410 mg/kg6 (Elimination Half Life)Male dogs plasma proteaseLC-MS/MSMale dogs plasma After Day 1 Repeated DoseIn VivoNoneEP 2023067975 WN.A.
4108
N.A.2024
AMVSEFLKQAWFIENEEQEYVQTLKSSKGGPGSAVSPYPTFNPSSDV
Peptide 147FreeAmidationLinearLV24L modificationsAnnexin A1 DerivativeAntiinflammatorySamples Were Collected At 2,5,10,20,40 Minutes After Dosing On Days 1 Or 1410 mg/kg5.9 (Elimination Half Life)Female dogs plasma proteaseLC-MS/MSFemale dogs plasma After Day 1 Repeated DoseIn VivoNoneEP 2023067975 WN.A.
4109
N.A.2024
AMVSEFLKQAWFIENEEQEYVQTLKSSKGGPGSAVSPYPTFNPSSDV
Peptide 147FreeAmidationLinearLV24L modificationsAnnexin A1 DerivativeAntiinflammatoryBlood Samples Were Collected At The Following Time Points: Pre-Dose, Then, 10 Min,20 Min,30Min,0.75,1,1.5,2,2.5,3,4,6,8,12,16 And 24 H After Infusion Start25 μg/kg0.79 (Elimination Half Life)Human plasma proteaseLC-MS/MSHuman plasmaIn VivoNoneEP 2023067975 WN.A.
4110
N.A.2024
AMVSEFLKQAWFIENEEQEYVQTLKSSKGGPGSAVSPYPTFNPSSDV
Peptide 147FreeAmidationLinearLV24L modificationsAnnexin A1 DerivativeAntiinflammatoryBlood Samples Were Collected At The Following Time Points: Pre-Dose, Then, 10 Min,20 Min,30Min,0.75,1,1.5,2,2.5,3,4,6,8,12,16 And 24 H After Infusion Start50 μg/kg0.92 (Elimination Half Life)Human plasma proteaseLC-MS/MSHuman plasmaIn VivoNoneEP 2023067975 WN.A.
4111
N.A.2024
AMVSEFLKQAWFIENEEQEYVQTLKSSKGGPGSAVSPYPTFNPSSDV
Peptide 147FreeAmidationLinearLV24L modificationsAnnexin A1 DerivativeAntiinflammatoryBlood Samples Were Collected At The Following Time Points: Pre-Dose, Then, 10 Min,20 Min,30Min,0.75,1,1.5,2,2.5,3,4,6,8,12,16 And 24 H After Infusion Start100μg/kg1.15 (Elimination Half Life)Human plasma proteaseLC-MS/MSHuman plasmaIn VivoNoneEP 2023067975 WN.A.
4112
N.A.2024
AMVSEFLKQAWFIENEEQEYVQTLKSSKGGPGSAVSPYPTFNPSSDV
Peptide 147FreeAmidationLinearLV24L modificationsAnnexin A1 DerivativeAntiinflammatoryBlood Samples Were Collected At The Following Time Points: Pre-Dose, Then, 10 Min,20 Min,30Min,0.75,1,1.5,2,2.5,3,4,6,8,12,16 And 24 H After Infusion Start150 μg/kg1.15 (Elimination Half Life)Human plasma proteaseLC-MS/MSHuman plasmaIn VivoNoneEP 2023067975 WN.A.
4113
N.A.2024
AMVSEFLKQAWFIENEEQEYVQTLKSSKGGPGSAVSPYPTFNPSSDV
Peptide 147FreeAmidationLinearLV24L modificationsAnnexin A1 DerivativeAntiinflammatoryBlood Samples Were Collected For Pk Purpose For Peptide 1 Determinations On Day 1 At The Following Time Points: Pre-Dose, Then 10 Min, 20 Min, 30 Min = 0.5, 0.75, 1.0, 1.5, 2.0, 2.5, 3.0, 4.0, 6.0, 8.0, Then 10 Min, 20 Min, 30 Min After The Second Infusion Start, I.E. 8.16, 8.32, 8.5, 8.75, 9.0, 9.5, 10.0, 10.5, 11.0, 12.0, 14.0, 16.0, Then 10 Min, 20 Min, 30 Min After The Second Infusion Start, I.E. 16.16, 16.32, 16.5, 16.75, 17.0, 17.5, 18.0, 18.5, 19.0, 20.0, 22.0 And 24 Hours After The First Infusion Start50 μg/kg1.38 (Elimination Half Life)Human plasma proteaseLC-MS/MSHuman plasma received three 8 hours apart 30-min peptide 1 repeated dose In VivoNoneEP 2023067975 WN.A.
4114
N.A.2024
AMVSEFLKQAWFIENEEQEYVQTLKSSKGGPGSAVSPYPTFNPSSDV
Peptide 147FreeAmidationLinearLV24L modificationsAnnexin A1 DerivativeAntiinflammatoryBlood Samples Were Collected For Pk Purpose For Peptide 1 Determinations On Day 1 At The Following Time Points: Pre-Dose, Then 10 Min, 20 Min, 30 Min = 0.5, 0.75, 1.0, 1.5, 2.0, 2.5, 3.0, 4.0, 6.0, 8.0, Then 10 Min, 20 Min, 30 Min After The Second Infusion Start, I.E. 8.16, 8.32, 8.5, 8.75, 9.0, 9.5, 10.0, 10.5, 11.0, 12.0, 14.0, 16.0, Then 10 Min, 20 Min, 30 Min After The Second Infusion Start, I.E. 16.16, 16.32, 16.5, 16.75, 17.0, 17.5, 18.0, 18.5, 19.0, 20.0, 22.0 And 24 Hours After The First Infusion Start100μg/kg2.18 (Elimination Half Life)Human plasma proteaseLC-MS/MSHuman plasma received three 8 hours apart 30-min peptide 1 repeated dose In VivoNoneEP 2023067975 WN.A.
4115
N.A.2024
AMVSEFLKQAWFIENEEQEYVQTLKSSKGGPGSAVSPYPTFNPSSDV
Peptide 147FreeAmidationLinearLV24L modificationsAnnexin A1 DerivativeAntiinflammatoryBlood Samples Were Collected For Pk Purpose For Peptide 1 Determinations On Day 1 At The Following Time Points: Pre-Dose, Then 10 Min, 20 Min, 30 Min = 0.5, 0.75, 1.0, 1.5, 2.0, 2.5, 3.0, 4.0, 6.0, 8.0, Then 10 Min, 20 Min, 30 Min After The Second Infusion Start, I.E. 8.16, 8.32, 8.5, 8.75, 9.0, 9.5, 10.0, 10.5, 11.0, 12.0, 14.0, 16.0, Then 10 Min, 20 Min, 30 Min After The Second Infusion Start, I.E. 16.16, 16.32, 16.5, 16.75, 17.0, 17.5, 18.0, 18.5, 19.0, 20.0, 22.0 And 24 Hours After The First Infusion Start140 μg/kg1.94 (Elimination Half Life)Human plasma proteaseLC-MS/MSHuman plasma received three 8 hours apart 30-min peptide 1 repeated dose In VivoNoneEP 2023067975 WN.A.
4116
N.A.2024
AMVSEFLKQAWFIENEEQEYVQTLKSSKGGPGSAVSPYPTFNPSSDV
Peptide 147FreeAmidationLinearLV24L modificationsAnnexin A1 DerivativeAntiinflammatoryBlood Samples Were Collected For Pk Purpose For Peptide 1 Determinations On Day 1 At The Following Time Points: Pre-Dose, Then 10 Min, 20 Min, 30 Min = 0.5, 0.75, 1.0, 1.5, 2.0, 2.5, 3.0, 4.0, 6.0, 8.0, Then 10 Min, 20 Min, 30 Min After The Second Infusion Start, I.E. 8.16, 8.32, 8.5, 8.75, 9.0, 9.5, 10.0, 10.5, 11.0, 12.0, 14.0, 16.0, Then 10 Min, 20 Min, 30 Min After The Second Infusion Start, I.E. 16.16, 16.32, 16.5, 16.75, 17.0, 17.5, 18.0, 18.5, 19.0, 20.0, 22.0 And 24 Hours After The First Infusion Start200 μg/kg1.94 (Elimination Half Life)Human plasma proteaseLC-MS/MSHuman plasma received three 8 hours apart 30-min peptide 1 repeated dose In VivoNoneEP 2023067975 WN.A.
4117
N.A.2024
AMVSEFLKQAWFIENEEQEYVQTLKSSKGGPGSAVSPYPTFNPSSDV
Peptide 147FreeAmidationLinearLV24L modificationsAnnexin A1 DerivativeAntiinflammatoryBlood Samples Were Collected For Pk Purpose For Peptide 1 Determinations On Day 1 At The Following Time Points: Pre-Dose, Then 10 Min, 20 Min, 30 Min = 0.5, 0.75, 1.0, 1.5, 2.0, 2.5, 3.0, 4.0, 6.0, 8.0, Then 10 Min, 20 Min, 30 Min After The Second Infusion Start, I.E. 8.16, 8.32, 8.5, 8.75, 9.0, 9.5, 10.0, 10.5, 11.0, 12.0, 14.0, 16.0, Then 10 Min, 20 Min, 30 Min After The Second Infusion Start, I.E. 16.16, 16.32, 16.5, 16.75, 17.0, 17.5, 18.0, 18.5, 19.0, 20.0, 22.0 And 24 Hours After The First Infusion Start250 μg/kg1.88 (Elimination Half Life)Human plasma proteaseLC-MS/MSHuman plasma received three 8 hours apart 30-min peptide 1 repeated dose In VivoNoneEP 2023067975 WN.A.
4118
388636462024
N.A.
(89Zr, Mn)-WPMNsN.A.FreeFreeLinearLMn and 89Zr labeling, MNPs modified with WL12-SH WL12 derivativeTargets PD-L1Blood samples were collected from orbital vein at 1, 3, 5, 10, 15, 20, 30, 45 min and 1, 1.5, 2, 3, 4, 14, 24, 48, 72, 96 h0.5 mg/ml0.1234 (Fast) (Metabolic Half Life)KM mouse blood proteaseRadioactivity assay using γ-counterKM mouse bloodIn VivoNoneNoneN.A.
4119
388636462024
N.A.
(89Zr, Mn)-WPMNsN.A.FreeFreeLinearLMn and 89Zr labeling, MNPs modified with WL12-SH WL12 derivativeTargets PD-L1Blood samples were collected from orbital vein at 1, 3, 5, 10, 15, 20, 30, 45 min and 1, 1.5, 2, 3, 4, 14, 24, 48, 72, 96 h0.5 mg/ml1.554 (Slow) (Distribution Half Life)KM mouse blood proteaseRadioactivity assay using γ-counterKM mouse blood sampleIn VivoNoneNoneN.A.
4120
386974232024
N.A.
DAE Rum55N.A.N.A.N.A.N.A.DN.A.Ruminococcus sp. CAG55 Epimerase50 °CN.A.4.5 (Activity Half Life)N.A.N.A.N.A.In VitroNoneNoneD-allulose/D-psicose 3-epimerase (DAE/DPE, EC 5.1.3.30) and D-tagatose 3-epimerase (DTE, EC 5.1.3.31), of which DAE usually exhibits higher catalytic activity
4121
386974232024
N.A.
E268R-EKL16N.A.N.A.N.A.N.A.N.A.N.A.Ruminococcus sp. CAG55 derivativeEpimerase50 °CN.A.135.3 (Activity Half Life)N.A.N.A.N.A.In VitroNoneNoneD-allulose/D-psicose 3-epimerase (DAE/DPE, EC 5.1.3.30) and D-tagatose 3-epimerase (DTE, EC 5.1.3.31), of which DAE usually exhibits higher catalytic activity
4122
387530952024
N.A.
Xyn10-HBN.A.N.A.N.A.N.A.N.A.N.A.GH10 xylanase from Halalkalibacterium halodurans C-125 GH10 xylanasepH 8.5 and 60 °CN.A.3 (Activity Half Life)N.A.N.A.N.A.In VitroNoneNoneXyn10-HB produced active XOS with antioxidant activity determined by the DPPH radical scavenging method (IC50 of 0.54 mg/mL after 4 h)
4123
381152312024
N.A.
Trx1PN.A.N.A.N.A.LinearLN.A.Derived from E. coli thioredoxin (Trx).N.A.N.A.N.A.124 ± 15 (T1/2 Cis-Trans Isomerizations)N.A.N.A.N.A.N.A.NoneNoneN.A.
4124
381152312024
N.A.
Trx1ThpN.A.N.A.N.A.LinearLIncorporation of 4-thiaproline (Thp) at position cisPro76Derived from E. coli thioredoxin (Trx).N.A.N.A.N.A.33 ± 3 (T1/2 Cis-Trans Isomerizations)N.A.N.A.N.A.N.A.NoneNoneN.A.
4125
378274962024
N.A.
TTRA81V heterozygous508N.A.N.A.LinearLAlanine (Ala) is substituted with valine (Val) at position 81Derived from missense mutation in the TTR geneCauses mild transthyretin amyloid cardiomyopathyN.A.3.6 μM21Urea between 0.5 and 9 M in phosphate buffer (1 mM of EDTA, 10 mM of sodium phosphate, and 100 mM of potassium chloride, pH = 7.4UPLCHuman serumIn VitroNoneNoneN.A.
4126
378274962024
N.A.
TTRA81V homozygous508N.A.N.A.LinearLAlanine (Ala) is substituted with valine (Val) at position 81Derived from missense mutation in the TTR geneCauses mild transthyretin amyloid cardiomyopathyN.A.3.6 μM17.5Urea between 0.5 and 9 M in phosphate buffer (1 mM of EDTA, 10 mM of sodium phosphate, and 100 mM of potassium chloride, pH = 7.4UPLCHuman serumIn VitroNoneNoneN.A.
4127
378274962024
N.A.
TTRWT (wild-type transthyretin)508N.A.N.A.LinearLNoneLiver‐secreted plasma proteinCauses mild transthyretin amyloid cardiomyopathyN.A.3.6 μM44Urea between 0.5 and 9 M in phosphate buffer (1 mM of EDTA, 10 mM of sodium phosphate, and 100 mM of potassium chloride, pH = 7.4UPLCHuman serumIn VitroNoneNoneN.A.
4128
378274962024
N.A.
TTRL55P mutation508N.A.N.A.LinearLleucine (Leu) is substituted with proline (Pro) at position 55Derived from missense mutation in the TTR gene (L55P)Causes mild transthyretin amyloid cardiomyopathyN.A.3.6 μM4.4Urea between 0.5 and 9 M in phosphate buffer (1 mM of EDTA, 10 mM of sodium phosphate, and 100 mM of potassium chloride, pH = 7.4UPLCHuman serumIn VitroNoneNoneN.A.
4129
382883382024
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
Efpeglenatide39N terminal amine group of His replaced by imidazo-acetyl AmidationLinearLConjugate in which LYS27 side chain linked to PEG-Fc Exendin-4 analogsAntidiabetesBlood samples were taken for PK measures pre-dose and at 1, 2, 4, 8, and 12 h post-dose on day 1, and once on days 2, 4, 7, 10, 14, 21, 28, 35, 42, and 494 μg/kg144 (terminal elimination half life)Human serum proteaseSandwich ELISAHuman serumIn Vivohttps://pubmed.ncbi.nlm.nih.gov/32175655/NoneN.A.
4130
382883382024
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
Efpeglenatide39N terminal amine group of His replaced by imidazo-acetyl AmidationLinearLConjugate in which LYS27 side chain linked to PEG-Fc Exendin-4 analogsAntidiabetesBlood samples were taken for PK measures pre-dose and at 1, 2, 4, 8, and 12 h post-dose on day 1, and once on days 2, 4, 7, 10, 14, 21, 28, 35, 42, and 498 μg/kg147 (terminal elimination half life)Human serum proteaseSandwich ELISAHuman serumIn Vivohttps://pubmed.ncbi.nlm.nih.gov/32175655/NoneN.A.
4131
382883382024
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
Efpeglenatide39N terminal amine group of His replaced by imidazo-acetyl AmidationLinearLConjugate in which LYS27 side chain linked to PEG-Fc Exendin-4 analogsAntidiabetesBlood samples were taken for PK measures pre-dose and at 1, 2, 4, 8, and 12 h post-dose on day 1, and once on days 2, 4, 7, 10, 14, 21, 28, 35, 42, and 4914 μg/kg135 (terminal elimination half life)Human serum proteaseSandwich ELISAHuman serumIn Vivohttps://pubmed.ncbi.nlm.nih.gov/32175655/NoneN.A.
4132
382883382024
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
Efpeglenatide39N terminal amine group of His replaced by imidazo-acetyl AmidationLinearLConjugate in which LYS27 side chain linked to PEG-Fc Exendin-4 analogsAntidiabetesBlood samples were taken for PK measures pre-dose and at 1, 2, 4, 8, and 12 h post-dose on day 1, and once on days 2, 4, 7, 10, 14, 21, 28, 35, 42, and 4920 μg/kg147 (terminal elimination half life)Human serum proteaseSandwich ELISAHuman serumIn Vivohttps://pubmed.ncbi.nlm.nih.gov/32175655/NoneN.A.
4133
382883382024
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
Efpeglenatide39N terminal amine group of His replaced by imidazo-acetyl AmidationLinearLConjugate in which LYS27 side chain linked to PEG-Fc Exendin-4 analogsAntidiabetesBlood samples were taken for PK measures pre-dose and at 1, 2, 4, 8, and 12 h post-dose on day 1, and once on days 2, 4, 7, 10, 14, 21, 28, 35, 42, and 4940 μg/kg141 (terminal elimination half life)Human serum proteaseSandwich ELISAHuman serumIn Vivohttps://pubmed.ncbi.nlm.nih.gov/32175655/NoneN.A.
4134
382883382024
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
Efpeglenatide39N terminal amine group of His replaced by imidazo-acetyl AmidationLinearLConjugate in which LYS27 side chain linked to PEG-Fc Exendin-4 analogsAntidiabetesBlood samples were taken for PK measures pre-dose and at 1, 2, 4, 8, and 12 h post-dose on day 1, and once on days 2, 4, 7, 10, 14, 21, 28, 35, 42, and 4960 μg/kg154 (terminal elimination half life)Human serum proteaseSandwich ELISAHuman serumIn Vivohttps://pubmed.ncbi.nlm.nih.gov/32175655/NoneN.A.
4135
382883382024
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
Efpeglenatide39N terminal amine group of His replaced by imidazo-acetyl AmidationLinearLConjugate in which LYS27 side chain linked to PEG-Fc Exendin-4 analogsAntidiabetesBlood samples were taken for PK measures pre-dose and at 1, 2, 4, 8, and 12 h post-dose on day 1, and once on days 2, 4, 7, 10, 14, 21, 28, 35, 42, and 49100 μg/kg180 (terminal elimination half life)Human serum proteaseSandwich ELISAHuman serumIn Vivohttps://pubmed.ncbi.nlm.nih.gov/32175655/NoneN.A.
4136
382883382024
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
Efpeglenatide39N terminal amine group of His replaced by imidazo-acetyl AmidationLinearLConjugate in which LYS27 side chain linked to PEG-Fc Exendin-4 analogsAntidiabetesblood samples were taken for PK assessments pre-dose on the first dosing day (day 1) and 8, 24, 48, 72, 96, 120, and 144 h after the first dose. Trough samples were taken immediately before dosing on days 8, 22, 36, and 50. Samples were taken again after the last (eighth) dose at 8, 24, 48, 72, 96, 120, and 144 h after dosing and 7, 10, 14, 21, 28, and 35 days after dosing1 mg155.03 (terminal elimination half life)Human serum proteaseSandwich ELISAHuman serumIn Vivohttps://pubmed.ncbi.nlm.nih.gov/32175655/NoneN.A.
4137
382883382024
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
Efpeglenatide39N terminal amine group of His replaced by imidazo-acetyl AmidationLinearLConjugate in which LYS27 side chain linked to PEG-Fc Exendin-4 analogsAntidiabetesblood samples were taken for PK assessments pre-dose on the first dosing day (day 1) and 8, 24, 48, 72, 96, 120, and 144 h after the first dose. Trough samples were taken immediately before dosing on days 8, 22, 36, and 50. Samples were taken again after the last (eighth) dose at 8, 24, 48, 72, 96, 120, and 144 h after dosing and 7, 10, 14, 21, 28, and 35 days after dosing2 mg151.53 ( terminal elimination half life)Human serum proteaseSandwich ELISAHuman serumIn Vivohttps://pubmed.ncbi.nlm.nih.gov/32175655/NoneN.A.
4138
382883382024
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
Efpeglenatide39N terminal amine group of His replaced by imidazo-acetyl AmidationLinearLConjugate in which LYS27 side chain linked to PEG-Fc Exendin-4 analogsAntidiabetesblood samples were taken for PK assessments pre-dose on the first dosing day (day 1) and 8, 24, 48, 72, 96, 120, and 144 h after the first dose. Trough samples were taken immediately before dosing on days 8, 22, 36, and 50. Samples were taken again after the last (eighth) dose at 8, 24, 48, 72, 96, 120, and 144 h after dosing and 7, 10, 14, 21, 28, and 35 days after dosing4 mg155.85 (terminal elimination half life)Human serum proteaseSandwich ELISAHuman serumIn Vivohttps://pubmed.ncbi.nlm.nih.gov/32175655/NoneN.A.
4139
382883382024
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
Efpeglenatide39N terminal amine group of His replaced by imidazo-acetyl AmidationLinearLConjugate in which LYS27 side chain linked to PEG-Fc Exendin-4 analogsAntidiabetesblood samples were taken for PK assessments pre-dose on the first dosing day (day 1) and 8, 24, 48, 72, 96, 120, and 144 h after the first dose. Samples were also taken 7, 10, 14, and 21 days after dosing. Trough samples were taken immediately before dosing on days 29 and 57. Finally, after the last (third) dose, samples were taken 8, 24, 48, 72, 96, 120, and 144 h after dosing and 7, 10, 14, 21, 28, and 35 days after dosing8 mg159.95 (terminal elimination half life)Human serum proteaseSandwich ELISAHuman serumIn Vivohttps://pubmed.ncbi.nlm.nih.gov/32175655/NoneN.A.
4140
382883382024
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
Efpeglenatide39N terminal amine group of His replaced by imidazo-acetyl AmidationLinearLConjugate in which LYS27 side chain linked to PEG-Fc Exendin-4 analogsAntidiabetesblood samples were taken for PK assessments pre-dose on the first dosing day (day 1) and 8, 24, 48, 72, 96, 120, and 144 h after the first dose. Samples were also taken 7, 10, 14, and 21 days after dosing. Trough samples were taken immediately before dosing on days 29 and 57. Finally, after the last (third) dose, samples were taken 8, 24, 48, 72, 96, 120, and 144 h after dosing and 7, 10, 14, 21, 28, and 35 days after dosing12 mg170.62 (terminal elimination half life)Human serum proteaseSandwich ELISAHuman serumIn Vivohttps://pubmed.ncbi.nlm.nih.gov/32175655/NoneN.A.
4141
382883382024
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
Efpeglenatide39N terminal amine group of His replaced by imidazo-acetyl AmidationLinearLConjugate in which LYS27 side chain linked to PEG-Fc Exendin-4 analogsAntidiabetesblood samples were taken for PK assessments pre-dose on the first dosing day (day 1) and 8, 24, 48, 72, 96, 120, and 144 h after the first dose. Samples were also taken 7, 10, 14, and 21 days after dosing. Trough samples were taken immediately before dosing on days 29 and 57. Finally, after the last (third) dose, samples were taken 8, 24, 48, 72, 96, 120, and 144 h after dosing and 7, 10, 14, 21, 28, and 35 days after dosing16 mg161.76 (terminal elimination half life)Human serum proteaseSandwich ELISAHuman serumIn Vivohttps://pubmed.ncbi.nlm.nih.gov/32175655/NoneN.A.
4142
389524872024
H-Aib-EGTFTSDVSSYLEGQAAKEFIAWLVRGRG
[3H]-semaglutide31FreeFreeLinearLAib modification at position 2, Lys26 side chain conjugated with (ADO-linker-Glu-C18(3H)GLP-1 analogsGLP-1 receptor agonistBlood sample were collected at predose, 8, 16, 24,32,40,48,56,64,72,96,120,144,168,240,336,504,672 and 840 hours post dose1 mg/ml168.3Human plasma proteaseLC-MS/MSHuman plasmaIn Vivohttps://pubmed.ncbi.nlm.nih.gov/28323117/, https://pubmed.ncbi.nlm.nih.gov/29205786/, https://pubmed.ncbi.nlm.nih.gov/33159658/NoneN.A.
4143
389524872024
H-Aib-EGTFTSDVSSYLEGQAAKEFIAWLVRGRG
Intact [3H]-semaglutide-related material31FreeFreeLinearLAib modification at position 2, Lys26 side chain conjugated with (ADO-linker-Glu-C18(3H), other metabolite may be attachedGLP-1 analogsGLP-1 receptor agonistBlood sample were collected at predose, 8, 16, 24,32,40,48,56,64,72,96,120,144,168,240,336,504,672 and 840 hours post dose1 mg/ml201.2Human plasma proteaseLC-MS/MSHuman plasmaIn Vivohttps://pubmed.ncbi.nlm.nih.gov/28323117/, https://pubmed.ncbi.nlm.nih.gov/29205786/, https://pubmed.ncbi.nlm.nih.gov/33159658/NoneN.A.
4144
389524872024
H-Aib-EGTFTSDVSSYLEGQAAKEFIAWLVRGRG
Dry [3H]-semaglutide-related material31FreeFreeLinearLAib modification at position 2, Lys26 side chain conjugated with (ADO-linker-Glu-C18(3H), other metabolite may be attachedGLP-1 analogsGLP-1 receptor agonistBlood sample were collected at predose, 8, 16, 24,32,40,48,56,64,72,96,120,144,168,240,336,504,672 and 840 hours post dose1 mg/ml180.5Human plasma proteaseLC-MS/MSHuman plasmaIn Vivohttps://pubmed.ncbi.nlm.nih.gov/28323117/, https://pubmed.ncbi.nlm.nih.gov/29205786/, https://pubmed.ncbi.nlm.nih.gov/33159658/NoneN.A.
4145
389524872024
H-Aib-EGTFTSDVSSYLEGQAAKEFIAWLVRGRG
Semaglutide31FreeFreeLinearLAib modification at position 2, Lys26 side chain conjugated with (ADO-linker-Glu-C18)GLP-1 analogsGLP-1 receptor agonistBlood samples for PK assessment of semaglutide were taken at the following time points after the first dose: 0, 6, 12, 18, 24, 30, 36, 42, 48, 60, 72, 84, 96, 120, 144 and 168 h and at the following time points after the last dose: 0, 6, 12, 18, 24, 30, 36, 42, 48, 60, 72, 84, 96, 120, 144, 168, 336, 504, 672 and 840 h. Additional PK samples were taken before dosing in weeks 4, 8 and 110.5 mg156Human blood sample proteaseLC-MS/MSHuman blood sample with once weekly dosage (at steady state)In Vivohttps://pubmed.ncbi.nlm.nih.gov/28323117/, https://pubmed.ncbi.nlm.nih.gov/29205786/, https://pubmed.ncbi.nlm.nih.gov/33159658/NoneN.A.
4146
389524872024
H-Aib-EGTFTSDVSSYLEGQAAKEFIAWLVRGRG
Semaglutide31FreeFreeLinearLAib modification at position 2, Lys26 side chain conjugated with (ADO-linker-Glu-C18)GLP-1 analogsGLP-1 receptor agonistBlood samples for PK assessment of semaglutide were taken at the following time points after the first dose: 0, 6, 12, 18, 24, 30, 36, 42, 48, 60, 72, 84, 96, 120, 144 and 168 h and at the following time points after the last dose: 0, 6, 12, 18, 24, 30, 36, 42, 48, 60, 72, 84, 96, 120, 144, 168, 336, 504, 672 and 840 h. Additional PK samples were taken before dosing in weeks 4, 8 and 111 mg159Human blood sample proteaseLC-MS/MSHuman blood sample with once weekly dosage (at steady state)In Vivohttps://pubmed.ncbi.nlm.nih.gov/28323117/, https://pubmed.ncbi.nlm.nih.gov/29205786/, https://pubmed.ncbi.nlm.nih.gov/33159658/NoneN.A.
4147
389524872024
H-Aib-EGTFTSDVSSYLEGQAAKEFIAWLVRGRG
Semaglutide31FreeFreeLinearLAib modification at position 2, Lys26 side chain conjugated with (ADO-linker-Glu-C18)GLP-1 analogsGLP-1 receptor agonistblood samples were taken 15 min prior to administration of semaglutide and 2, 8, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 38, 42, 48, 54, 60, 66, 72, 96, 144, 192, 240, 360, and 480 h after administration of semaglutide0.5 mg183 (elimination half life)Human serum proteaseLC-MS/MSHuman serum (Normal Renal Function Group)In Vivohttps://pubmed.ncbi.nlm.nih.gov/28323117/, https://pubmed.ncbi.nlm.nih.gov/29205786/, https://pubmed.ncbi.nlm.nih.gov/33159658/NoneN.A.
4148
389524872024
H-Aib-EGTFTSDVSSYLEGQAAKEFIAWLVRGRG
Semaglutide31FreeFreeLinearLAib modification at position 2, Lys26 side chain conjugated with (ADO-linker-Glu-C18)GLP-1 analogsGLP-1 receptor agonistblood samples were taken 15 min prior to administration of semaglutide and 2, 8, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 38, 42, 48, 54, 60, 66, 72, 96, 144, 192, 240, 360, and 480 h after administration of semaglutide0.5 mg169 (elimination half life)Human serum proteaseLC-MS/MSHuman serum (Mild Renal Function Group)In Vivohttps://pubmed.ncbi.nlm.nih.gov/28323117/, https://pubmed.ncbi.nlm.nih.gov/29205786/, https://pubmed.ncbi.nlm.nih.gov/33159658/NoneN.A.
4149
389524872024
H-Aib-EGTFTSDVSSYLEGQAAKEFIAWLVRGRG
Semaglutide31FreeFreeLinearLAib modification at position 2, Lys26 side chain conjugated with (ADO-linker-Glu-C18)GLP-1 analogsGLP-1 receptor agonistblood samples were taken 15 min prior to administration of semaglutide and 2, 8, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 38, 42, 48, 54, 60, 66, 72, 96, 144, 192, 240, 360, and 480 h after administration of semaglutide0.5 mg201 (elimination half life)Human serum proteaseLC-MS/MSHuman serum (Moderate Renal Function Group)In Vivohttps://pubmed.ncbi.nlm.nih.gov/28323117/, https://pubmed.ncbi.nlm.nih.gov/29205786/, https://pubmed.ncbi.nlm.nih.gov/33159658/NoneN.A.
4150
389524872024
H-Aib-EGTFTSDVSSYLEGQAAKEFIAWLVRGRG
Semaglutide31FreeFreeLinearLAib modification at position 2, Lys26 side chain conjugated with (ADO-linker-Glu-C18)GLP-1 analogsGLP-1 receptor agonistblood samples were taken 15 min prior to administration of semaglutide and 2, 8, 14, 16, 18, 20, 22, 24, 26, 28, 30, 32, 34, 38, 42, 48, 54, 60, 66, 72, 96, 144, 192, 240, 360, and 480 h after administration of semaglutide0.5 mg221 (elimination half life)Human serum proteaseLC-MS/MSHuman serum (Severe Renal Function Group)In Vivohttps://pubmed.ncbi.nlm.nih.gov/28323117/, https://pubmed.ncbi.nlm.nih.gov/29205786/, https://pubmed.ncbi.nlm.nih.gov/33159658/NoneN.A.
4151
389524872024
H-Aib-EGTFTSDVSSYLEGQAAKEFIAWLVRGRG
Semaglutide31FreeFreeLinearLAib modification at position 2, Lys26 side chain conjugated with (ADO-linker-Glu-C18)GLP-1 analogsGLP-1 receptor agonistFor ESRD subjects on hemodialysis, hourly blood samples were drawn during each of the first two hemodialysis sessions post-administration (each hemodialysis session lasted for ~2–4 h).0.5 mg243 (elimination half life)Human serum proteaseLC-MS/MSHuman serum dosage 1–24 H after hemodialysis, With No Hemodialysis For 48 H Post-Dose (End Stage Renal Disease Renal Function Group)In Vivohttps://pubmed.ncbi.nlm.nih.gov/28323117/, https://pubmed.ncbi.nlm.nih.gov/29205786/, https://pubmed.ncbi.nlm.nih.gov/33159658/NoneN.A.
4152
389524872024
H-Aib-EGTFTSDVSSYLEGQAAKEFIAWLVRGRG
Semaglutide31FreeFreeLinearLAib modification at position 2, Lys26 side chain conjugated with (ADO-linker-Glu-C18)GLP-1 analogsGLP-1 receptor agonistBlood samples were taken to determine the plasma concentration profiles of semaglutide 15 minutes prior to dosing, at time zero, and at 6, 12, 18, 24, 30, 36, 42, 48, 54, 60, 72, 96, 120, 144, 168, 336, 504, 672 and 840 hours (up to 35 days) after administration of semaglutide0.5 mg150 (Terminal elimination half life)Human plasma proteaseLC-MS/MSHuman plasma (Normal Hepatic Function Group)In Vivohttps://pubmed.ncbi.nlm.nih.gov/28323117/, https://pubmed.ncbi.nlm.nih.gov/29205786/, https://pubmed.ncbi.nlm.nih.gov/33159658/NoneN.A.
4153
389524872024
H-Aib-EGTFTSDVSSYLEGQAAKEFIAWLVRGRG
Semaglutide31FreeFreeLinearLAib modification at position 2, Lys26 side chain conjugated with (ADO-linker-Glu-C18)GLP-1 analogsGLP-1 receptor agonistBlood samples were taken to determine the plasma concentration profiles of semaglutide 15 minutes prior to dosing, at time zero, and at 6, 12, 18, 24, 30, 36, 42, 48, 54, 60, 72, 96, 120, 144, 168, 336, 504, 672 and 840 hours (up to 35 days) after administration of semaglutide0.5 mg155 (Terminal elimination half life)Human plasma proteaseLC-MS/MSHuman plasma (Mild Hepatic Function Group)In Vivohttps://pubmed.ncbi.nlm.nih.gov/28323117/, https://pubmed.ncbi.nlm.nih.gov/29205786/, https://pubmed.ncbi.nlm.nih.gov/33159658/NoneN.A.
4154
389524872024
H-Aib-EGTFTSDVSSYLEGQAAKEFIAWLVRGRG
Semaglutide31FreeFreeLinearLAib modification at position 2, Lys26 side chain conjugated with (ADO-linker-Glu-C18)GLP-1 analogsGLP-1 receptor agonistBlood samples were taken to determine the plasma concentration profiles of semaglutide 15 minutes prior to dosing, at time zero, and at 6, 12, 18, 24, 30, 36, 42, 48, 54, 60, 72, 96, 120, 144, 168, 336, 504, 672 and 840 hours (up to 35 days) after administration of semaglutide0.5 mg151 (Terminal elimination half life)Human plasma proteaseLC-MS/MSHuman plasma (Moderate Hepatic Function Group)In Vivohttps://pubmed.ncbi.nlm.nih.gov/28323117/, https://pubmed.ncbi.nlm.nih.gov/29205786/, https://pubmed.ncbi.nlm.nih.gov/33159658/NoneN.A.
4155
389524872024
H-Aib-EGTFTSDVSSYLEGQAAKEFIAWLVRGRG
Semaglutide31FreeFreeLinearLAib modification at position 2, Lys26 side chain conjugated with (ADO-linker-Glu-C18)GLP-1 analogsGLP-1 receptor agonistBlood samples were taken to determine the plasma concentration profiles of semaglutide 15 minutes prior to dosing, at time zero, and at 6, 12, 18, 24, 30, 36, 42, 48, 54, 60, 72, 96, 120, 144, 168, 336, 504, 672 and 840 hours (up to 35 days) after administration of semaglutide0.5 mg163 (Terminal elimination half life)Human plasma proteaseLC-MS/MSHuman plasma (Severe Hepatic Function Group)In Vivohttps://pubmed.ncbi.nlm.nih.gov/28323117/, https://pubmed.ncbi.nlm.nih.gov/29205786/, https://pubmed.ncbi.nlm.nih.gov/33159658/NoneN.A.
4156
389524872024
H-Aib-EGTFTSDVSSYLEGQAAKEFIAWLVRGRG
Semaglutide31FreeFreeLinearLAib modification at position 2, Lys26 side chain conjugated with (ADO-linker-Glu-C18)GLP-1 analogsGLP-1 receptor agonistN.A.20 mg153Human plasma proteaseLuminescence oxygen channelling immunoassay (LOCI)Human plasma dosed at steady state (Healthy)In Vivohttps://pubmed.ncbi.nlm.nih.gov/28323117/, https://pubmed.ncbi.nlm.nih.gov/29205786/, https://pubmed.ncbi.nlm.nih.gov/33159658/NoneN.A.
4157
389524872024
H-Aib-EGTFTSDVSSYLEGQAAKEFIAWLVRGRG
Semaglutide31FreeFreeLinearLAib modification at position 2, Lys26 side chain conjugated with (ADO-linker-Glu-C18)GLP-1 analogsGLP-1 receptor agonistN.A.40 mg161Human plasma proteaseLuminescence oxygen channelling immunoassay (LOCI)Human plasma dosed at steady state (Healthy)In Vivohttps://pubmed.ncbi.nlm.nih.gov/28323117/, https://pubmed.ncbi.nlm.nih.gov/29205786/, https://pubmed.ncbi.nlm.nih.gov/33159658/NoneN.A.
4158
389524872024
H-Aib-EGTFTSDVSSYLEGQAAKEFIAWLVRGRG
Semaglutide31FreeFreeLinearLAib modification at position 2, Lys26 side chain conjugated with (ADO-linker-Glu-C18)GLP-1 analogsGLP-1 receptor agonistN.A.40 mg158Human plasma proteaseLuminescence oxygen channelling immunoassay (LOCI)Human plasma dosed at steady state (Type 2 Diabetic)In Vivohttps://pubmed.ncbi.nlm.nih.gov/28323117/, https://pubmed.ncbi.nlm.nih.gov/29205786/, https://pubmed.ncbi.nlm.nih.gov/33159658/NoneN.A.
4159
389524872024
H-Aib-EGTFTSDVSSYLEGQAAKEFIAWLVRGRG
Semaglutide31FreeFreeLinearLAib modification at position 2, Lys26 side chain conjugated with (ADO-linker-Glu-C18)GLP-1 analogsGLP-1 receptor agonist10 days10 mg160Human plasma proteaseLC-MS/MSHuman plasma dosed with 10 mg Once Daily Semaglutide (Subjects In The Fasting Arm Were Fasting Overnight For At Least 10 H Before Each Dosing)In Vivohttps://pubmed.ncbi.nlm.nih.gov/28323117/, https://pubmed.ncbi.nlm.nih.gov/29205786/, https://pubmed.ncbi.nlm.nih.gov/33159658/NoneN.A.
4160
389524872024
H-Aib-EGTFTSDVSSYLEGQAAKEFIAWLVRGRG
Semaglutide31FreeFreeLinearLAib modification at position 2, Lys26 side chain conjugated with (ADO-linker-Glu-C18)GLP-1 analogsGLP-1 receptor agonist10 days10 mg152Human plasma proteaseLC-MS/MSHuman plasma dosed with 10 Mg Once Daily Semaglutide (Subjects In The Reference Arm Were Fasting Overnight For At Least 6 H Before Each Dosing)In Vivohttps://pubmed.ncbi.nlm.nih.gov/28323117/, https://pubmed.ncbi.nlm.nih.gov/29205786/, https://pubmed.ncbi.nlm.nih.gov/33159658/NoneN.A.
4161
389524872024
H-Aib-EGTFTSDVSSYLEGQAAKEFIAWLVRGRG
Semaglutide31FreeFreeLinearLAib modification at position 2, Lys26 side chain conjugated with (ADO-linker-Glu-C18)GLP-1 analogsGLP-1 receptor agonistBlood samples for semaglutide PK assessment were drawn onday 1 (pre- and post-dose), then pre-dose on days 6 to 107 mg141Human plasma proteaseN.A.Human plasma (Type 2 Diabetic Patient With Upper Gastrointestinal Disease)In Vivohttps://pubmed.ncbi.nlm.nih.gov/28323117/, https://pubmed.ncbi.nlm.nih.gov/29205786/, https://pubmed.ncbi.nlm.nih.gov/33159658/NoneN.A.
4162
389524872024
H-Aib-EGTFTSDVSSYLEGQAAKEFIAWLVRGRG
Semaglutide31FreeFreeLinearLAib modification at position 2, Lys26 side chain conjugated with (ADO-linker-Glu-C18)GLP-1 analogsGLP-1 receptor agonistBlood samples for semaglutide PK assessment were drawn onday 1 (pre- and post-dose), then pre-dose on days 6 to 107 mg142Human plasma proteaseN.A.Human plasma (Type 2 Diabetic Patient Without Upper Gastrointestinal Disease)In Vivohttps://pubmed.ncbi.nlm.nih.gov/28323117/, https://pubmed.ncbi.nlm.nih.gov/29205786/, https://pubmed.ncbi.nlm.nih.gov/33159658/NoneN.A.
4163
389524872024
H-Aib-EGTFTSDVSSYLEGQAAKEFIAWLVRGRG
Semaglutide31FreeFreeLinearLAib modification at position 2, Lys26 side chain conjugated with (ADO-linker-Glu-C18)GLP-1 analogsGLP-1 receptor agonistBlood samples were drawn into K3EDTA tubes pre-dose on day 1, and at set time points on days 9 and 1010 mg150Human plasma proteaseLC-MS/MSHuman plasma dosed with 10 mg Semaglutide Once Daily For 5 DaysIn Vivohttps://pubmed.ncbi.nlm.nih.gov/28323117/, https://pubmed.ncbi.nlm.nih.gov/29205786/, https://pubmed.ncbi.nlm.nih.gov/33159658/NoneN.A.
4164
389524872024
H-Aib-EGTFTSDVSSYLEGQAAKEFIAWLVRGRG
Semaglutide31FreeFreeLinearLAib modification at position 2, Lys26 side chain conjugated with (ADO-linker-Glu-C18)GLP-1 analogsGLP-1 receptor agonistBlood samples were drawn into K3EDTA tubes pre-dose on day 1, and at set time points on days 9 and 1010 mg156Human plasma proteaseLC-MS/MSHuman plasma dosed with 10 mg Semaglutide Once Daily For 5 Days And With Omeprazole 40 MgIn Vivohttps://pubmed.ncbi.nlm.nih.gov/28323117/, https://pubmed.ncbi.nlm.nih.gov/29205786/, https://pubmed.ncbi.nlm.nih.gov/33159658/NoneN.A.
4165
381165632023
MKIILWLCVFGLFLATLFPISWQMPVESGLSSEDSASSESFASKIKRHGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPSGGGGGSGGGGSGGGGS-(DARP)-GGGGSGGGGSGGGGSMDSDETGFEHSGLWVSVLAGLLLGACQAHPIPDSSPLLQFGGQVRQRYLYTDDAQQTEAHLEIREDGTVGGAADQSPESLLQLKALKPGVIQILGVKTSRFLCQRPDGALYGSLHFDPEACSFRELLLEDGYNVYQSEAHGLPLHLPGNKSPHRDPAPRGPARFLPLPGLPPALPEPPGILAPQPPDVGSSDPLSMVGPSQGRSPSYAS
Ex-DARP-FGF21327Exendin-4 peptide (Ex) fused to the N-terminus of the DARPin (DARP) protein via (GGGGS)3, His-tag and TEV protease site introduced at position 1FGF21 fused to the C-terminus of the DARPin (DARP) protein via (GGGGS)3 linkerLinearLL98R and P171A amino acid substitutions in FBGF21Exendin-4, DARPin, FGF21 fusion proteinAntidiabetes, AntiobesityApproximately 40 µL of blood was collected from the orbital venous plexus at different time points (1, 3, 8, 12, 24, 36, 48, and 72 h)10 nmol/kg27.6 ± 3.2C57BL/6 mice plasma proteaseELISAC57BL/6 mice plasmaIn VivoNoneNoneEx-DARP-FGF21 and Ex-DARP were efficaciously bound to HSA with half-maximal binding concentrations of 4.5 nM and 1.9 nM, respectively
4166
380973782023
CR
Au_CR2Au gold particle conjuagtion at N terminal through formation of Au-S bondAmidationLinearLNoneSyntheticAntimicrobialBlood samples collected at 5 min and at 1, 3, 5,24, and 48 h10 mg/kg∼17.5Mice plasma proteaseICP-MSMice plasmaIn VivoNoneNoneMIC(μg/mL) = 1.56 against S. aureus
4167
380973782023
CR
Au_CR2Au gold particle conjuagtion at N terminal through formation of Au-S bondAmidationLinearLNoneSyntheticAntimicrobialBlood samples collected at 5 min and at 1, 3, 5,24, and 48 h10 mg/kg∼17.5Mice plasma proteaseICP-MSMice plasmaIn VivoNoneNoneMIC(μg/mL) >100 against E.coli
4168
380973782023
CR
Au_CR2Au gold particle conjuagtion at N terminal through formation of Au-S bondAmidationLinearLNoneSyntheticAntimicrobialBlood samples collected at 5 min and at 1, 3, 5,24, and 48 h10 mg/kg∼17.5Mice plasma proteaseICP-MSMice plasmaIn VivoNoneNoneMIC(μg/mL) >100 against B.subtilis
4169
380973782023
CR
Au_CR2Au gold particle conjuagtion at N terminal through formation of Au-S bondAmidationLinearLNoneSyntheticAntimicrobialBlood samples collected at 5 min and at 1, 3, 5,24, and 48 h10 mg/kg∼17.5Mice plasma proteaseICP-MSMice plasmaIn VivoNoneNoneMIC(μg/mL) = 1.56 against C.albicans
4170
380928942023
MPRPRLLAALCGALLCAPSLLVALDICSKNPCHNGGLCEEISQEVRGDVFPSYTCTCLKGYAGNHCETKCVEPLGLENGNIANSQIAASSVRVTFLGLQHWVPELARLNRAGMVNAWTPSSNDDNPWIQVNLLRRMWVTGVVTQGASRLASHEYLKAFKVAYSLNGHEFDFIHDVNKKHKEFVGNWNKNAVHVNLFETPVEAQYVRLYPTSCHTACTLRFELLGCELNGCANPLGLKNNSIPDKQITASSSYKTWGLHLFSWNPSYARLDKQGNFNAWVAGSYGNDQWLQVDLGSSKEVTGIITQGARNFGSVQFVASYKVAYSNDSANWTEYQDPRTGSSKIFPGNWDNHSHKKNLFETPILARYVRILPVAWHNRIALRLELLGC
Tag-free rhMFG-E838723 amino acid leader sequence of cystatin S introduced at N terminal FreeLinearLNoneExpressed in Expi293F cellsAntiinflammatory (Including Radiation Injury)Blood samples (100 μl per time point) were collected starting from 2 to 6 hours50 µg1.45 (Terminal Elimination Half Life)SD rats plasma proteaseELISASD rats plasmaIn VivoNoneNoneThe tag-free rhMFG-E8 demonstrated markedly higher cell adhesion binding activity (to SVEC4-10 cells) compared to E. coli-expressed His-tagged rhMFG-E8, which binds to αVβ3 integrin on the membrane of phagocytes
4171
380928942023
MPRPRLLAALCGALLCAPSLLVALDICSKNPCHNGGLCEEISQEVRGDVFPSYTCTCLKGYAGNHCETKCVEPLGLENGNIANSQIAASSVRVTFLGLQHWVPELARLNRAGMVNAWTPSSNDDNPWIQVNLLRRMWVTGVVTQGASRLASHEYLKAFKVAYSLNGHEFDFIHDVNKKHKEFVGNWNKNAVHVNLFETPVEAQYVRLYPTSCHTACTLRFELLGCELNGCANPLGLKNNSIPDKQITASSSYKTWGLHLFSWNPSYARLDKQGNFNAWVAGSYGNDQWLQVDLGSSKEVTGIITQGARNFGSVQFVASYKVAYSNDSANWTEYQDPRTGSSKIFPGNWDNHSHKKNLFETPILARYVRILPVAWHNRIALRLELLGC
Tag-free rhMFG-E838723 amino acid leader sequence of cystatin S introduced at N terminal FreeLinearLNoneExpressed in Expi293F cellsAntiinflammatory (Including Radiation Injury)Blood samples (100 μl per time point) were collected starting from 2 to 12 hours50 µg2.33 (Terminal Elimination Half Life)SD rats plasma proteaseELISASD rats plasmaIn VivoNoneNoneThe tag-free rhMFG-E8 demonstrated markedly higher cell adhesion binding activity (to SVEC4-10 cells) compared to E. coli-expressed His-tagged rhMFG-E8, which binds to αVβ3 integrin on the membrane of phagocytes
4172
380270632023
QVTLKESGPGILQPSQTLSLTCSFSGFSLNTFGMGVSWIRQPSGKGLEWLAHIFWDDDKHYNPSLKSRLTISKDTSNNQVFLKITTVDTADTATYYCVRYGFDGFPYWGQGTGGGGSGGGGSGGGGSDVVMTQTPLSLPVSLGDQASISCRSNQSLVHSNGNTYLHWYLQKPGQSPKLLIYKVSNRFSGVPDRPSGSGSGTDFTLKISRVEAEDLGFYFCSQSTRVPWTFGGGTKLEIKR -METDTLLLWVLLLWVPGSTGDEFMGYQGPPGPPGPPGIPGNHGNNGNNGATGHEGAKGEKGDKGDLGPRGERGQHGPKGEKGYPGIPGYCGPPGPPGPPGIPGNHGNNGNNGATGHEGAKGEKGDKGDLGPRGERGQHGPKGEKGYPGIPDYKDDDDKLQGGRHHHHHH
ScFv9-CD466FreeFusion of CDLinearLBiotinylationCD sequence originates from the C1qTNF3 protein and scFv9 sequence is derived from an antibody fragment to target amyloid beta (Aβ)Treatment of AD and Parkinson diseasePlasma was collected at 0, 2, 4, 8, and 24 h after injection250 μg1.82TgCRND8 mice plasma proteaseDirect ELISATgCRND8 mice plasmaIn VivoNoneNoneN.A.
4173
380270632023
QVTLKESGPGILQPSQTLSLTCSFSGFSLNTFGMGVSWIRQPSGKGLEWLAHIFWDDDKHYNPSLKSRLTISKDTSNNQVFLKITTVDTADTATYYCVRYGFDGFPYWGQGTGGGGSGGGGSGGGGSDVVMTQTPLSLPVSLGDQASISCRSNQSLVHSNGNTYLHWYLQKPGQSPKLLIYKVSNRFSGVPDRPSGSGSGTDFTLKISRVEAEDLGFYFCSQSTRVPWTFGGGTKLEIKR 
ScFv9304FreeFreeLinearLBiotinylationThe scFv9 sequence is derived from an antibody fragment to target amyloid beta (Aβ)Treatment of AD and Parkinson diseasePlasma was collected at 0, 2, 4, 8, and 24 h after injection250 μg0.74TgCRND8 mice plasma proteaseDirect ELISATgCRND8 mice plasmaIn VivoNoneNoneN.A.
4174
378803182023
VAIALKAAHYHTHKE
L115AcetylationFreeLinearLNoneDerived from calciterminAntimicrobial37 °C0.0001 M>2Human plasma proteaseHPLCHuman plasma with 1 ml of ammonium acetate buffer (pH 7.4) In VitroNoneNoneCFU = 40 ± 10 for 0.032 mg/mL peptide concentration (0.1 mL of microbial suspension after 24 hours of incubation at 37°C) (Effect of peptide derivatives on Candida albicans (ATCC 10231) proliferation)
4175
378803182023
VAIALKAAHYHTHKE
L215AcetylationAmidationLinearLNoneDerived from calciterminAntimicrobial37 °C0.0001 M68Human plasma proteaseHPLCHuman plasma with 1 ml of ammonium acetate buffer (pH 7.4) In VitroNoneNoneCFU = 211 ± 25 for 0.032 mg/mL peptide concentration (0.1 mL of microbial suspension after 24 hours of incubation at 37°C) (Effect of peptide derivatives on Candida albicans (ATCC 10231) proliferation)
4176
378803182023
VAIALKAAHYHTHKE
L315FreeAmidationLinearLNoneDerived from calciterminAntimicrobial37 °C0.0001 M20Human plasma proteaseHPLCHuman plasma with 1 ml of ammonium acetate buffer (pH 7.4) In VitroNoneNoneCFU = 189 ± 23 for 0.032 mg/mL peptide concentration (0.1 mL of microbial suspension after 24 hours of incubation at 37°C) (Effect of peptide derivatives on Candida albicans (ATCC 10231) proliferation)
4177
378803182023
VAIALKAAHYHTHKE
Wild-type Calcitermin (WT)15FreeFreeLinearLNoneC-terminal cleavage fragment of calgranulin CAntimicrobial37 °C0.0001 M18 ± 3Human plasma proteaseHPLCHuman plasma with 1 ml of ammonium acetate buffer (pH 7.4) In VitroNoneNoneCFU = 28 ± 15 for 0.032 mg/mL peptide concentration (0.1 mL of microbial suspension after 24 hours of incubation at 37°C) (Effect of peptide derivatives on Candida albicans (ATCC 10231) proliferation)
4178
378754812023
N.A.
IL-15-Cy7N.A.FreeFreeLinearLCy7Derived from Interleukin-15AntitumorThe blood sample was harvested at timed intervals (2 min, 5 min, 15 min, 30 min, 1 h, 2 h, 4 h, 8 h, 12 h, and 24 h)N.A.0.69Mice blood proteaseFluorescence spectrophotometryMice bloodIn VivoNoneNoneNot mentioned
4179
378754812023
N.A.
biNV-IL-15-Cy7N.A.FreeFreeLinearLCy7Derived from Interleukin-15AntitumorThe blood sample was harvested at timed intervals (2 min, 5 min, 15 min, 30 min, 1 h, 2 h, 4 h, 8 h, 12 h, and 24 h)N.A.5.66Mice blood proteaseFluorescence spectrophotometryMice bloodIn VivoNoneNoneNot mentioned
4180
378748232023
GWGIPWCTLDPGSLQCAWLGKHGGGGSGGVVCQDWEGVELCWQGG
MDK147242AcetylationFreeCyclic (Disulphide Bond Bw C7-C16, C32-C41) LIL-7Ra binding domain linked with yc binding domain with the help of linker GGS linkerSyntheticIL-7R agonist peptide37 °C10 mM60Human Plasma ProteaseLC-MS/MSHuman plasmaIn VitroNoneNoneIC50(nM) = 340 (IC50 values in a competition ELISA for compound binding to human IL-7Rα)
4181
378748232023
GWGIPWCTLDPGSLQCAWLGKHGGGGSGGVVCQDWEGVELCWQGG
MDK147242AcetylationFreeCyclic (Disulphide Bond Bw C7-C16, C32-C41) LIL-7Ra binding domain linked with yc binding domain with the help of linker GGS linkerSyntheticIL-7R agonist peptide37 °C10 mM104Cynomolgus monkeys plasma proteaseLC-MS/MSCynomolgus monkeys plasmaIn VitroNoneNoneIC50(nM) = 190 (IC50 values in a competition ELISA for compound binding to Cyno IL-7Rα)
4182
378748232023
GSGSGSGSGSGSGSGSGSGSGWGIPWCTLDPGSLQCAWLGKHGGGGSGGVVCQDWEGVELCWQGGGWGIPWCTLDPGSLQCAWLGKHGGGGSGGVVCQDWEGVELCWQGG
MDK-703 110Fused with IgG2 Fc chain via (Gly-Ser)10 linker, Fc-fragments consisting of the CH2 and CH3 domains of the heavy chain and hinge regions of human IgG2 Fc modified as follows: The first and second cysteines of the hinge region were replaced with serine to prevent detrimental disulfide bridge formation; the last amino acid (lysine) of the Fc region was replaced with an alanineFreeLinearLNoneSyntheticIL-7R agonist peptideBlood samples were collected at pre-Dose (day 1), 0.5, 1 h, 2 h, 4 h, 8 h, 24 h, 48 h, 72 h, 96 h, 120 h, 144 h, 168 h, 192 h, and 216 h post-dose1 mg/kg46 (Terminal Half Life)Cynomolgus monkeys serum proteaseSandwich ELISACynomolgus monkeys serumIn VivoNoneNoneIC50(nM) = 190 (IC50 values in a competition ELISA for compound binding to Cyno IL-7Rα)
4183
378354892023
QQTNWSLGGGSC
QQT*-IRDye80012QQT* conjugated with IRDye800 at C terminus using linkerFreeLinearLNoneSyntheticUsed for in vivo imaging to identify premalignant Colorectal LesionsRP-HPLC was performed at 0, 0.5, 1, 2, 4, 8, and 24 h30 μM3.6APC mice serum proteaseRP-HPLCAPC mice serumIn VivoNoneNoneNot mentioned
4184
377596832023
DCAWHLGELVWCTSLDQINVTFLDLEYEMKKLEEAIKKLEESYIDLKEL
IBP-EK132Conjugation with human immunoglobulin G Fc-binding peptide (IBP) at n terminusFreeLinearLNoneFusion proteinAntiviralSerial blood samples were collected from monkeys that received IBP-EK1 or EK1 before injection and at 2, 4, 6, 24, 72, and 144 h post injection10 mg/kg37.67Rhesus monkeys serum proteaseHPLC-MS/MSRhesus monkeys serumIn VivoNoneNoneIC50 = 788 nM for IBP-EK1 ( against Pseudotyped SARS-CoV-2 Variants on Caco-2 Cells)
4185
377596832023
DCAWHLGELVWCTSLDQINVTFLDLEYEMKKLEEAIKKLEESYIDLKEL
IBP-EK132Conjugation with human immunoglobulin G Fc-binding peptide (IBP) at n terminusFreeLinearLNoneFusion proteinAntiviralSerial blood samples were collected from monkeys that received IBP-EK1 or EK1 before injection and at 2, 4, 6, 24, 72, and 144 h post injection10 mg/kg39.72Rhesus monkeys serum proteaseHPLC-MS/MSRhesus monkeys serumIn VivoNoneNoneIC50 = 788 nM for IBP-EK1 ( against Pseudotyped SARS-CoV-2 Variants on Caco-2 Cells)
4186
374497812023
pSar200-b-pCys(SO2Et)30
NCL30230Polysarcosine = poly(N-methyl glycine)FreeLinearLfluorescently labeled with Atto647N, polysarcosine-block-poly(S-ethylsulfonyl-l-cysteine)syntheticImprove the therapeutic profile of hydrophobic drugs, reduce or completely avoid protein corona formationBlood samples of 50 μL were collected from the tail vein at the defined time points after systemic administration: 10 min, 1 h, 6 h, 24 h, 72 h5 μg/μL11.4C57BL/6 mice plasma proteaseFluorescence spectrophotometryC57BL/6 mice plasma In VivoNoneNoneNot mentioned
4187
374497812023
pSar200-b-pCys(SO2Et)30
2F-CL30230Polysarcosine = poly(N-methyl glycine)FreeLinearLfluorescently labeled with Atto647N, polysarcosine-block-poly(S-ethylsulfonyl-l-cysteine)syntheticImprove the therapeutic profile of hydrophobic drugs, reduce or completely avoid protein corona formationBlood samples of 50 μL were collected from the tail vein at the defined time points after systemic administration: 10 min, 1 h, 6 h, 24 h, 72 h5 μg/μL11.3C57BL/6 mice plasma proteaseFluorescence spectrophotometryC57BL/6 mice plasma In VivoNoneNoneNot mentioned
4188
374497812023
pSar200-b-pCys(SO2Et)30
3F-CL30230Polysarcosine = poly(N-methyl glycine)FreeLinearLfluorescently labeled with Atto647N, polysarcosine-block-poly(S-ethylsulfonyl-l-cysteine)syntheticImprove the therapeutic profile of hydrophobic drugs, reduce or completely avoid protein corona formationBlood samples of 50 μL were collected from the tail vein at the defined time points after systemic administration: 10 min, 1 h, 6 h, 24 h, 72 h5 μg/μL19.1C57BL/6 mice plasma proteaseFluorescence spectrophotometryC57BL/6 mice plasma In VivoNoneNoneNot mentioned
4189
373974952023
SLAFVDVLN
Peptide9FreeFreeLinearLRemoving an Asp residueIsolated from Merluccius productus fish protein hydrolysateInhibits BACE-1Blood was taken after 0, 5, and 30 min and 2, 6, and 24 h after injectio4 mg/kg0.69Mouse plasma proteaseMass spectrometryMouse plasmaIn VivoNoneNoneKi(µM)= 0.0940 BACE-1 activity with peptide which has reduced activity due to inhibition by peptide
4190
373909792023
H-Aib-DGTFTSELSRLREGARLQRLLQGLLQGLVGK
BI-343433FreeAmidationLinearLLys33 conjuagted with HLE (fatty acid based half life extension group),Substituting Ser with 2-aminoisobutyric acid (Aib) at position 2Lipidated secretin analogSecretin receptor agonist N.A.30 nmol/kg<15Male NMRI mice plasma proteaseMass spectrometryMale NMRI mice plasma (Non fasted)In VivoNoneNoneEC50 =15.5 pM for BI-3434
4191
373909792023
HSDGTFTSELSRLREEARLKRLLQGLV
Stapled secretin27FreeAmidationCyclic (E16-K20 Lactam Bridge)LE16, K20 modificationHuman secretin modified analogSecretin receptor agonist N.A.30 nmol/kgN.A.Male NMRI mice plasma proteaseMass spectrometryMale NMRI mice plasma (Non fasted)In VivoNoneNoneEC50 = 1172 nM for native secretin on murine adipocytes
4192
373848952023
HRHTKQRHTALH
CLA-coated PTX-SPIONs@HRH12FreeFreeLinearLNoneSyntheticAntiangiogenic (used for targeted delivery of Paclitaxel in non-small cell lung carcinoma)Mice were euthanized over 24 h at t = 0.5, 1, 4, 8, and 24 h15.6 μg/mL17.1Mice Plasma ProteaseHPLCMice plasma In VivoNoneNoneThe activity value for CLA-coated PTX-SPIONs@HRH at the maximal therapeutic concentration (100 μg/mL) resulted in 12.8% cell viability on A549 lung adenocarcinoma cells
4193
373848952023
HRHTKQRHTALH
CLA-coated PTX-SPIONs@HRH12FreeFreeLinearLNoneSyntheticAntiangiogenic (used for targeted delivery of Paclitaxel in non-small cell lung carcinoma)Mice were euthanized over 24 h at t = 0.5, 1, 4, 8, and 24 h15.6 μg/mL17.1Mice Plasma ProteaseHPLCMice plasma In VivoNoneNoneThe activity value for CLA-coated PTX-SPIONs@HRH at the maximal therapeutic concentration (100 μg/mL) resulted in 12.8% cell viability on A549 lung adenocarcinoma cells
4194
373732032023
LRKLRKRLLRLVGRQLEEFL
HM-10/1020FreeFreeLinearLNoneChimeric high-density lipoprotein mimetic peptideAnticancerTimepoints of 0, 10, 20, 30, 60, and 120 min2 μM164Human plasma proteaseTriple Quadrupole Mass spectrometryHuman plasmaIn VitroNoneNoneEnzyme Activity = 0.682 at 2 microMolar of HM1010 (Cytochrome P450 (CYP1A2) Induction in Single-Donor Human Hepatocytes Lot HH1086)
4195
373732032023
LRKLRKRLLRLVGRQLEEFL
HM-10/1020FreeFreeLinearLNoneChimeric high-density lipoprotein mimetic peptideAnticancerTimepoints of 0, 10, 20, 30, 60, and 120 min2 μM82.5SD rats plasma proteaseTriple Quadrupole Mass spectrometrySD rats plasma In VitroNoneNoneNot mentioned
4196
373732032023
LRKLRKRLLRLVGRQLEEFL
HM-10/1020FreeFreeLinearLNoneChimeric high-density lipoprotein mimetic peptideAnticancerTimepoints of 0, 10, 20, 30, 60, and 120 min2 μM54.6Beagle dogs plasma proteaseTriple Quadrupole Mass spectrometryBeagle dogs plasmaIn VitroNoneNoneNot mentioned
4197
373732032023
LRKLRKRLLRLVGRQLEEFL
HM-10/1020FreeFreeLinearLNoneChimeric high-density lipoprotein mimetic peptideAnticancerTimepoints of 0, 10, 20, 30, 60, and 120 min2 μM52.7Cynomolgus monkeys plasma proteaseTriple Quadrupole Mass spectrometryCynomolgus monkeys plasma In VitroNoneNoneNot mentioned
4198
373732032023
LRKLRKRLLRLVGRQLEEFL
HM-10/1020FreeFreeLinearLNoneChimeric high-density lipoprotein mimetic peptideAnticancerTimepoints of 0, 10, 20, 30, 60, and 120 min2 μM5.68CD-1 mouse plasma proteaseTriple Quadrupole Mass spectrometryCD-1 mouse plasmaIn VitroNoneNoneNot mentioned
4199
373732032023
LRKLRKRLLRLVGRQLEEFL
HM-10/1020FreeFreeLinearLNoneChimeric high-density lipoprotein mimetic peptideAnticancer120 minutes2 μM372Gastric fluid proteaseTriple Quadrupole Mass spectrometrySimulated Gastric Fluid (SGF) at pH = 1.3In VitroNoneNoneEnzyme Activity = 0.682 at 2 microMolar of HM1010 (Cytochrome P450 (CYP1A2) Induction in Single-Donor Human Hepatocytes Lot HH1086)
4200
373732032023
LRKLRKRLLRLVGRQLEEFL
HM-10/1020FreeFreeLinearLNoneChimeric high-density lipoprotein mimetic peptideAnticancer120 minutes2 μM2.72Intestinal fluid proteaseTriple Quadrupole Mass spectrometrySimulated Intestinal Fluid (SIF) at pH = 5.5In VitroNoneNoneEnzyme Activity = 0.682 at 2 microMolar of HM1010 (Cytochrome P450 (CYP1A2) Induction in Single-Donor Human Hepatocytes Lot HH1086)
4201
373732032023
LRKLRKRLLRLVGRQLEEFL
HM-10/1020FreeFreeLinearLNoneChimeric high-density lipoprotein mimetic peptideAnticancer120 minutes2 μM>120N.A.Triple Quadrupole Mass spectrometrypotassium phosphate buffers of pH 1.3 (acidic)In VitroNoneNoneEnzyme Activity = 0.682 at 2 microMolar of HM1010 (Cytochrome P450 (CYP1A2) Induction in Single-Donor Human Hepatocytes Lot HH1086)
4202
373732032023
LRKLRKRLLRLVGRQLEEFL
HM-10/1020FreeFreeLinearLNoneChimeric high-density lipoprotein mimetic peptideAnticancer120 minutes2 μM>120N.A.Triple Quadrupole Mass spectrometrypotassium phosphate buffers of pH 5.5 (slightly acidic)In VitroNoneNoneEnzyme Activity = 0.682 at 2 microMolar of HM1010 (Cytochrome P450 (CYP1A2) Induction in Single-Donor Human Hepatocytes Lot HH1086)
4203
373732032023
LRKLRKRLLRLVGRQLEEFL
HM-10/1020FreeFreeLinearLNoneChimeric high-density lipoprotein mimetic peptideAnticancer120 minutes2 μM433N.A.Triple Quadrupole Mass spectrometrypotassium phosphate buffers of pH 7.4 (basic)In VitroNoneNoneEnzyme Activity = 0.682 at 2 microMolar of HM1010 (Cytochrome P450 (CYP1A2) Induction in Single-Donor Human Hepatocytes Lot HH1086)
4204
373732032023
LRKLRKRLLRLVGRQLEEFL
HM-10/1020FreeFreeLinearLNoneChimeric high-density lipoprotein mimetic peptideAnticancerAt the assay points (time zero, 15,30, 60, 90, and 120 minutes), samples were removed for analysis2 μM (0.5 mg protein/mL of each species pooled together)32.5CD-1 mouse Liver Microsomes proteaseLC-MS/MSCD-1 mouse Liver Microsomes In VitroNoneNoneN.A.
4205
373732032023
LRKLRKRLLRLVGRQLEEFL
HM-10/1020FreeFreeLinearLNoneChimeric high-density lipoprotein mimetic peptideAnticancerAt the assay points (time zero, 15,30, 60, 90, and 120 minutes), samples were removed for analysis2 μM (0.5 mg protein/mL of each species pooled together)27.7SD rats Liver Microsome ProteaseLC-MS/MSSD rats Liver MicrosomeIn VitroNoneNoneN.A.
4206
373732032023
LRKLRKRLLRLVGRQLEEFL
HM-10/1020FreeFreeLinearLNoneChimeric high-density lipoprotein mimetic peptideAnticancerAt the assay points (time zero, 15,30, 60, 90, and 120 minutes), samples were removed for analysis2 μM (0.5 mg protein/mL of each species pooled together)33Beagle dogs Liver Microsome ProteaseLC-MS/MSBeagle dogs Liver MicrosomeIn VitroNoneNoneN.A.
4207
373732032023
LRKLRKRLLRLVGRQLEEFL
HM-10/1020FreeFreeLinearLNoneChimeric high-density lipoprotein mimetic peptideAnticancerAt the assay points (time zero, 15,30, 60, 90, and 120 minutes), samples were removed for analysis2 μM (0.5 mg protein/mL of each species pooled together)21.8Cynomolgus monkeys Liver Microsome ProteaseLC-MS/MSCynomolgus monkeys Liver microsomeIn VitroNoneNoneN.A.
4208
373732032023
LRKLRKRLLRLVGRQLEEFL
HM-10/1020FreeFreeLinearLNoneChimeric high-density lipoprotein mimetic peptideAnticancerAt the assay points (time zero, 15,30, 60, 90, and 120 minutes), samples were removed for analysis2 μM (0.5 mg protein/mL of each species pooled together)20.3Human Liver Microsome proteaseLC-MS/MSHuman Liver MicrosomeIn VitroNoneNoneN.A.
4209
373732032023
LRKLRKRLLRLVGRQLEEFL
HM-10/1020FreeFreeLinearLNoneChimeric high-density lipoprotein mimetic peptideAnticancerAt the assay points (time zero, 15, 30, 60,120, and 180 minutes), samples were removed for analysis2 μM (0.5 million cells/mL, of each species pooled together) <15CD-1 mouse Hepatocytes Lysate ProteaseLC-MS/MSCD-1 mouse Hepatocytes LysateIn VitroNoneNoneEnzyme Activity = 0.682 at 2 microMolar of HM1010 (Cytochrome P450 (CYP1A2) Induction in Single-Donor Human Hepatocytes Lot HH1086)
4210
373732032023
LRKLRKRLLRLVGRQLEEFL
HM-10/1020FreeFreeLinearLNoneChimeric high-density lipoprotein mimetic peptideAnticancerAt the assay points (time zero, 15, 30, 60,120, and 180 minutes), samples were removed for analysis2 μM (0.5 million cells/mL, of each species pooled together) 5.81SD rats Hepatocytes Lysates proteaseLC-MS/MSSD rats hepatocytes LysatesIn VitroNoneNoneN.A.
4211
373732032023
LRKLRKRLLRLVGRQLEEFL
HM-10/1020FreeFreeLinearLNoneChimeric high-density lipoprotein mimetic peptideAnticancerAt the assay points (time zero, 15, 30, 60,120, and 180 minutes), samples were removed for analysis2 μM (0.5 million cells/mL, of each species pooled together) 10.7Beagle dogs Hepatocytes Lysates proteaseLC-MS/MSBeagle dogs Hepatocytes LysatesIn VitroNoneNoneN.A.
4212
373732032023
LRKLRKRLLRLVGRQLEEFL
HM-10/1020FreeFreeLinearLNoneChimeric high-density lipoprotein mimetic peptideAnticancerAt the assay points (time zero, 15, 30, 60,120, and 180 minutes), samples were removed for analysis2 μM (0.5 million cells/mL, of each species pooled together) 12.1Cynomolgus monkeys Hepatocytes Lysates proteaseLC-MS/MSCynomolgus monkeys Hepatocytes LysatesIn VitroNoneNoneN.A.
4213
373732032023
LRKLRKRLLRLVGRQLEEFL
HM-10/1020FreeFreeLinearLNoneChimeric high-density lipoprotein mimetic peptideAnticancerAt the assay points (time zero, 15, 30, 60,120, and 180 minutes), samples were removed for analysis2 μM (0.5 million cells/mL, of each species pooled together) 5.28Human Hepatocytes Lysates proteaseLC-MS/MSHuman HepatocytesIn VitroNoneNoneEnzyme Activity = 0.682 at 2 microMolar of HM1010 (Cytochrome P450 (CYP1A2) Induction in Single-Donor Human Hepatocytes Lot HH1086)
4214
373732032023
LRKLRKRLLRLVGRQLEEFL
HM-10/1020FreeFreeLinearLNoneChimeric high-density lipoprotein mimetic peptideAnticancerAt the assay points (time zero, 15, 30, 60,120, and 180 minutes), samples were removed for analysis2 μM (0.5 million cells/mL, of each species pooled together) 5.28Human Hepatocytes Lysates proteaseLC-MS/MSHuman Hepatocytes LysatesIn VitroNoneNoneEnzyme Activity = 3.18 at 2 microMolar of HM1010 (Cytochrome P450 (CYP2B6) Induction in Single-Donor Human Hepatocytes Lot HH1086)
4215
373732032023
LRKLRKRLLRLVGRQLEEFL
HM-10/1020FreeFreeLinearLNoneChimeric high-density lipoprotein mimetic peptideAnticancerAt the assay points (time zero, 15, 30, 60,120, and 180 minutes), samples were removed for analysis2 μM (0.5 million cells/mL, of each species pooled together) 5.28Human Hepatocytes Lysates proteaseLC-MS/MSHuman Hepatocytes LysatesIn VitroNoneNoneEnzyme Activity = 2.06 at 2 microMolar of HM1010 (Cytochrome P450 (CYP3A4) Induction in Single-Donor Human Hepatocytes Lot HH1086)
4216
370941322023
GQWHCTTSFPHHYCLY-Bip
SNIO–CBP16Single nanometer iron oxide and PEG conjugation at N terminalAmidationCyclic (C5-C14 Disulfide Bond)LNoneSINO-CBP productUsed in detection of Liver FibrosisN.A.2 nmol/g animal5.7 ± 1.9 (Elimination Half Life)Mice blood proteaseDynamic T1-weighted MRIMice bloodIn VivoNoneNoneKd = 18.4 µM (Binding affinity of SNIO–CBP toward human type I collagen)
4217
370734942023
pGlu-LTPTPNW(Man)GT
Carmo‐HrTH‐I10pGlu = PyroglutamateAmidationLinearLC‐mannosylated tryptophan residue at position 8Derived from the corpora cardiaca (CC) of the Indian stick insect Carausius morosusHypertrehalosemia In Ligated Stick Insects0, 2‐, 5‐, 10‐and 30 min at Room temp100 pmol5C.Morosus hemolymph proteaseHPLCC.Morosus hemolymphIn VitroNoneNone[Lipid]T0 min(µg/µL) = 9.32 ± 1.59 for Natural Carmo‐HrTH‐I (10 pmol) (Biological activity of a crude methanolic extract of corpora cardiaca (CC) from the natural hypertrehalosemic hormones (HrTHs) extracted from the CC of the Indian stick insect(Carausius morosus) in an in vivo bioassay withL. migratoria)
4218
370475882023
VIKLSGRELVRAQIAISGMSTWSKRSL
B7-3327FreeFreeLinearLNoneDerived as a single-chain peptidomimetic of the B-chain of H2 relaxinTreatment of Acute Cardiac FailureA total of 80 µL of samples was removed at various time points (0 min, 30 min, 60 min, 120 min, 240 min, and 480 min)400 µg/mL6Human serum proteaseRP-HPLCHuman serumIn VitroNoneNoneHEK-7BP Binding B.S.A. Free Eu-H2 pKi = 7.28 ± 0.11
4219
370475882023
VIKLSGRELVRAQIAISGMSTWSKRSL
AcK(PalmGlu)-PEG12-B7-3327Ac modifed Lysine in Palmitic fatty acid linked with B7-33 using PEG linkerFreeLinearLNoneB7-33 analogTreatment of Acute Cardiac FailureA total of 80 µL of samples was removed at various time points (0 min, 30 min, 60 min, 120 min, 240 min, and 480 min)400 µg/mL60Human serum proteaseRP-HPLCHuman serumIn VitroNoneNoneHEK-7BP Binding B.S.A. Free Eu-H2 pKi =7.52 ± 0.13
4220
369899422023
H-Aib-EGTFTSDVSSYLEGQAAKEFIAWLVRGRG
Semaglutide31FreeFreeLinearLAib modification at position 2, Lys20 side chain conjugated with (ADO-linker-Glu-C18)GLP-1 analogsAntidiabetes, AntiobesityN.A.N.A.7.22 - 9.26 Rats plasma proteaseLC-MS/MSRats plasmaIn VivoPubChem CID: 56843331NoneN.A.
4221
369827732023
CRGDKGPDC
CEND-19FreeFreeCyclic (C1-C9 Disulfide Bond)LNoneiRGD cyclic peptideAntitumorBlood samples were collected for pharmacokinetic evaluations pre-dose and at 1, 5, 10, 15 and 30 min, and 1, 2 and 6 h post-dose in rats, dogs and monkeys, and 3, 10, 30 and 90 min, and 4 and 8 h post-dose in mice1.5 mg/kg0.306Mouse plasma proteaseLC-MS/MSMouse plasmaIn VivoNoneNoneN.A.
4222
369827732023
CRGDKGPDC
CEND-19FreeFreeCyclic (C1-C9 Disulfide Bond)LNoneiRGD cyclic peptideAntitumorBlood samples were collected for pharmacokinetic evaluations pre-dose and at 1, 5, 10, 15 and 30 min, and 1, 2 and 6 h post-dose in rats, dogs and monkeys, and 3, 10, 30 and 90 min, and 4 and 8 h post-dose in mice4.5 mg/kg0.344Mouse plasma proteaseLC-MS/MSMouse plasmaIn VivoNoneNoneN.A.
4223
369827732023
CRGDKGPDC
CEND-19FreeFreeCyclic (C1-C9 Disulfide Bond)LNoneiRGD cyclic peptideAntitumorBlood samples were collected for pharmacokinetic evaluations pre-dose and at 1, 5, 10, 15 and 30 min, and 1, 2 and 6 h post-dose in rats, dogs and monkeys, and 3, 10, 30 and 90 min, and 4 and 8 h post-dose in mice13.5 mg/kg0.547Mouse plasma proteaseLC-MS/MSMouse plasmaIn VivoNoneNoneN.A.
4224
369827732023
CRGDKGPDC
CEND-19FreeFreeCyclic (C1-C9 Disulfide Bond)LNoneiRGD cyclic peptideAntitumorBlood samples were collected for pharmacokinetic evaluations pre-dose and at 1, 5, 10, 15 and 30 min, and 1, 2 and 6 h post-dose in rats, dogs and monkeys, and 3, 10, 30 and 90 min, and 4 and 8 h post-dose in mice1 mg/kg0.805Rats plasma proteaseLC-MS/MSRats plasmaIn VivoNoneNoneN.A.
4225
369827732023
CRGDKGPDC
CEND-19FreeFreeCyclic (C1-C9 Disulfide Bond)LNoneiRGD cyclic peptideAntitumorBlood samples were collected for pharmacokinetic evaluations pre-dose and at 1, 5, 10, 15 and 30 min, and 1, 2 and 6 h post-dose in rats, dogs and monkeys, and 3, 10, 30 and 90 min, and 4 and 8 h post-dose in mice1 mg/kg0.248Rats plasma proteaseLC-MS/MSRats plasmaIn VivoNoneNoneN.A.
4226
369827732023
CRGDKGPDC
CEND-19FreeFreeCyclic (C1-C9 Disulfide Bond)LNoneiRGD cyclic peptideAntitumorBlood samples were collected for pharmacokinetic evaluations pre-dose and at 1, 5, 10, 15 and 30 min, and 1, 2 and 6 h post-dose in rats, dogs and monkeys, and 3, 10, 30 and 90 min, and 4 and 8 h post-dose in mice5 mg/kg0.46Rats plasma proteaseLC-MS/MSRats plasmaIn VivoNoneNoneN.A.
4227
369827732023
CRGDKGPDC
CEND-19FreeFreeCyclic (C1-C9 Disulfide Bond)LNoneiRGD cyclic peptideAntitumorBlood samples were collected for pharmacokinetic evaluations pre-dose and at 1, 5, 10, 15 and 30 min, and 1, 2 and 6 h post-dose in rats, dogs and monkeys, and 3, 10, 30 and 90 min, and 4 and 8 h post-dose in mice5 mg/kg0.437Rats plasma proteaseLC-MS/MSRats plasmaIn VivoNoneNoneN.A.
4228
369827732023
CRGDKGPDC
CEND-19FreeFreeCyclic (C1-C9 Disulfide Bond)LNoneiRGD cyclic peptideAntitumorBlood samples were collected for pharmacokinetic evaluations pre-dose and at 1, 5, 10, 15 and 30 min, and 1, 2 and 6 h post-dose in rats, dogs and monkeys, and 3, 10, 30 and 90 min, and 4 and 8 h post-dose in mice75 mg/kg0.341Rats plasma proteaseLC-MS/MSRats plasmaIn VivoNoneNoneN.A.
4229
369827732023
CRGDKGPDC
CEND-19FreeFreeCyclic (C1-C9 Disulfide Bond)LNoneiRGD cyclic peptideAntitumorBlood samples were collected for pharmacokinetic evaluations pre-dose and at 1, 5, 10, 15 and 30 min, and 1, 2 and 6 h post-dose in rats, dogs and monkeys, and 3, 10, 30 and 90 min, and 4 and 8 h post-dose in mice75 mg/kg0.391Rats plasma proteaseLC-MS/MSRats plasmaIn VivoNoneNoneN.A.
4230
369827732023
CRGDKGPDC
CEND-19FreeFreeCyclic (C1-C9 Disulfide Bond)LNoneiRGD cyclic peptideAntitumorBlood samples were collected for pharmacokinetic evaluations pre-dose and at 1, 5, 10, 15 and 30 min, and 1, 2 and 6 h post-dose in rats, dogs and monkeys, and 3, 10, 30 and 90 min, and 4 and 8 h post-dose in mice1 mg/kg0.665Dogs plasma proteaseLC-MS/MSDogs plasmaIn VivoNoneNoneN.A.
4231
369827732023
CRGDKGPDC
CEND-19FreeFreeCyclic (C1-C9 Disulfide Bond)LNoneiRGD cyclic peptideAntitumorBlood samples were collected for pharmacokinetic evaluations pre-dose and at 1, 5, 10, 15 and 30 min, and 1, 2 and 6 h post-dose in rats, dogs and monkeys, and 3, 10, 30 and 90 min, and 4 and 8 h post-dose in mice1 mg/kg0.668Dogs plasma proteaseLC-MS/MSDogs plasmaIn VivoNoneNoneN.A.
4232
369827732023
CRGDKGPDC
CEND-19FreeFreeCyclic (C1-C9 Disulfide Bond)LNoneiRGD cyclic peptideAntitumorBlood samples were collected for pharmacokinetic evaluations pre-dose and at 1, 5, 10, 15 and 30 min, and 1, 2 and 6 h post-dose in rats, dogs and monkeys, and 3, 10, 30 and 90 min, and 4 and 8 h post-dose in mice5 mg/kg0.655Dogs plasma proteaseLC-MS/MSDogs plasmaIn VivoNoneNoneN.A.
4233
369827732023
CRGDKGPDC
CEND-19FreeFreeCyclic (C1-C9 Disulfide Bond)LNoneiRGD cyclic peptideAntitumorBlood samples were collected for pharmacokinetic evaluations pre-dose and at 1, 5, 10, 15 and 30 min, and 1, 2 and 6 h post-dose in rats, dogs and monkeys, and 3, 10, 30 and 90 min, and 4 and 8 h post-dose in mice5 mg/kg0.648Dogs plasma proteaseLC-MS/MSDogs plasmaIn VivoNoneNoneN.A.
4234
369827732023
CRGDKGPDC
CEND-19FreeFreeCyclic (C1-C9 Disulfide Bond)LNoneiRGD cyclic peptideAntitumorBlood samples were collected for pharmacokinetic evaluations pre-dose and at 1, 5, 10, 15 and 30 min, and 1, 2 and 6 h post-dose in rats, dogs and monkeys, and 3, 10, 30 and 90 min, and 4 and 8 h post-dose in mice75 mg/kg0.615Dogs plasma proteaseLC-MS/MSDogs plasmaIn VivoNoneNoneN.A.
4235
369827732023
CRGDKGPDC
CEND-19FreeFreeCyclic (C1-C9 Disulfide Bond)LNoneiRGD cyclic peptideAntitumorBlood samples were collected for pharmacokinetic evaluations pre-dose and at 1, 5, 10, 15 and 30 min, and 1, 2 and 6 h post-dose in rats, dogs and monkeys, and 3, 10, 30 and 90 min, and 4 and 8 h post-dose in mice75 mg/kg0.62Dogs plasma proteaseLC-MS/MSDogs plasmaIn VivoNoneNoneN.A.
4236
369827732023
CRGDKGPDC
CEND-19FreeFreeCyclic (C1-C9 Disulfide Bond)LNoneiRGD cyclic peptideAntitumorBlood samples were collected for pharmacokinetic evaluations pre-dose and at 1, 5, 10, 15 and 30 min, and 1, 2 and 6 h post-dose in rats, dogs and monkeys, and 3, 10, 30 and 90 min, and 4 and 8 h post-dose in mice5 mg/kg0.888Monkeys Plasma ProteaseLC-MS/MSMonkeys plasma In VivoNoneNoneN.A.
4237
369827732023
CRGDKGPDC
CEND-19FreeFreeCyclic (C1-C9 Disulfide Bond)LNoneiRGD cyclic peptideAntitumorBlood samples were collected for pharmacokinetic evaluations pre-dose and at 1, 5, 10, 15 and 30 min, and 1, 2 and 6 h post-dose in rats, dogs and monkeys, and 3, 10, 30 and 90 min, and 4 and 8 h post-dose in mice50 mg/kg0.956Monkeys Plasma ProteaseLC-MS/MSMonkeys plasma In VivoNoneNoneN.A.
4238
369827732023
CRGDKGPDC
CEND-19FreeFreeCyclic (C1-C9 Disulfide Bond)LNoneiRGD cyclic peptideAntitumor1 day3.2 mg/kg1.956Human plasma proteaseN.A.Human plasmaIn VivoNoneNoneN.A.
4239
369827732023
CRGDKGPDC
CEND-19FreeFreeCyclic (C1-C9 Disulfide Bond)LNoneiRGD cyclic peptideAntitumorplasma samples were collected from patients before the CEND-1 infusion and at 3 min (±1 min), 15 min (±3 min), 30 min (±3 min), 1 hour (±5 min), ¾ h (±10 min) and 6/8 h (±10 min) after completion of the infusion (cycle 1 day 1 of nab-paclitaxel+gemcitabine chemotherapy treatment) (Combination therapy after 7 days of run in therapy)3.2 mg/kg1.725Human plasma proteaseN.A.Human plasma after nab-paclitaxel and gemcitabineIn VivoNoneNoneN.A.
4240
369827732023
CRGDKGPDC
CEND-19FreeFreeCyclic (C1-C9 Disulfide Bond)LNoneiRGD cyclic peptideAntitumorplasma samples were collected from patients before the CEND-1 infusion and at 3 min (±1 min), 15 min (±3 min), 30 min (±3 min), 1 hour (±5 min), ¾ h (±10 min) and 6/8 h (±10 min) after completion of the infusion (cycle 1 day 1 of nab-paclitaxel+gemcitabine chemotherapy treatment) (Combination therapy after 7 days of run in therapy)3.2 mg/kg1.598Human plasma proteaseLC-MS/MSHuman plasma after nab-paclitaxel and gemcitabineIn VivoNoneNoneN.A.
4241
369020212023
RNWELRLK-(PEG)4-RNWELRLK-(PEG)4
PDC16FreePEG4 spacer was designed and subsequently reacted with a cysteine at the carboxyl terminus then, the elongated thiol-modified homodimer peptide was conjugated with DOXLinearLNoneHER2-targeting peptide–DOX conjugateAntitumorThe PDC was incubated with human plasma (final peptide concentration of 50 μM) for 0, 2, 4, 8, 12, 24, and 48 h 50 μM24Human plasma proteaseHPLCHuman plasmaIn VitroNoneNoneThe IC50 value for the PDC (Peptide-Drug Conjugate) is 140 nM. This value indicates that the PDC is more potent in killing HER2-positive SKBR-3 cells compared to free DOX, which has an IC50 of 410 nM
4242
368731812023
DH-α-(4-pentenyl)-Ala-NPQIR
DR3penA8FreeAmidationLinearLα-(4-pentenyl)-Ala introduced at positions 3 of DR8 DR8 analogAlleviates Pulmonary FibrosisSamples were taken from the mixture at 0, 15, 30, 60, 120 and 240 min10 mmol/L174.63 ± 31.66Mice serum proteaseRP-HPLCC57BL/6 mice serumIn VitroNoneNoneDR3penA has Minimum effective concentration is 2.5 μmol/L in both TGF-β1-induced NIH3T3 cells and A549 cells
4243
368731812023
DHN-α-(4-pentenyl)-Ala-PQIR
DR4penA8FreeAmidationLinearLα-(4-pentenyl)-Ala introduced at positions 4 of DR8 DR8 analogAlleviates Pulmonary FibrosisSamples were taken from the mixture at 0, 15, 30, 60, 120 and 240 min10 mmol/L270.65 ± 16.43Mice serum proteaseRP-HPLCC57BL/6 mice serumIn VitroNoneNoneDR8 has Minimum effective concentrations are 20 μmol/L in TGF-β1-induced NIH3T3 cells and 10 μmol/L in A549 cells
4244
367808992023
SWMEEVIKLCGRELVRAQIAICGMSTWSXGGGSGGSGGGQLYSALANKCCHVGCTKRSLARFCX
LY354037864FreeRelaxin-A chain linked with albVHH domain at C terminus, A and B chain linked by linkerLinearLNonerelaxin-2 analogTreatment of Chronic Heart FailureN.A.200 nmol/kg36.4 (Terminal Half Life)Rats plasma proteaseLC-MSRats plasmaIn VivoNoneNoneEC 50 (nM) = 109 ± 24 of LY3540378 in Rat RXFP2
4245
367808992023
SWMEEVIKLCGRELVRAQIAICGMSTWSXGGGSGGSGGGQLYSALANKCCHVGCTKRSLARFCX
LY354037864FreeRelaxin-A chain linked with albVHH domain at C terminus, A and B chain linked by linkerLinearLNonerelaxin-2 analogTreatment of Chronic Heart FailureN.A.100 nmol/kg124 (Terminal Half Life)Cynomolgus monkeys plasma proteaseLC-MSCynomolgus monkeys plasmaIn VivoNoneNoneEC 50 (nM) = 19.3 ± 4.0 of LY3540378 in Cynomolgus monkey RXFP2
4246
367808992023
SWMEEVIKLCGRELVRAQIAICGMSTWSXGGGSGGSGGGQLYSALANKCCHVGCTKRSLARFCX
LY354037864FreeRelaxin-A chain linked with albVHH domain at C terminus, A and B chain linked by linkerLinearLNonerelaxin-2 analogTreatment of Chronic Heart FailureN.A.100 nmol/kg45.7 (Terminal Half Life)Cynomolgus monkeys plasma proteaseLC-MSCynomolgus monkeys plasmaIn VivoNoneNoneEC 50 (nM) = 19.3 ± 4.0 of LY3540378 in Cynomolgus monkey RXFP2
4247
367808992023
SWMEEVIKLCGRELVRAQIAICGMSTWSXGGGSGGSGGGQLYSALANKCCHVGCTKRSLARFCX
LY354037864FreeRelaxin-A chain linked with albVHH domain at C terminus, A and B chain linked by linkerLinearLNonerelaxin-2 analogTreatment of Chronic Heart FailureN.A.30 nmol/kg39.7 ± 1.8 (Terminal Half Life)SD rats plasma proteaseLC-MSSD rats plasmaIn VivoNoneNoneEC 50 (nM) = 109 ± 24 of LY3540378 in Rat RXFP2
4248
367807862023
HADGSFSDEMNTILDNLAAKDFIAWLIQTKITD
hGLP-2 (variant 6)33FreeFreeLinearLAddition of a C16 monoacid at position 20 of the hGLP-2 peptideProglucagon-derived intestinal hormoneAntiapoptosis, Antiinflammatory Blood samples were drawn from the tail at t = 0.5, 1, 2, 4, 8, 12, 24, 36, and 48 h400 µg/kg9.5Female SD rats plasma proteaseRIAFemale SD rats plasma In VivoNoneNoneEC50 = 0.44 nM for hGLP-2R in the presence of 1% HSA
4249
367193262023
RGDfK
68Ga(AAZ3A-endoHB)-c(RGD)5Ga labelling, conjugation of AAZ3A-endoHB-NCS to c(RGD)(cyclo(Arg-Gly-Asp-D-Phe-Lys) peptide at N terminusFreeCyclic (RGDfK)MixNoneSyntheticPositron Emission Tomography (PET) imaging37 °CN.A.Stable upto 4 hourHuman serum proteaseUPLC-UV-RAHuman serum In VitroNoneNoneN.A.
4250
366319712023
VDKPPYLPRPRPPROIYNO
Onc7219FreeAmidation, Orn=Ornithine at position 19LinearLOrn=Ornithine at position 15OncocinsAntimicrobialProdrug and Onc72 concentrations were determined 5 min, 15 min, 30 min, 1 h, 2 h, 4 h, 8 h, and 24 h postadministration4.34 mmol/kg43CD-1 mice plasma proteaseLC-MSCD-1 mice plasma In VivoNoneNone(Onc72 in 19% MHB2 medium) MIC = 12.5 μmol L−1 (29 mg L−1) on E.coli BW25113
4251
366319712023
VDKPPYLPRPRPPROIYNO
Onc7219FreeAmidation, Orn=Ornithine at position 19LinearLOrn=Ornithine at position 15OncocinsAntimicrobialProdrug and Onc72 concentrations were determined 5 min, 15 min, 30 min, 1 h, 2 h, 4 h, 8 h, and 24 h postadministration4.34 mmol/kg43CD-1 mice plasma proteaseLC-MSCD-1 mice plasma In VivoNoneNone(Onc72 in 25% mouse serum ) MIC = 25 μmol L−1 (58 mg L−1) on E.coli BW25113
4252
366319712023
VDKPPYLPRPRPPROIYNO
Onc7219FreeAmidation, Orn=Ornithine at position 19LinearLOrn=Ornithine at position 15OncocinsAntimicrobialProdrug and Onc72 concentrations were determined 5 min, 15 min, 30 min, 1 h, 2 h, 4 h, 8 h, and 24 h postadministration4.34 mmol/kg43CD-1 mice plasma proteaseLC-MSCD-1 mice plasma In VivoNoneNoneOnc72 Showed negligible hemolytic activity (below 0.2%) up to the highest tested concentration (50 μmol L−1), similar to the negative control (PBS)
4253
366319712023
VDKPPYLPRPRPPROIYNO
Onc7219FreeAmidation, Orn=Ornithine at position 19LinearLOrn=Ornithine at position 15OncocinsAntimicrobialProdrug and Onc72 concentrations were determined 5 min, 15 min, 30 min, 1 h, 2 h, 4 h, 8 h, and 24 h postadministration4.34 mmol/kg43CD-1 mice plasma proteaseLC-MSCD-1 mice plasma In VivoNoneNoneOnc72: Non-toxic to human HepG2 and HEK293 cell lines at 50 μmol L−1
4254
366319712023
LVPRVDKPPYLPRPRPPROIYNO
5k-prodrug23Onc72 N-terminally coupled via a short peptide linker LVPR to 5 kDa thiol PEGsAmidation, Orn at position 23LinearLOrn at postion 19OncocinsAntimicrobialProdrug and Onc72 concentrations were determined 5 min, 15 min, 30 min, 1 h, 2 h, 4 h, 8 h, and 24 h postadministration4.34 mmol/kg66CD-1 mice plasma proteasecELISACD-1 mice plasma In VivoNoneNone(Prodrugs of Onc72) MIC values >50 μmol L−1 on E.coli BW25113
4255
366319712023
LVPRVDKPPYLPRPRPPROIYNO
5k-prodrug23Onc72 N-terminally coupled via a short peptide linker LVPR to 5 kDa thiol PEGsAmidation, Orn at position 23LinearLOrn at postion 19OncocinsAntimicrobialProdrug and Onc72 concentrations were determined 5 min, 15 min, 30 min, 1 h, 2 h, 4 h, 8 h, and 24 h postadministration4.34 mmol/kg66CD-1 mice plasma proteasecELISACD-1 mice plasma In VivoNoneNoneProdrugs Showed negligible hemolytic activity (below 0.2%) up to the highest tested concentration (50 μmol L−1), similar to the negative control (PBS)
4256
366319712023
LVPRVDKPPYLPRPRPPROIYNO
5k-prodrug23Onc72 N-terminally coupled via a short peptide linker LVPR to 5 kDa thiol PEGsAmidation, Orn at position 23LinearLOrn at postion 19OncocinsAntimicrobialProdrug and Onc72 concentrations were determined 5 min, 15 min, 30 min, 1 h, 2 h, 4 h, 8 h, and 24 h postadministration4.34 mmol/kg66CD-1 mice plasma proteasecELISACD-1 mice plasma In VivoNoneNone5 kDa thiol-PEG: Reduced cell viability to ≈89% for both HepG2 and HEK293 cell lines
4257
366319712023
LVPRVDKPPYLPRPRPPROIYNO
20k-prodrug23Onc72 N-terminally coupled via a short peptide linker LVPR to 20 kDa thiol PEGsAmidation, Orn at position 23LinearLOrn at postion 19OncocinsAntimicrobialProdrug and Onc72 concentrations were determined 5 min, 15 min, 30 min, 1 h, 2 h, 4 h, 8 h, and 24 h postadministration4.34 mmol/kg324CD-1 mice plasma proteasecELISACD-1 mice plasma In VivoNoneNone(Prodrugs of Onc72) MIC values >50 μmol L−1 on E.coli BW25113
4258
366319712023
LVPRVDKPPYLPRPRPPROIYNO
20k-prodrug23Onc72 N-terminally coupled via a short peptide linker LVPR to 20 kDa thiol PEGsAmidation, Orn at position 23LinearLOrn at postion 19OncocinsAntimicrobialProdrug and Onc72 concentrations were determined 5 min, 15 min, 30 min, 1 h, 2 h, 4 h, 8 h, and 24 h postadministration4.34 mmol/kg324CD-1 mice plasma proteasecELISACD-1 mice plasma In VivoNoneNoneProdrugs Showed negligible hemolytic activity (below 0.2%) up to the highest tested concentration (50 μmol L−1), similar to the negative control (PBS)
4259
366319712023
LVPRVDKPPYLPRPRPPROIYNO
20k-prodrug23Onc72 N-terminally coupled via a short peptide linker LVPR to 20 kDa thiol PEGsAmidation, Orn at position 23LinearLOrn at postion 19OncocinsAntimicrobialProdrug and Onc72 concentrations were determined 5 min, 15 min, 30 min, 1 h, 2 h, 4 h, 8 h, and 24 h postadministration4.34 mmol/kg324CD-1 mice plasma proteasecELISACD-1 mice plasma In VivoNoneNone20 kDa thiol-PEG: Reduced cell viability more significantly, to ≈70% for both cell lines
4260
366319712023
VDKPPYLPRPRPPROIYNO
Onc7219FreeAmidation, Orn=Ornithine at position 19LinearLOrn=Ornithine at position 15SyntheticAntimicrobialAliquots weretaken in triplicates after 0, 1, 2, 4, and 8 h for Onc72 and 0, 4, 8, and 24 hfor both prodrugs31.5 μmol/L≈80Cell lysate protease (Obtained From An E. Coli Bw25113 Culture)RP-HPLCE. coli BW25113 cell lysateIn VitroNoneNone(Onc72 in 19% MHB2 medium) MIC = 12.5 μmol L−1 (29 mg L−1) on E.coli BW25113
4261
366319712023
LVPRVDKPPYLPRPRPPROIYNO
5k-prodrug23Onc72 N-terminally coupled via a short peptide linker LVPR to 5 kDa thiol PEGsAmidation, Orn at position 23LinearLOrn at postion 19SyntheticAntimicrobial0, 4, 8, 16, and 24 h aliquots (47.5 μL) were taken in triplicates31.5 μmol/L8Mouse serum proteaseSerum stability assayMouse serumIn VivoNoneNone5 kDa thiol-PEG: Reduced cell viability to ≈89% for both HepG2 and HEK293 cell lines
4262
366319712023
LVPRVDKPPYLPRPRPPROIYNO
20k-prodrug23Onc72 N-terminally coupled via a short peptide linker LVPR to 20 kDa thiol PEGsAmidation, Orn at position 23LinearLOrn at postion 19SyntheticAntimicrobial0, 4, 8, 16, and 24 h aliquots (47.5 μL) were taken in triplicates31.5 μmol/L14Mouse serum proteaseSerum stability assayMouse serumIn VivoNoneNone20 kDa thiol-PEG: Reduced cell viability more significantly, to ≈70% for both cell lines
4263
366308262023
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
Exendin-439FreeAmidationLinearLFluorescently labeledIsolated from the saliva of the Gila monster lizard (Heloderma suspectum)AntidiabetesBlood collection at 5-min, 1-, 2-, 4-, 8-, 24-, 48-, 72-, 96-, 120-, 144- and 168-h1000 nmol kg−12.12 ± 0.3 (T1/2 Elimination)Naïve mice plasma proteaseFluorescence assayNaïve mice plasmaIn VivoPDB id: 7MLLNoneEC50 = 0.04 ± 0.01 nM for exendin
4264
366308262023
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
Ex-PEGRh(4.4 ± 1.1nm)39FreePEGylation (Rh(4.4 ± 1.1nm)) and linked via DBCOLinearLFluorescently labeledExendin-4 analogsAntidiabetesBlood collection at 5-min, 1-, 2-, 4-, 8-, 24-, 48-, 72-, 96-, 120-, 144- and 168-h1000 nmol kg−123.14 ± 3.2(T1/2 Elimination)Naïve mice plasma proteaseFluorescence assayNaïve mice plasmaIn VivoNoneNoneEC50 = 1.3 ± 0.2 nM
4265
366308262023
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
Ex-PEGMw(46.3KDa)39FreePEGylation (Mw(46.3KDa)) and linked via DBCOLinearLFluorescently labeledExendin-4 analogsAntidiabetesBlood collection at 5-min, 1-, 2-, 4-, 8-, 24-, 48-, 72-, 96-, 120-, 144- and 168-h1000 nmol kg−134.91 ± 4.5(T1/2 Elimination)Naïve mice plasma proteaseFluorescence assayNaïve mice plasmaIn VivoNoneNoneEC50 = 2.7 ± 0.5 nM
4266
366308262023
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
Ex-POEGMAopt(54.7KDa)39FreePOEGMA (poly[oligo(ethylene glycol) methyl ether methacrylate]) conjugation (MW opt = 54.7KDa)LinearLFluorescently labeledExendin-4 analogsAntidiabetesBlood collection at 5-min, 1-, 2-, 4-, 8-, 24-, 48-, 72-, 96-, 120-, 144- and 168-h1000 nmol kg−197.3 ± 3.2(T1/2 Elimination)Naïve mice plasma proteaseFluorescence assayNaïve mice plasmaIn VivoNoneNoneEC50 = 2.8 ± 0.7 nM
4267
366308262023
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
Exendin-439FreeAmidationLinearLFluorescently labeledIsolated from the saliva of the Gila monster lizard (Heloderma suspectum)AntidiabetesBlood collection at 5-min, 1-, 2-, 4-, 8-, 24-, 48-, 72-, 96-, 120-, 144- and 168-h1000 nmol kg−11.88 ± 0.2(T1/2 Elimination)Naïve mice plasma proteaseFluorescence assayNaïve mice plasmaIn VivoPDB id: 7MLLNoneEC50 = 0.04 ± 0.01 nM for exendin
4268
366308262023
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
Ex-PEGRh(4.4 ± 1.1nm)39FreePEGylation (Rh(4.4 ± 1.1nm)) and linked via DBCOLinearLFluorescently labeledExendin-4 analogsAntidiabetesBlood collection at 5-min, 1-, 2-, 4-, 8-, 24-, 48-, 72-, 96-, 120-, 144- and 168-h1000 nmol kg−111.9 ± 2.7 (T1/2 Elimination)Immunized mice plasma proteaseFluorescence assayImmunized mice plasmaIn VivoNoneNoneEC50 = 1.3 ± 0.2 nM
4269
366308262023
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
Ex-POEGMAopt(54.7KDa)39FreePOEGMA (poly[oligo(ethylene glycol) methyl ether methacrylate]) conjugation (MW opt = 54.7KDa)LinearLFluorescently labeledExendin-4 analogsAntidiabetesBlood collection at 5-min, 1-, 2-, 4-, 8-, 24-, 48-, 72-, 96-, 120-, 144- and 168-h1000 nmol kg−112.1 ± 1.0 (T1/2 Elimination)Immunized mice plasma proteaseFluorescence assayImmunized mice plasmaIn VivoNoneNoneEC50 = 2.8 ± 0.7 nM
4270
366308262023
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
Ex-POEGMAopt(54.7KDa)39FreePOEGMA (poly[oligo(ethylene glycol) methyl ether methacrylate]) conjugation (MW opt = 54.7KDa)LinearLFluorescently labeledExendin-4 analogsAntidiabetesBlood collection at 5-min, 1-, 2-, 4-, 8-, 24-, 48-, 72-, 96-, 120-, 144- and 168-h1000 nmol kg−1105.7 ± 6 (T1/2 Elimination)Immunized mice plasma proteaseFluorescence assayImmunized mice plasmaIn VivoNoneNoneEC50 = 2.8 ± 0.7 nM
4271
365954402023
(y-D-Glu)-(4S)-aminoproline-LEX
TP0597850 (18)4Tripeptide linker {5-aminopentanoic acid [Ape(5)]–Glu–Asp} of 1 was replaced by a shorter linker (γ-D-Glu), X = Structure given in paperFreeLinearLX=Structure given in paperSyntheticMMP2 InhibitorsN.A.N.A.265N.A.N.A.N.A.N.A.NoneNoneKi = 0.034 nM for MM2 inhibition
4272
365092202023
KLLKINLKALAALAKKIL
KM8 18FreeAmidationLinearLNoneAnalogue of MastoparanAntitumorN.A.N.A.30Mouse plasma proteasePlasma stability assayMouse plasmaIn VivoNoneNoneN.A.
4273
364107922023
HGDGSFSDEMNTILDNLAARDFINWLIQTKITD
Teduglutide33FreeFreeLinearLNoneGLP-2 analogueSmall Bowel Hypertrophic EffectBlood (0.3 ml) was then collected from the jugularvein at 0.25, 0.5, 1, 1.5, 2, 3, 4, 6, and 8 hours for teduglutide and 1, 4, 8, 24, 48, 72, 96, 230, 244, 268, 192, 216, 240, 264, 288, 312, and 336 hours for HM15912670 nmol/kg0.6 ± 0.1SD rats serum proteaseGLP-2 ELISASD rats serumIn VivoNoneNoneEC50 = 0.12 ± 0.056 nM for teduglutide peptide (In vitro potency of GLP-2 analogs on human GLP-2 receptor in cell-based functional assays of dose-response cAMP)
4274
364107922023
GDGSFSDEMNTILDNLAARDFINWLIQTRITDK
HM1591234[(1H-imidazol-4-yl)-acetyl 1]Conjugation of GT15912 and hIgG4 Fc was carried out through the formation of amine bonds between the bi functional PEG and Lys34 in GT15912 or the N-terminal amino acid in hIgG4 FcLinearLNoneGLP-2 analogueSmall Bowel Hypertrophic EffectBlood (0.3 ml) was then collected from the jugularvein at 0.25, 0.5, 1, 1.5, 2, 3, 4, 6, and 8 hours for teduglutide and 1, 4, 8, 24, 48, 72, 96, 230, 244, 268, 192, 216, 240, 264, 288, 312, and 336 hours for HM1591213 nmol/kg42.3 ± 3.4SD rats serum proteaseGLP-2 ELISASD rats serumIn VivoNoneNoneEC50 = 0.327 ± 0.096 nM for HM15912 peptide (In vitro potency of GLP-2 analogs on human GLP-2 receptor in cell-based functional assays of dose-response cAMP)
4275
366308262023
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
Exendin39Fluorescently labelledAmidationLinearLNoneDerived from Gila monsterAntidiabetesTen μl of blood was collected from a tiny incision on the tail vein into tubes containing 90 μl of 1,000 U ml-1 heparin (Sigma) at 5-min, 1-, 2-, 4-, 8-, 24-, 48-, 72-, 96-, 120-, 144- and 168-h. 1000 nmol/kg2.12 ± 0.3 (T1/2 Elimination) Naïve mice plasma proteasefluorescence assayNaïve mice plasmaIn VivoPDB id: 7MLLNoneEC50 (nM) = 0.04 ± 0.01
4276
366308262023
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
Ex-PEGRh 39Fluorescently labelledExendin-DBCO was conjugated to azide-functional PEG(27.7KDa)LinearLNoneExendin-4 analogsAntidiabetesTen μl of blood was collected from a tiny incision on the tail vein into tubes containing 90 μl of 1,000 U ml-1 heparin (Sigma) at 5-min, 1-, 2-, 4-, 8-, 24-, 48-, 72-, 96-, 120-, 144- and 168-h. 1000 nmol/kg23.14 ± 3.2 (T1/2 Elimination) Naïve mice plasma proteasefluorescence assayNaïve mice plasmaIn VivoNoneNoneEC50 (nM) = 1.3 ± 0.2
4277
366308262023
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
Ex-PEGMw 39Fluorescently labelledExendin-DBCO was conjugated to azide-functional PEG(46.3 KDa)LinearLNoneExendin-4 analogsAntidiabetesTen μl of blood was collected from a tiny incision on the tail vein into tubes containing 90 μl of 1,000 U ml-1 heparin (Sigma) at 5-min, 1-, 2-, 4-, 8-, 24-, 48-, 72-, 96-, 120-, 144- and 168-h. 1000 nmol/kg34.91 ± 4.5 (T1/2 Elimination) Naïve mice plasma proteasefluorescence assayNaïve mice plasmaIn VivoNoneNoneEC50 (nM) = 2.7 ± 0.5
4278
366308262023
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
Ex-POEGMAopt 39Fluorescently labelledExendin-DBCO was conjugated to azide-functional POEGMA(54.7KDa)LinearLNoneExendin-4 analogsAntidiabetesTen μl of blood was collected from a tiny incision on the tail vein into tubes containing 90 μl of 1,000 U ml-1 heparin (Sigma) at 5-min, 1-, 2-, 4-, 8-, 24-, 48-, 72-, 96-, 120-, 144- and 168-h. 1000 nmol/kg97.3 ± 3.2 (T1/2 Elimination) Naïve mice plasma proteasefluorescence assayNaïve mice plasmaIn VivoNoneNoneEC50 (nM) = 2.8 ± 0.7
4279
366308262023
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
Exendin 39Fluorescently labelledAmidationLinearLNoneDerived from Gila monsterAntidiabetesTen μl of blood was collected from a tiny incision on the tail vein into tubes containing 90 μl of 1,000 U ml-1 heparin (Sigma) at 5-min, 1-, 2-, 4-, 8-, 24-, 48-, 72-, 96-, 120-, 144- and 168-h. 1000 nmol/kg1.88 ± 0.2 (T1/2 Elimination) Immunized mice plasma proteasefluorescence assayImmunized mice plasmaIn VivoPDB id: 7MLLNoneEC50 (nM) = 0.04 ± 0.01
4280
366308262023
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
Ex-PEGRh 39Fluorescently labelledExendin-DBCO was conjugated to azide-functional PEG(27.7KDa)LinearLNoneExendin-4 analogsAntidiabetesTen μl of blood was collected from a tiny incision on the tail vein into tubes containing 90 μl of 1,000 U ml-1 heparin (Sigma) at 5-min, 1-, 2-, 4-, 8-, 24-, 48-, 72-, 96-, 120-, 144- and 168-h. 1000 nmol/kg11.9 ± 2.7 (T1/2 Elimination) Immunized mice plasma proteasefluorescence assayImmunized mice plasmaIn VivoNoneNoneEC50 (nM) = 1.3 ± 0.2
4281
366308262023
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
Ex-POEGMAopt 39Fluorescently labelledExendin-DBCO was conjugated to azide-functional POEGMA(54.7KDa)LinearLNoneExendin-4 analogsAntidiabetesTen μl of blood was collected from a tiny incision on the tail vein into tubes containing 90 μl of 1,000 U ml-1 heparin (Sigma) at 5-min, 1-, 2-, 4-, 8-, 24-, 48-, 72-, 96-, 120-, 144- and 168-h. 1000 nmol/kg105.7 ± 6 (T1/2 Elimination) Immunized mice plasma proteasefluorescence assayImmunized mice plasmaIn VivoNoneNoneEC50 (nM) = 2.8 ± 0.7
4282
N.A.2023
Y-Aib-EGTFISDLSI-Aib-KDRIHQ-Aib-EFIEWLLAQRG
SEQ ID NO 631FreeAmidationLinearLAib = α-aminoisobutyric acidExendin-4 analogsAntidiabetesBlood samples were collected after 0.08, 0.25, 0.5, 1 , 2, 4, 8, 24, 32, And 48 H post I.V. application0.25 mg/kg7.9Mice plasma proteaseLC-MSMice plasmaIn VivoNoneEP 2022074607 WIC50 hGIPR (nM) = 0.5
4283
N.A.2023
Y-Aib-EGTFISDLSI-Aib-KDRIHQ-Aib-EFIEWLLAQRG
SEQ ID NO 631FreeAmidationLinearLAib = α-aminoisobutyric acidExendin-4 analogsAntidiabetesBlood samples were collected after 0.25, 0.5, 1 , 2, 4, 8, 24, 32, and 48 H post S.C. application0.5 mg/kg8.21Mice plasma proteaseLC-MSMice plasmaIn VivoNoneEP 2022074607 WIC50 hGIPR (nM) = 0.5
4284
N.A.2023
Y-Aib-EGT-Iva-ISDLSI-Aib-KDRIHQ-Aib-EFIEWLLAQRG
SEQ ID NO 1631FreeAmidationLinearLAib = α-aminoisobutyric acid, Iva = IsovalineExendin-4 analogsAntidiabetesBlood samples were collected after 0.08, 0.25, 0.5, 1 , 2, 4, 8, 24, 32, and 48 H post I.V. application0.25 mg/kg7.33Mice plasma proteaseLC-MSMice plasmaIn VivoNoneEP 2022074607 WIC50 hGIPR (nM) = 0.1
4285
N.A.2023
Y-Aib-EGT-Iva-ISDLSI-Aib-KDRIHQ-Aib-EFIEWLLAQRG
SEQ ID NO 1631FreeAmidationLinearLAib = α-aminoisobutyric acid, Iva = IsovalineExendin-4 analogsAntidiabetesBlood samples were collected after 0.25, 0.5, 1 , 2, 4, 8, 24, 32, and 48 H post S.C. application0.5 mg/kg5.69Mice plasma proteaseLC-MSMice plasmaIn VivoNoneEP 2022074607 WIC50 hGIPR (nM) = 0.1
4286
N.A.2023
Y-Aib-EGTFISDLSI-Aib-KEEIHQ-Aib-EFIEWLLAQGPSSGAPPPS
SEQ ID NO 1939FreeAmidationLinearLAib = α-aminoisobutyric acidExendin-4 analogsAntidiabetesBlood samples were collected after 0.08, 0.25, 0.5, 1 , 2, 4, 8, 24, 32, and 48 H post I.V. application0.25 mg/kg8.68Mice plasma proteaseLC-MSMice plasmaIn VivoNoneEP 2022074607 WIC50 hGIPR (nM) = 2.0
4287
N.A.2023
Y-Aib-EGTFISDLSI-Aib-KEEIHQ-Aib-EFIEWLLAQGPSSGAPPPS
SEQ ID NO 1939FreeAmidationLinearLAib = α-aminoisobutyric acidExendin-4 analogsAntidiabetesBlood samples were collected after 0.25, 0.5, 1 , 2, 4, 8, 24, 32, and 48 H post S.C. application0.5 mg/kg10.3Mice plasma proteaseLC-MSMice plasmaIn VivoNoneEP 2022074607 WIC50 hGIPR (nM) = 2.0
4288
N.A.2023
Y-Aib-EGTFISDLSI-Aib-KDRIHQEEFIQWLLAQGPSSGAPPPS
SEQ ID NO 3539FreeAmidationLinearLAib = α-aminoisobutyric acidExendin-4 analogsAntidiabetesBlood samples were collected after 0.08, 0.25, 0.5, 1 , 2, 4, 8, 24, 32, and 48 H post I.V. application0.25 mg/kg6.19Mice plasma proteaseLC-MSMice plasmaIn VivoNoneEP 2022074607 WIC50 hGIPR (nM) = 0.6
4289
N.A.2023
Y-Aib-EGTFISDLSI-Aib-KDRIHQEEFIQWLLAQGPSSGAPPPS
SEQ ID NO 3539FreeAmidationLinearLAib = α-aminoisobutyric acidExendin-4 analogsAntidiabetesBlood samples were collected after 0.25, 0.5, 1 , 2, 4, 8, 24, 32, and 48 H post S.C. application0.5 mg/kg6.97Mice plasma proteaseLC-MSMice plasmaIn VivoNoneEP 2022074607 WIC50 hGIPR (nM) = 0.6
4290
N.A.2023
Y-Aib-EGTFISDLSI-Aib-KDRIHQ-Aib-EFIEWLLAQRG
SEQ ID NO 631FreeAmidationLinearLAib = α-aminoisobutyric acidExendin-4 analogsAntidiabetesBlood samples were collected after 0.08, 0.25, 0.5, 1 , 2, 4, 8, 24, 32, and 48 H post I.V. application0.25 mg/kg11.2Rats plasma proteaseLC-MSRats plasmaIn VivoNoneEP 2022074607 WIC50 hGIPR (nM) = 0.5
4291
N.A.2023
Y-Aib-EGTFISDLSI-Aib-KDRIHQ-Aib-EFIEWLLAQRG
SEQ ID NO 631FreeAmidationLinearLAib = α-aminoisobutyric acidExendin-4 analogsAntidiabetesBlood samples were collected after 0.25, 0.5, 1 , 2, 4, 8, 24, 32, and 48 H post S.C. application0.5 mg/kg9.7Rats plasma proteaseLC-MSRats plasmaIn VivoNoneEP 2022074607 WIC50 hGIPR (nM) = 0.5
4292
N.A.2023
Y-Aib-EGT-Iva-ISDLSI-Aib-KDRIHQ-Aib-EFIEWLLAQRG
SEQ ID NO 1631FreeAmidationLinearLAib = α-aminoisobutyric acid, Iva = IsovalineExendin-4 analogsAntidiabetesBlood samples were collected after 0.08, 0.25, 0.5, 1 , 2, 4, 8, 24, 32, and 48 H post I.V. application0.25 mg/kg11.5Rats plasma proteaseLC-MSRats plasmaIn VivoNoneEP 2022074607 WIC50 hGIPR (nM) = 0.1
4293
N.A.2023
Y-Aib-EGT-Iva-ISDLSI-Aib-KDRIHQ-Aib-EFIEWLLAQRG
SEQ ID NO 1631FreeAmidationLinearLAib = α-aminoisobutyric acid, Iva = IsovalineExendin-4 analogsAntidiabetesBlood samples were collected after 0.25, 0.5, 1 , 2, 4, 8, 24, 32, and 48 H post S.C. application0.5 mg/kg10.8Rats plasma proteaseLC-MSRats plasmaIn VivoNoneEP 2022074607 WIC50 hGIPR (nM) = 0.1
4294
N.A.2023
Y-Aib-EGTFISDLSI-Aib-KEEIHQ-Aib-EFIEWLLAQGPSSGAPPPS
SEQ ID NO 1939FreeAmidationLinearLAib = α-aminoisobutyric acidExendin-4 analogsAntidiabetesBlood samples were collected after 0.08, 0.25, 0.5, 1 , 2, 4, 8, 24, 32, and 48 H post I.V. application0.25 mg/kg19.6Rats plasma proteaseLC-MSRats plasmaIn VivoNoneEP 2022074607 WIC50 hGIPR (nM) = 2
4295
N.A.2023
Y-Aib-EGTFISDLSI-Aib-KEEIHQ-Aib-EFIEWLLAQGPSSGAPPPS
SEQ ID NO 1939FreeAmidationLinearLAib = α-aminoisobutyric acidExendin-4 analogsAntidiabetesBlood samples were collected after 0.25, 0.5, 1 , 2, 4, 8, 24, 32, and 48 H post S.C. application0.5 mg/kg20.1Rats plasma proteaseLC-MSRats plasmaIn VivoNoneEP 2022074607 WIC50 hGIPR (nM) = 2
4296
N.A.2023
Y-Aib-EGTFISDLSI-Aib-KERIHQ-Aib-EFIEWLLAQGPSSGAPPPS
SEQ ID NO 2139FreeAmidationLinearLAib = α-aminoisobutyric acidExendin-4 analogsAntidiabetesBlood samples were collected after 0.08, 0.25, 0.5, 1 , 2, 4, 8, 24, 32, and 48 H post I.V. application0.25 mg/kg12.9Rats plasma proteaseLC-MSRats plasmaIn VivoNoneEP 2022074607 WIC50 hGIPR (nM) = 0.8
4297
N.A.2023
Y-Aib-EGTFISDLSI-Aib-KERIHQ-Aib-EFIEWLLAQGPSSGAPPPS
SEQ ID NO 2139FreeAmidationLinearLAib = α-aminoisobutyric acidExendin-4 analogsAntidiabetesBlood samples were collected after 0.25, 0.5, 1 , 2, 4, 8, 24, 32, and 48 H post S.C. application0.5 mg/kg12.1Rats plasma proteaseLC-MSRats plasmaIn VivoNoneEP 2022074607 WIC50 hGIPR (nM) = 0.8
4298
N.A.2023
Y-Aib-EGTFISDLSI-Aib-KDR-Aib-HQ-Aib-EFIEWLLAQRPSSGAPPPS
SEQ ID NO 2239FreeAmidationLinearLAib = α-aminoisobutyric acidExendin-4 analogsAntidiabetesBlood samples were collected after 0.08, 0.25, 0.5, 1 , 2, 4, 8, 24, 32, and 48 H post I.V. application0.25 mg/kg13.6Rats plasma proteaseLC-MSRats plasmaIn VivoNoneEP 2022074607 WIC50 hGIPR (nM) = 1
4299
N.A.2023
Y-Aib-EGTFISDLSI-Aib-KDR-Aib-HQ-Aib-EFIEWLLAQRPSSGAPPPS
SEQ ID NO 2239FreeAmidationLinearLAib = α-aminoisobutyric acidExendin-4 analogsAntidiabetesBlood samples were collected after 0.25, 0.5, 1 , 2, 4, 8, 24, 32, and 48 H post S.C. application0.5 mg/kg15.5Rats plasma proteaseLC-MSRats plasmaIn VivoNoneEP 2022074607 WIC50 hGIPR (nM) = 1
4300
N.A.2023
Y-Aib-EGTFISDLSI-Aib-KDRIHQEEFIQWLLAQGPSSGAPPPS
SEQ ID NO 3539FreeAmidationLinearLAib = α-aminoisobutyric acidExendin-4 analogsAntidiabetesBlood samples were collected after 0.08, 0.25, 0.5, 1 , 2, 4, 8, 24, 32, and 48 H post I.V. application0.25 mg/kg14.5Rats plasma proteaseLC-MSRats plasmaIn VivoNoneEP 2022074607 WIC50 hGIPR (nM) = 0.6
4301
N.A.2023
Y-Aib-EGTFISDLSI-Aib-KDRIHQEEFIQWLLAQGPSSGAPPPS
SEQ ID NO 3539FreeAmidationLinearLAib = α-aminoisobutyric acidExendin-4 analogsAntidiabetesBlood samples were collected after 0.25, 0.5, 1 , 2, 4, 8, 24, 32, and 48 H post S.C. application0.5 mg/kg14.3Rats plasma proteaseLC-MSRats plasmaIn VivoNoneEP 2022074607 WIC50 hGIPR (nM) = 0.6
4302
N.A.2023
Y-Aib-EGTFISDLSI-Aib-KEEIHQ-Aib-EFIEWLLAQGPSSGAPPPS
SEQ ID NO 1939FreeAmidationLinearLAib = α-aminoisobutyric acidExendin-4 analogsAntidiabetesBlood samples were collected at 0 H and after 0.083, 0.25, 0.5, 1 , 2, 4, 8, 24, 32, 48, 56, 72, 80, and 96 H post I.V. application 0.05 mg/kg64.1Minipigs plasma proteaseLC-MSMinipigs plasmaIn VivoNoneEP 2022074607 WIC50 hGIPR (nM) = 2
4303
N.A.2023
Y-Aib-EGTFISDLSI-Aib-KEEIHQ-Aib-EFIEWLLAQGPSSGAPPPS
SEQ ID NO 1939FreeAmidationLinearLAib = α-aminoisobutyric acidExendin-4 analogsAntidiabetesBlood samples were collected at 0 H and after 0.25, 0.5, 1 , 2, 4, 8, 24, 32, 48, 56, 72, 80, and 96 H post S.C. application0.1 mg/kgN.A.Minipigs plasma proteaseLC-MSMinipigs plasmaIn VivoNoneEP 2022074607 WIC50 hGIPR (nM) = 2
4304
N.A.2023
GFCRCLCRRGVCRCIC
RTD-116FreeFreeLinearLNoneTheta DefensinAntimicrobialBlood samples were collected at 0.25, 1, 2, 4, 8, and 24 H post-dose via terminal cardiac puncture5 mg/kg6.05 (Elimination Half Life)Mouse plasma proteaseLC-MS with reverse phase liquid chromatographyMouse plasmaIn VivoNoneUS 2022/0048569 WAdministering an effective amount of the effective 9-defensin or the effective 0-dcfcnsin analog to the individual in need of treatment, wherein the effective amount provides antimicrobial activity directed to the microbe
4305
N.A.2023
GSSFLSPEHQRVQQRKESKKPPAKLQPR
SEQ ID NO 128FreeFreeLinearLNoneHuman Ghrelin AnalogGhrelin Receptor AgonistSolutions were incubated at 37 C for 60, 120 and 180 Minutes1 mg/ml0.2Plasma proteaseLC-MSDiluted plasma In VitroNoneEP 2023054305 WEC50(nM) = 0.83
4306
N.A.2023
PSXFLSPEHQRVQQRKESKKPPAKLQPRK
SEQ ID NO 229FreeFreeLinearLX = Octanoyl-Dpr at position 3Human Ghrelin AnalogGhrelin Receptor AgonistSolutions were incubated at 37 C for 60, 120 and 180 Minutes1 mg/ml>19Plasma proteaseLC-MSDiluted plasma In VitroNoneEP 2023054305 WEC50(nM) = 1.9
4307
N.A.2023
PSXFLSPTHSRVSSRKESKKPPAKLSPRK
SEQ ID NO 2329FreeFreeLinearLX = Octanoyl-Dpr at position 3Human Ghrelin AnalogGhrelin Receptor AgonistSolutions were incubated at 37 C for 60, 120 and 180 Minutes1 mg/ml>58Plasma proteaseLC-MSDiluted plasma In VitroNoneEP 2023054305 WEC50(nM) = 103
4308
N.A.2023
PSXFLSPYHSRVSSRKESKKPPAKLSPRK
SEQ ID NO 2429FreeFreeLinearLX = Octanoyl-Dpr at position 3Human Ghrelin AnalogGhrelin Receptor AgonistSolutions were incubated at 37 C for 60, 120 and 180 Minutes1 mg/ml>58Plasma proteaseLC-MSDiluted plasma In VitroNoneEP 2023054305 WEC50(nM) = 54.5
4309
N.A.2023
PXXFLSPTHSRVSSRKESKKPPAKLSPRK
SEQ ID NO 2529FreeFreeLinearLX = Octanoyl-Dpr at position 3, NMeS = N-Methyl-L-Serine at position 2Human Ghrelin AnalogGhrelin Receptor AgonistSolutions were incubated at 37 C for 60, 120 and 180 Minutes1 mg/ml17Plasma proteaseLC-MSDiluted plasma In VitroNoneEP 2023054305 WEC50(nM) = 70.5
4310
N.A.2023
PXXFLSPTHSRVSSRKESKKPPAKLSPRK
SEQ ID NO 2629FreeFreeLinearLX = Octanoyl-Dpr at position 3, Deg = Di-ethyl glycine at position 2Human Ghrelin AnalogGhrelin Receptor AgonistSolutions were incubated at 37 C for 60, 120 and 180 Minutes1 mg/ml>58Plasma proteaseLC-MSDiluted plasma In VitroNoneEP 2023054305 WEC50(nM) = 138
4311
N.A.2023
PXXFLSPTHSRVSSRKESKKPPAKLSPRK
SEQ ID NO 2729FreeFreeLinearLX = Octanoyl-Dpr at position 3, Tie = L-te/t-butyl-glycine at position 2Human Ghrelin AnalogGhrelin Receptor AgonistSolutions were incubated at 37 C for 60, 120 and 180 Minutes1 mg/ml>58Plasma proteaseLC-MSDiluted plasma In VitroNoneEP 2023054305 WEC50(nM) = 61.8
4312
N.A.2023
PXXFLSPTHSRVSSRKESKKPPAKLSPRK
SEQ ID NO 2829FreeFreeLinearLX = Octanoyl-Dpr at position 3, Aib = 2-aminoisobutyric acid at position 2Human Ghrelin AnalogGhrelin Receptor AgonistSolutions were incubated at 37 C for 60, 120 and 180 Minutes1 mg/ml>58Plasma proteaseLC-MSDiluted plasma In VitroNoneEP 2023054305 WEC50(nM) = 72.4
4313
N.A.2023
PVXFLSPTHSRVSSRKESKKPPAKLSPRK
SEQ ID NO 2929FreeFreeLinearLX = Octanoyl-Dpr at position 3Human Ghrelin AnalogGhrelin Receptor AgonistSolutions were incubated at 37 C for 60, 120 and 180 Minutes1 mg/ml>58Plasma proteaseLC-MSDiluted plasma In VitroNoneEP 2023054305 WEC50(nM) = 36.6
4314
N.A.2023
PTXFLSPTHSRVSSRKESKKPPAKLSPRK
SEQ ID NO 3029FreeFreeLinearLX = Octanoyl-Dpr at position 3Human Ghrelin AnalogGhrelin Receptor AgonistSolutions were incubated at 37 C for 60, 120 and 180 Minutes1 mg/ml>58Plasma proteaseLC-MSDiluted plasma In VitroNoneEP 2023054305 WEC50(nM) = 56.5
4315
N.A.2023
PXXFLSPYHSRVSSRKESKKPPAKLSPRK
SEQ ID NO 3129FreeFreeLinearLX = Octanoyl-Dpr at position 3, NMeS = N- methyl-L-serine at position 2Human Ghrelin AnalogGhrelin Receptor AgonistSolutions were incubated at 37 C for 60, 120 and 180 Minutes1 mg/ml12Plasma proteaseLC-MSDiluted plasma In VitroNoneEP 2023054305 WEC50(nM) = 50.3
4316
N.A.2023
SXFLSPTHSRVSSRKESKKPPAKLSPRK
SEQ ID NO 3228FreeFreeLinearLX = Octanoyl-Dpr at position 2Human Ghrelin AnalogGhrelin Receptor AgonistSolutions were incubated at 37 C for 60, 120 and 180 Minutes1 mg/ml>58Plasma proteaseLC-MSDiluted plasma In VitroNoneEP 2023054305 WEC50(nM) = 142
4317
N.A.2023
PSXXLSPYHSRVSSRKESKKPPAKLSPRK
SEQ ID NO 3329FreeFreeLinearLX = Octanoyl-Dpr at position 3, 1Nal = 3-(l-naphthyl)-L-alanine at position 4Human Ghrelin AnalogGhrelin Receptor AgonistSolutions were incubated at 37 C for 60, 120 and 180 Minutes1 mg/ml>58Plasma proteaseLC-MSDiluted plasma In VitroNoneEP 2023054305 WEC50(nM) = 61
4318
N.A.2023
PXXXLSPYHSRVSSRKESKKPPAKLSPRK
SEQ ID NO 3429FreeFreeLinearLNMeS = N- methyl-L-serineat position 2,X = Octanoyl-Dpr at position 3, Nal = 3-(l-naphthyl)-L-alanine at position 4Human Ghrelin AnalogGhrelin Receptor AgonistSolutions were incubated at 37 C for 60, 120 and 180 Minutes1 mg/ml25Plasma proteaseLC-MSDiluted plasma In VitroNoneEP 2023054305 WEC50(nM) = 27.2
4319
N.A.2023
PSXFLSPTHQRVSSRKESKKPPAKLSPRK
SEQ ID NO 3529FreeFreeLinearLX = Octanoyl-Dpr at position 3Human Ghrelin AnalogGhrelin Receptor AgonistSolutions were incubated at 37 C for 60, 120 and 180 Minutes1 mg/ml63Plasma proteaseLC-MSDiluted plasma In VitroNoneEP 2023054305 WEC50(nM) = 76.7
4320
N.A.2023
PSXFLSPTHSRVQSRKESKKPPAKLSPRK
SEQ ID NO 3629FreeFreeLinearLX = Octanoyl-Dpr at position 3Human Ghrelin AnalogGhrelin Receptor AgonistSolutions were incubated at 37 C for 60, 120 and 180 Minutes1 mg/ml>58Plasma proteaseLC-MSDiluted plasma In VitroNoneEP 2023054305 WEC50(nM) = 44.5
4321
N.A.2023
PSXFLSPTHSRVSQRKESKKPPAKLSPRK
SEQ ID NO 3729FreeFreeLinearLX = Octanoyl-Dpr at position 3Human Ghrelin AnalogGhrelin Receptor AgonistSolutions were incubated at 37 C for 60, 120 and 180 Minutes1 mg/ml>58Plasma proteaseLC-MSDiluted plasma In VitroNoneEP 2023054305 WEC50(nM) = 27.5
4322
N.A.2023
PSXFLSPTHSRVSSRKESKKPPAKLQPRK
SEQ ID NO 3829FreeFreeLinearLX = Octanoyl-Dpr at position 3Human Ghrelin AnalogGhrelin Receptor AgonistSolutions were incubated at 37 C for 60, 120 and 180 Minutes1 mg/ml>58Plasma proteaseLC-MSDiluted plasma In VitroNoneEP 2023054305 WEC50(nM) = 56.1
4323
N.A.2023
Y-Aib-EGTFTSDYSILLEEQAAREFIEWLLAGGPSKGAPPPS
Parent compound 139FreeFreeLinearLAib at position 2, Chem. 8 [2-[2-[2-[[2-[2-[2-[[(4S)-4-carboxy-4-(15- carboxypentadecanoylamino)butanoyl]amino]ethoxy]ethoxy]acetyl]amino]ethoxy]ethoxy] acetyl] attached to Lys33SyntheticGLP-1/GIP receptor co-agonistN.A.3 mg104 (Terminal Half Life)Beagle dogs plasma proteaseLC-MSBeagle dogs plasmaIn VivoNoneEP 2023051315 WhGLP-1R, CRE Luc 0% HSA EC50(pM) = 2.1
4324
N.A.2023
Y-Aib-EGTFTSDYSILLEEQAAREFIEWLLAGGPSKGAPPPS
Parent compound 339FreeFreeLinearLAib at position 2, Chem. 7 [(2S)-2-amino-6-[[(2S)-2-amino-6-[[(4S)-4-carboxy-4-(17-carboxyheptadecanoylamino)butanoyl]amino]hexanoyl]amino]hexanoyl] attached to Lys33SyntheticGLP-1/GIP receptor co-agonistN.A.2.9 mg131 (Terminal Half Life)Beagle dogs plasma proteaseLC-MSBeagle dogs plasmaIn VivoNoneEP 2023051315 WhGLP-1R, CRE Luc 0% HSA EC50(pM) = 4
4325
N.A.2023
Y-Aib-EGTFTSDYSILLEKQAAREFIEWLLAGGPSSGAPPPS
Parent compound 439FreeFreeLinearLAib at position 2, Chem. 7 [(2S)-2-amino-6-[[(2S)-2-amino-6-[[(4S)-4-carboxy-4-(17- carboxyheptadecanoylamino)butanoyl]amino]hexanoyl]amino]hexanoyl] attached to Lys16SyntheticGLP-1/GIP receptor co-agonistN.A.2.9 mg56 (Terminal Half Life)Beagle dogs plasma proteaseLC-MSBeagle dogs plasmaIn VivoNoneEP 2023051315 WhGLP-1R, CRE Luc 0% HSA EC50(pM) = 4.2
4326
N.A.2023
Y-Aib-EGTFTSDYSI-Aib-LDKIAQKAFVQWLIAGGPSSGAPPPS
Parent compound 539FreeAmidationLinearLAib at position 2 and 13, Chem.16[2-[2-[2-[[2-[2-[2-[[(4S)-4-carboxy-4-(19- carboxynonadecanoylamino)butanoyl]amino]ethoxy]ethoxy]acetyl]amino]ethoxy]ethoxy] acetyl] attached to Lys SyntheticGLP-1/GIP receptor co-agonistN.A.3 mg134 (Terminal Half Life)Beagle dogs plasma proteaseLC-MSBeagle dogs plasmaIn VivoNoneEP 2023051315 WhGLP-1R, CRE Luc 0% HSA EC50(pM) = 9.7
4327
N.A.2023
KVY-Aib-EGTFTSDYSILLEEQAAREFIEWLLAGGPSKGAPPPS
Non-converting compound 141Lys side chain conatins Chem. 16[(4S)-4-carboxy-4-(15-carboxypentadecanoylamino)butanoyl] attached to Lys1FreeLinearLAib at position 4, Chem. 8[2-[2-[2-[[2-[2-[2-[[(4S)-4-carboxy-4-(15-carboxypentadecanoylamino)butanoyl]amino]ethoxy]ethoxy]acetyl]amino]ethoxy]ethoxy] acetyl] attached to Lys33SyntheticGLP-1/GIP receptor co-agonistN.A.2.8 mg137 (Terminal Half Life)Beagle dogs plasma proteaseLC-MSBeagle dogs plasmaIn VivoNoneEP 2023051315 WN.A.
4328
N.A.2023
KVY-Aib-EGTFTSDYSILLEEQAAREFIEWLLAGGPSKGAPPPS
Non-converting compound 241Lys side chain conatins Chem. 16[(4S)-4-carboxy-4-(15-carboxypentadecanoylamino)butanoyl] attached to Lys1 FreeLinearLAib at position 4,Chem. 10[(2S)-2-amino-6-[[(2S)-2-amino-6-[[(4S)-4- carboxy-4-(15-carboxypentadecanoylamino)butanoyl]amino]hexanoyl]amino]hexanoyl] attached to Lys33 SyntheticGLP-1/GIP receptor co-agonistN.A.3.5 mg130 (Terminal Half Life)Beagle dogs plasma proteaseLC-MSBeagle dogs plasmaIn VivoNoneEP 2023051315 WN.A.
4329
N.A.2023
KVY-Aib-EGTFTSDYSILLEKQAAREFIEWLLAGGPSSGAPPPS
Non-converting compound 341Lys side chain conatins Chem. 16[(4S)-4-carboxy-4-(15-carboxypentadecanoylamino)butanoyl] attached to Lys1 , FreeLinearLAib at position 4,Chem. 7[(2S)-2-amino-6-[[(2S)-2-amino-6-[[(4S)-4-carboxy-4-(17-carboxyheptadecanoylamino)butanoyl]amino]hexanoyl]amino]hexanoyl] attached to Lys 16SyntheticGLP-1/GIP receptor co-agonistN.A.3 mg115 (Terminal Half Life)Beagle dogs plasma proteaseLC-MSBeagle dogs plasmaIn VivoNoneEP 2023051315 WN.A.
4330
N.A.2023
KVY-Aib-EGTFTSDYSI-Aib-LDKIAQKAFVQWLIAGGPSSGAPPPS
Non-converting compound 441Lys side chain conatins Chem. 16[(4S)-4-carboxy-4-(15-carboxypentadecanoylamino)butanoyl attached to Lys1AmidationLinearLAib at position 4,Chem. 11[2-[2-[2-[[2-[2-[2-[[(4S)-4-carboxy-4-(19-carboxynonadecanoylamino)butanoyl]amino]ethoxy]ethoxy]acetyl]amino]ethoxy]ethoxy] acetyl] attached to Lys20SyntheticGLP-1/GIP receptor co-agonistN.A.3 mg136 (Terminal Half Life)Beagle dogs plasma proteaseLC-MSBeagle dogs plasmaIn VivoNoneEP 2023051315 WN.A.
4331
N.A.2023
k-Sar-Y-Aib-EGTFTSDYSILLEEQAAREFIEWLLAGGPSKGAPPPS
Compound 141D-Lys conjugated with [(4S)-4-carboxy-4-(15-carboxypentadecanoylamino)butanoyl]FreeLinearMixChem. 8[2-[2-[2-[[2-[2-[2-[[(4S)-4-carboxy-4-(15- carboxypentadecanoylamino)butanoyl]amino]ethoxy]ethoxy]acetyl]amino]ethoxy]ethoxy] acetyl] attached to Lys33 , Sar2, Aib modificationsSyntheticGLP-1/GIP receptor co-agonistN.A.3.1 mg146 (Terminal Half Life)Beagle dogs plasma proteaseLC-MSBeagle dogs plasmaIn VivoNoneEP 2023051315 WN.A.
4332
N.A.2023
G-Aeg-Y-Aib-EGTFTSDYSILLEEQAAREFIEWLLAGGPSKGAPPPS
Compound 241FreeFreeLinearLAeg = N-(2-aminoethyl)glycine, Chem.16[(4S)-4-carboxy-4-(15-carboxypentadecanoylamino)butanoyl] attached to Aeg2, Chem.8[2-[2-[2-[[2-[2-[2-[[(4S)-4-carboxy-4-(15-carboxypentadecanoylamino)butanoyl]amino]ethoxy]ethoxy]acetyl]amino]ethoxy]ethoxy]acetyl] attached to Lys33SyntheticGLP-1/GIP receptor co-agonistN.A.2.9 mg142 (Terminal Half Life) Beagle dogs plasma proteaseLC-MSBeagle dogs plasmaIn VivoNoneEP 2023051315 WN.A.
4333
N.A.2023
K-Sar-Y-Aib-EGTFTSDYSILLEEQAAREFIEWLLAGGPSKGAPPPS
Compound 341Chem. 16 [(4S)-4-carboxy-4-(15-carboxypentadecanoylamino)butanoyl] attached to Lys1FreeLinearLChem. 8[2-[2-[2-[[2-[2-[2-[[(4S)-4-carboxy-4-(15- carboxypentadecanoylamino)butanoyl]amino]ethoxy]ethoxy]acetyl]amino]ethoxy]ethoxy] acetyl] attached to Lys33, Sar2 modificationSyntheticGLP-1/GIP receptor co-agonistN.A.3 mg139 (Terminal Half Life)Beagle dogs plasma proteaseLC-MSBeagle dogs plasmaIn VivoNoneEP 2023051315 WN.A.
4334
N.A.2023
L-Aeg-Y-Aib-EGTFTSDYSILLEEQAAREFIEWLLAGGPSKGAPPPS
Compound 541Chem. 16[(4S)-4-carboxy-4-(15-carboxypentadecanoylamino)butanoyl] attached to L-AegFreeLinearLChem. 8[2-[2-[2-[[2-[2-[2-[[(4S)-4-carboxy-4-(15- carboxypentadecanoylamino)butanoyl]amino]ethoxy]ethoxy]acetyl]amino]ethoxy]ethoxy] acetyl] attached to Lys33SyntheticGLP-1/GIP receptor co-agonistN.A.2.8 mg106 (Terminal Half Life)Beagle dogs plasma proteaseLC-MSBeagle dogs plasmaIn VivoNoneEP 2023051315 WN.A.
4335
N.A.2023
K-Sar-Y-Aib-EGTFTSDYSILLEEQAAREFIEWLLAGGPSKGAPPPS
Compound 1241Chem. 16[(4S)-4-carboxy-4-(15-carboxypentadecanoylamino)butanoyl] attached to Lys1FreeLinearLChem. 10[(2S)-2-amino-6-[[(2S)-2-amino-6-[[(4S)-4- carboxy-4-(15-carboxypentadecanoylamino)butanoyl]amino]hexanoyl]amino]hexanoyl] attached to Lys33, Sar2 modficationsSyntheticGLP-1/GIP receptor co-agonistN.A.2.7 mg143 (Terminal Half Life)Beagle dogs plasma proteaseLC-MSBeagle dogs plasmaIn VivoNoneEP 2023051315 WN.A.
4336
N.A.2023
K-Sar-Y-Aib-EGTFTSDYSILLEEQAAREFIEWLLAGGPSKGAPPPS
Compound 1341Chem. 17[(4S)-4-carboxy-4-(17-carboxyheptadecanoylamino)butanoyl] attached to Lys1FreeLinearLChem. 10[(2S)-2-amino-6-[[(2S)-2-amino-6-[[(4S)-4- carboxy-4-(15-carboxypentadecanoylamino)butanoyl]amino]hexanoyl]amino]hexanoyl] attached to Lys33, Sar2 modificationsSyntheticGLP-1/GIP receptor co-agonistN.A.2.8 mg121 (Terminal Half Life)Beagle dogs plasma proteaseLC-MSBeagle dogs plasmaIn VivoNoneEP 2023051315 WN.A.
4337
N.A.2023
K-Sar-Y-Aib-EGTFTSDYSILLEEQAAREFIEWLLAGGPSKGAPPPS
Compound 1441Chem. 22[(2S)-2,6-bis[[(4S)-4-carboxy-4-(15-carboxypentadecanoylamino)butanoyl]amino]hexanoyl] attached to Lys1FreeLinearLChem. 10[(2S)-2-amino-6-[[(2S)-2-amino-6-[[(4S)-4-carboxy-4-(15- carboxypentadecanoylamino)butanoyl]amino]hexanoyl]amino]hexanoyl] attached to Lys33, Sar2 modificationsSyntheticGLP-1/GIP receptor co-agonistN.A.3.2 mg119 (Terminal Half Life)Beagle dogs plasma proteaseLC-MSBeagle dogs plasmaIn VivoNoneEP 2023051315 WN.A.
4338
N.A.2023
K-Sar-Y-Aib-EGTFTSDYSILLEEQAAREFIEWLLAGGPSKGAPPPS
Compound 1541Chem. 17[(4S)-4-carboxy-4-(17-carboxyheptadecanoylamino)butanoyl] attached to Lys1FreeLinearLChem. 7[(2S)-2-amino-6-[[(2S)-2-amino-6-[[(4S)-4- carboxy-4-(17-carboxyheptadecanoylamino)butanoyl]amino]hexanoyl]amino]hexanoyl] attached to Lys33, Sar2 modificationsSyntheticGLP-1/GIP receptor co-agonistN.A.2 mg124 (Terminal Half Life)Beagle dogs plasma proteaseLC-MSBeagle dogs plasmaIn VivoNoneEP 2023051315 WN.A.
4339
N.A.2023
K-Sar-Y-Aib-EGTFTSDYSILLEKQAAREFIEWLLAGGPSSGAPPPS
Compound 1641Chem. 16[(4S)-4-carboxy-4-(15-carboxypentadecanoylamino)butanoyl] attached to Lys1FreeLinearLChem. 7[(2S)-2-amino-6-[[(2S)-2-amino-6-[[(4S)-4-carboxy-4-(17- carboxyheptadecanoylamino)butanoyl]amino]hexanoyl]amino]hexanoyl] attached to Lys 16, Sar2 modificationsSyntheticGLP-1/GIP receptor co-agonistN.A.2.9 mg96 (Terminal Half Life)Beagle dogs plasma proteaseLC-MSBeagle dogs plasmaIn VivoNoneEP 2023051315 WN.A.
4340
N.A.2023
G-Aeg-Y-Aib-EGTFTSDYSILLEKQAAREFIEWLLAGGPSSGAPPPS
Compound 1741Chem. 16 [(4S)-4-carboxy-4-(15-carboxypentadecanoylamino)butanoyl] attached to G-AegFreeLinearLChem.7[(2S)-2-amino-6-[[(2S)-2-amino-6-[[(4S)-4-carboxy-4-(17- carboxyheptadecanoylamino)butanoyl]amino]hexanoyl]amino]hexanoyl] attached to Lys16, Aib modificationsSyntheticGLP-1/GIP receptor co-agonistN.A.3.2 mg105 (Terminal Half Life)Beagle dogs plasma proteaseLC-MSBeagle dogs plasmaIn VivoNoneEP 2023051315 WN.A.
4341
N.A.2023
K-Sar-Y-Aib-EGTFTSDYSI-Aib-LDKIAQKAFVQWLIAGGPSSGAPPPS
Compound 1841Chem. 16[(4S)-4-carboxy-4-(15-carboxypentadecanoylamino)butanoyl] attached to Lys1AmidationLinearLChem.11 [2-[2-[2-[[2-[2-[2-[[(4S)-4-carboxy-4-(19- carboxynonadecanoylamino)butanoyl]amino]ethoxy]ethoxy]acetyl]amino]ethoxy]ethoxy] acetyl] attached to Lys20, Sar2 modificationSyntheticGLP-1/GIP receptor co-agonistN.A.2.9 mg88 (Terminal Half Life)Beagle dogs plasma proteaseLC-MSBeagle dogs plasmaIn VivoNoneEP 2023051315 WN.A.
4342
N.A.2023
Y-Aib-EGTFTSDYSILLEEQAAREFIEWLLAGGPSKGAPPPS
Parent compound 139FreeFreeLinearLAib at position 2, Chem. 8 [2-[2-[2-[[2-[2-[2-[[(4S)-4-carboxy-4-(15- carboxypentadecanoylamino)butanoyl]amino]ethoxy]ethoxy]acetyl]amino]ethoxy]ethoxy] acetyl] attached to Lys33SyntheticGLP-1/GIP receptor co-agonistN.A.2 nmol/kg121 (Terminal Half Life)Minipigs plasma proteaseELISA or similar antibody based assay or LC-MSMinipigs plasmaIn VivoNoneEP 2023051315 WhGLP-1R, CRE Luc 0% HSA EC50(pM) = 2.1
4343
N.A.2023
Y-Aib-EGTFTSDYSILLEEQAAREFIEWLLAGGPSKGAPPPS
Parent compound 239FreeFreeLinearLAib at position 2, Chem. 10[(2S)-2-amino-6-[[(2S)-2-amino-6-[[(4S)-4-carboxy-4-(15-carboxypentadecanoylamino)butanoyl]amino]hexanoyl]amino]hexanoyl attached to Lys33SyntheticGLP-1/GIP receptor co-agonistN.A.1 nmol/kg104 (Terminal Half Life)Minipigs plasma proteaseELISA or similar antibody based assay or LC-MSMinipigs plasmaIn VivoNoneEP 2023051315 WhGLP-1R, CRE Luc 0% HSA EC50(pM) = 1.5
4344
N.A.2023
Y-Aib-EGTFTSDYSILLEKQAAREFIEWLLAGGPSSGAPPPS
Parent compound 439FreeFreeLinearLAib at position 2, Chem. 7 [(2S)-2-amino-6-[[(2S)-2-amino-6-[[(4S)-4-carboxy-4-(17- carboxyheptadecanoylamino)butanoyl]amino]hexanoyl]amino]hexanoyl] attached to Lys16SyntheticGLP-1/GIP receptor co-agonistN.A.1 nmol/kg106 (Terminal Half Life)Minipigs plasma proteaseELISA or similar antibody based assay or LC-MSMinipigs plasmaIn VivoNoneEP 2023051315 WhGLP-1R, CRE Luc 0% HSA EC50(pM) = 4.2
4345
N.A.2023
KVY-Aib-EGTFTSDYSILLEEQAAREFIEWLLAGGPSKGAPPPS
Non-converting compound 141Lys side chain conatins Chem. 16[(4S)-4-carboxy-4-(15-carboxypentadecanoylamino)butanoyl] attached to Lys1FreeLinearLAib at position 4, Chem. 8[2-[2-[2-[[2-[2-[2-[[(4S)-4-carboxy-4-(15-carboxypentadecanoylamino)butanoyl]amino]ethoxy]ethoxy]acetyl]amino]ethoxy]ethoxy] acetyl] attached to Lys33SyntheticGLP-1/GIP receptor co-agonistN.A.2 nmol/kg170 (Terminal Half Life)Minipigs plasma proteaseELISA or similar antibody based assay or LC-MSMinipigs plasmaIn VivoNoneEP 2023051315 WN.A.
4346
N.A.2023
k-Sar-Y-Aib-EGTFTSDYSILLEEQAAREFIEWLLAGGPSKGAPPPS
Compound 141D-Lys conjugated with [(4S)-4-carboxy-4-(15-carboxypentadecanoylamino)butanoyl]FreeLinearMixChem. 8[2-[2-[2-[[2-[2-[2-[[(4S)-4-carboxy-4-(15- carboxypentadecanoylamino)butanoyl]amino]ethoxy]ethoxy]acetyl]amino]ethoxy]ethoxy] acetyl] attached to Lys33 , Sar2 modificationSyntheticGLP-1/GIP receptor co-agonistN.A.20 nmol/kg118 (Terminal Half Life)Minipigs plasma proteaseELISA or similar antibody based assay or LC-MSMinipigs plasmaIn VivoNoneEP 2023051315 WN.A.
4347
N.A.2023
K-Sar-Y-Aib-EGTFTSDYSILLEEQAAREFIEWLLAGGPSKGAPPPS
Compound 341Chem. 16 [(4S)-4-carboxy-4-(15-carboxypentadecanoylamino)butanoyl] attached to Lys1FreeLinearLChem. 8[2-[2-[2-[[2-[2-[2-[[(4S)-4-carboxy-4-(15- carboxypentadecanoylamino)butanoyl]amino]ethoxy]ethoxy]acetyl]amino]ethoxy]ethoxy] acetyl] attached to Lys33, Sar2 modificationsSyntheticGLP-1/GIP receptor co-agonistN.A.2 nmol/kg119 (Terminal Half Life)Minipigs plasma proteaseELISA or similar antibody based assay or LC-MSMinipigs plasmaIn VivoNoneEP 2023051315 WN.A.
4348
N.A.2023
K-Sar-Y-Aib-EGTFTSDYSILLEEQAAREFIEWLLAGGPSKGAPPPS
Compound 941Chem. 19[2-[[(4S)-4-carboxy-4-(15-carboxypentadecanoylamino)butanoyl]amino]acetyl] attached to Lys1FreeLinearLChem. 8[2-[2-[2-[[2-[2-[2-[[(4S)-4-carboxy-4-(15- carboxypentadecanoylamino)butanoyl]amino]ethoxy]ethoxy]acetyl]amino]ethoxy]ethoxy] acetyl] attached to Lys33, Sar2 modificationsSyntheticGLP-1/GIP receptor co-agonistN.A.20 nmol/kg102 (Terminal Half Life)Minipigs plasma proteaseELISA or similar antibody based assay or LC-MSMinipigs plasmaIn VivoNoneEP 2023051315 WN.A.
4349
N.A.2023
k-Sar-Y-Aib-EGTFTSDYSILLEEQAAREFIEWLLAGGPSKGAPPPS
Compound 1041Chem. 21[2-[2-[2-[[2-[2-[2-[[(4S)-4-carboxy-4-(15- carboxypentadecanoylamino)butanoyl]amino]ethoxy]ethoxy]acetyl]amino]ethoxy]ethoxy] acetyl] attached to D-Lys1FreeLinearMixChem. 8[2-[2-[2-[[2-[2-[2-[[(4S)-4- carboxy-4-(15- carboxypentadecanoylamino)butanoyl]amino]ethoxy]ethoxy]acetyl]amino]ethoxy]ethoxy] acetyl] attached to Lys33 SyntheticGLP-1/GIP receptor co-agonistN.A.20 nmol/kg118 (Terminal Half Life)Minipigs plasma proteaseELISA or similar antibody based assay or LC-MSMinipigs plasmaIn VivoNoneEP 2023051315 WN.A.
4350
N.A.2023
EVQLLESGGGLVQPGGSLRLSCAASGFTFRSFGMSWVRQAPGKGPEWVSSISGSGSDTLYADSVKGRFTISRDNSKNTLYLQMNSLRPEDTAVYYCTIGGSLSRSSQGTLVTVSSDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLYITREPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALKFHYTQKSLSLSPG
TA-Alb23-Fc-ABDEG341Alb23 fused at the N-termini of both Fc domains of efgartigimodFreeLinearLNoneSyntheticFcRN AntagonistBlood sample were collected for Pk Measurement Ar : Test Day 1 (Td1)(Pre-Dosing), Td1(Prior To Dosing), Td1(5 Min), Td2(24 Hrs Post Dosing), Td3, Td4, Td6, Td8, Td11, Td15, Td18, Td22, Td29, Td36 And Td4320 mg/kg27Cynomolgus monkeys serum proteaseSandwich ELISACynomolgus monkeys serumIn VivoNoneEP 2023066180 WN.A.
4351
N.A.2023
EVQLLESGGGLVQPGGSLRLSCAASGFTFRSFGMSWVRQAPGKGPEWVSSISGSGSDTLYADSVKGRFTISRDNSKNTLYLQMNSLRPEDTAVYYCTIGGSLSRSSQGTLVTVSSDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLYITREPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALKFHYTQKSLSLSPG
TA-Alb23-Fc-ABDEG341Alb23 fused at the N-termini of both Fc domains of efgartigimodFreeLinearLNoneSyntheticFcRN AntagonistBlood sample were collected for PK measurement Ar : Test Day 1 (Td1)(Pre-Dosing), Td1(Prior To Dosing), Td1(5 Min), Td2(24 Hrs Post Dosing), Td3, Td4, Td6, Td8, Td11, Td15, Td18, Td22, Td29, Td36 And Td435 mg/kg28 ± 23Cynomolgus monkeys serum proteaseSandwich ELISACynomolgus monkeys serumIn VivoNoneEP 2023066180 WN.A.
4352
N.A.2023
EVQLLESGGGLVQPGGSLRLSCAASGFTFRSFGMSWVRQAPGKGPEWVSSISGSGSDTLYADSVKGRFTISRDNSKNTLYLQMNSLRPEDTAVYYCTIGGSLSRSSQGTLVTVSSDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLYITREPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALKFHYTQKSLSLSPG
TA-Alb23-Fc-ABDEG341Alb23 fused at the N-termini of both Fc domains of efgartigimodFreeLinearLNoneSyntheticFcRN AntagonistBlood sample were collected for PK measurement Ar : Test Day 1 (Td1)(Pre-Dosing), Td1(Prior To Dosing), Td1(5 Min), Td2(24 Hrs Post Dosing), Td3, Td4, Td6, Td8, Td11, Td15, Td18, Td22, Td29, Td36 And Td4320 mg/kg26.5C2 Cynomolgus monkeys serum proteaseSandwich ELISAC2 Cynomolgus monkeys serumIn VivoNoneEP 2023066180 WN.A.
4353
N.A.2023
EVQLLESGGGLVQPGGSLRLSCAASGFTFRSFGMSWVRQAPGKGPEWVSSISGSGSDTLYADSVKGRFTISRDNSKNTLYLQMNSLRPEDTAVYYCTIGGSLSRSSQGTLVTVSSDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLYITREPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALKFHYTQKSLSLSPG
TA-Alb23-Fc-ABDEG341Alb23 fused at the N-termini of both Fc domains of efgartigimodFreeLinearLNoneSyntheticFcRN AntagonistBlood sample were collected for PK Measurement Ar : Test Day 1 (Td1)(Pre-Dosing), Td1(Prior To Dosing), Td1(5 Min), Td2(24 Hrs Post Dosing), Td3, Td4, Td6, Td8, Td11, Td15, Td18, Td22, Td29, Td36 And Td435 mg/kg13.4C4 Cynomolgus monkeys serum proteaseSandwich ELISAC4 Cynomolgus monkeys serumIn VivoNoneEP 2023066180 WN.A.
4354
N.A.2023
EVQLLESGGGLVQPGGSLRLSCAASGFTFRSFGMSWVRQAPGKGPEWVSSISGSGSDTLYADSVKGRFTISRDNSKNTLYLQMNSLRPEDTAVYYCTIGGSLSRSSQGTLVTVSSDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLYITREPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALKFHYTQKSLSLSPG
TA-Alb23-Fc-ABDEG341Alb23 fused at the N-termini of both Fc domains of efgartigimodFreeLinearLNoneSyntheticFcRN AntagonistBlood sample were collected for PK measurement Ar : Test Day 1 (Td1)(Pre-Dosing), Td1(Prior To Dosing), Td1(5 Min), Td2(24 Hrs Post Dosing), Td3, Td4, Td6, Td8, Td11, Td15, Td18, Td22, Td29, Td36 And Td435 mg/kg54.4C5 Cynomolgus monkeys serum proteaseSandwich ELISAC5 Cynomolgus monkeys serumIn VivoNoneEP 2023066180 WN.A.
4355
N.A.2023
EVQLLESGGGLVQPGGSLRLSCAASGFTFRSFGMSWVRQAPGKGPEWVSSISGSGSDTLYADSVKGRFTISRDNSKNTLYLQMNSLRPEDTAVYYCTIGGSLSRSSQGTLVTVSSDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLYITREPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALKFHYTQKSLSLSPG
TA-Alb23-Fc-ABDEG341Alb23 fused at the N-termini of both Fc domains of efgartigimodFreeLinearLNoneSyntheticFcRN AntagonistBlood sample were collected for PK Measurement Ar : Test Day 1 (Td1)(Pre-Dosing), Td1(Prior To Dosing), Td1(5 Min), Td2(24 Hrs Post Dosing), Td3, Td4, Td6, Td8, Td11, Td15, Td18, Td22, Td29, Td36 And Td435 mg/kg16.9C6 Cynomolgus monkeys serum proteaseSandwich ELISAC6 Cynomolgus monkeys serumIn VivoNoneEP 2023066180 WN.A.
4356
N.A.2023
DKTHTCPPCPAPELLGGPSVFLFPPKPKDTLYITREPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALKFHYTQKSLSLSPGGGGGSGGGGSGGGGSGGGGSEVQLLESGGGLVQPGGSLRLSCAASGFTFRSFGMSWVRQAPGKGPEWVSSISGSGSDTLYADSVKGRFTISRDNSKNTLYLQMNSLRPEDTAVYYCTIGGSLSRSSQGTLVTVSS
TA-Fc-ABDEG-Alb23361FreeAlb23 fused at the C-termini of both Fc domains of ABDEG via a 20GS linkerLinearLNoneSyntheticFcRN AntagonistN.A.30 mg/kg15G1-1 Cynomolgus monkeys serum proteaseSandwich ELISAG1-1 Cynomolgus monkeys serumIn VivoNoneEP 2023066180 WN.A.
4357
N.A.2023
DKTHTCPPCPAPELLGGPSVFLFPPKPKDTLYITREPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALKFHYTQKSLSLSPGGGGGSGGGGSGGGGSGGGGSEVQLLESGGGLVQPGGSLRLSCAASGFTFRSFGMSWVRQAPGKGPEWVSSISGSGSDTLYADSVKGRFTISRDNSKNTLYLQMNSLRPEDTAVYYCTIGGSLSRSSQGTLVTVSS
TA-Fc-ABDEG-Alb23361FreeAlb23 fused at the C-termini of both Fc domains of ABDEG via a 20GS linkerLinearLNoneSyntheticFcRN AntagonistN.A.30 mg/kg9.3G1-2 Cynomolgus monkeys serum proteaseSandwich ELISAG1-2 Cynomolgus monkeys serumIn VivoNoneEP 2023066180 WN.A.
4358
N.A.2023
DKTHTCPPCPAPELLGGPSVFLFPPKPKDTLYITREPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALKFHYTQKSLSLSPGGGGGSGGGGSGGGGSGGGGSEVQLLESGGGLVQPGGSLRLSCAASGFTFRSFGMSWVRQAPGKGPEWVSSISGSGSDTLYADSVKGRFTISRDNSKNTLYLQMNSLRPEDTAVYYCTIGGSLSRSSQGTLVTVSS
TA-Fc-ABDEG-Alb23361FreeAlb23 fused at the C-termini of both Fc domains of ABDEG via a 20GS linkerLinearLNoneSyntheticFcRN AntagonistN.A.30 mg/kg4.5G1-3 Cynomolgus monkeys serum proteaseSandwich ELISAG1-3 Cynomolgus monkeys serumIn VivoNoneEP 2023066180 WN.A.
4359
N.A.2023
DKTHTCPPCPAPELLGGPSVFLFPPKPKDTLYITREPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALKFHYTQKSLSLSPGGGGGSGGGGSGGGGSGGGGSEVQLLESGGGLVQPGGSLRLSCAASGFTFRSFGMSWVRQAPGKGPEWVSSISGSGSDTLYADSVKGRFTISRDNSKNTLYLQMNSLRPEDTAVYYCTIGGSLSRSSQGTLVTVSS
TA-Fc-ABDEG-Alb23361FreeAlb23 fused at the C-termini of both Fc domains of ABDEG via a 20GS linkerLinearLNoneSyntheticFcRN AntagonistN.A.75 mg/kg13G2-1 Cynomolgus monkeys serum proteaseSandwich ELISAG2-1 Cynomolgus monkeys serumIn VivoNoneEP 2023066180 WN.A.
4360
N.A.2023
DKTHTCPPCPAPELLGGPSVFLFPPKPKDTLYITREPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALKFHYTQKSLSLSPGGGGGSGGGGSGGGGSGGGGSEVQLLESGGGLVQPGGSLRLSCAASGFTFRSFGMSWVRQAPGKGPEWVSSISGSGSDTLYADSVKGRFTISRDNSKNTLYLQMNSLRPEDTAVYYCTIGGSLSRSSQGTLVTVSS
TA-Fc-ABDEG-Alb23361FreeAlb23 fused at the C-termini of both Fc domains of ABDEG via a 20GS linkerLinearLNoneSyntheticFcrn AntagonistN.A.75 mg/kg6.1G2-2 Cynomolgus monkeys serum proteaseSandwich ELISAG2-2 Cynomolgus monkeys serumIn VivoNoneEP 2023066180 WN.A.
4361
N.A.2023
DKTHTCPPCPAPELLGGPSVFLFPPKPKDTLYITREPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALKFHYTQKSLSLSPGGGGGSGGGGSGGGGSGGGGSEVQLLESGGGLVQPGGSLRLSCAASGFTFRSFGMSWVRQAPGKGPEWVSSISGSGSDTLYADSVKGRFTISRDNSKNTLYLQMNSLRPEDTAVYYCTIGGSLSRSSQGTLVTVSS
TA-Fc-ABDEG-Alb23361FreeAlb23 fused at the C-termini of both Fc domains of ABDEG via a 20GS linkerLinearLNoneSyntheticFcrn AntagonistN.A.75 mg/kg12G2-3 Cynomolgus monkeys serum proteaseSandwich ELISAG2-3 Cynomolgus monkeys serumIn VivoNoneEP 2023066180 WN.A.
4362
N.A.2023
AEAKYAKEAVEALVEIWTLPNLTREQWQAFIYKLRDDPSQSSELLSEAKKLNDSQAPKASGSLAEAKEAANAELDSYGVSDFYKRLIDKAKTVEGVEALKDAILAALP
ZTPA001108FreeABD (albumin Binding Domain)LinearLNoneTslp Binding Z VariantsAntiinflammatoryBlood samples (0.5 mL) were collected at the following time points: Predose, At 10 And 30 Min And 1 , 6, 10, 26, 50, 72, And 96 H Postdose And At Days 6, 7, 8, 11 , 13, 15, 18, And 221.33 mg/kg3-4 (Terminal Half Life)Cynomolgus monkeys serum proteaseSandwich PK-ELISACynomolgus monkeys serumIn VivoNoneEP 2023053030 WIC50(nM) = 0.5
4363
N.A.2023
GSLAEAKEAANAELDSYGVSDFYKRLIDKAKTVEGVEALKDAILAALPGGGGSAEAKYAKEAVEALVEIWTLPNLTREQWQAFIYKLRDDPSQSSELLSEAKKLNDSQAPK
ZTPA104111ABD (albumin Binding Domain)FreeLinearLNoneTslp Binding Z VariantsAntiinflammatoryBlood sampling time points were divided into two cohorts as follows: Cohort A (N=3 Per Test Item) Were Bled Predose, At 5 Min And 1 , 8, 72, 168, 264, 408 And 504 H Postdose; And Cohort B (N=3 Per Test Item) Were Bled Predose, At 30 Min And 3, 24, 120, 216, 336 And 456 H Postdose1.2 mg/kg36 (Terminal Half Life)SD rats serum proteaseELISASD rats serumIn VivoNoneEP 2023053030 WIC50(nM) = 0.03
4364
N.A.2023
AEAKYAKEAVEALVEIWTLPNLTREQWQAFIYKLRDDPSQSSELLSEAKKLNDSQAPKASGSLAEAKEAANAELDSYGVSDFYKRLIDKAKTVEGVEALKDAILAALP
ZTPA001108FreeABD (albumin Binding Domain)LinearLNoneTslp Binding Z VariantsAntiinflammatoryBlood sampling time points were divided into two cohorts as follows: Cohort A (N=3 Per Test Item) Were Bled Predose, At 5 Min And 1 , 8, 72, 168, 264, 408 And 504 H Postdose; And Cohort B (N=3 Per Test Item) Were Bled Predose, At 30 Min And 3, 24, 120, 216, 336 And 456 H Postdose1.2 mg/kg29 (Terminal Half Life)SD rats serum proteaseELISASD rats serumIn VivoNoneEP 2023053030 WIC50(nM) = 0.5
4365
366308262023
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
Exendin39Fluorescently labelledAmidationLinearLNoneDerived from Gila monsterAntidiabetesTen μl of blood was collected from a tiny incision on the tail vein into tubes containing 90 μl of 1,000 U ml-1 heparin (Sigma) at 5-min, 1-, 2-, 4-, 8-, 24-, 48-, 72-, 96-, 120-, 144- and 168-h. 1000 nmol/kg0.65 ± 0.04 (T1/2 Absorption) Naïve mice plasma proteaseFluorescence assayNaïve mice plasmaIn VivoPDB id: 7MLLNoneEC50 (nM) = 0.04 ± 0.01
4366
366308262023
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
Ex-PEGRh 39Fluorescently labelledPEG Rh(27.7Kda)LinearLNoneExendin-4 analogsAntidiabetesTen μl of blood was collected from a tiny incision on the tail vein into tubes containing 90 μl of 1,000 U ml-1 heparin (Sigma) at 5-min, 1-, 2-, 4-, 8-, 24-, 48-, 72-, 96-, 120-, 144- and 168-h. 1000 nmol/kg6.59 ± 0.27 (T1/2 Absorption) Naïve mice plasma proteaseFluorescence assayNaïve mice plasmaIn VivoPDB id: 7MLLNoneEC50 (nM) = 1.3 ± 0.2
4367
366308262023
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
Ex-PEGMw 39Fluorescently labelledPEG MW(46.3 Kda)LinearLNoneExendin-4 analogsAntidiabetesTen μl of blood was collected from a tiny incision on the tail vein into tubes containing 90 μl of 1,000 U ml-1 heparin (Sigma) at 5-min, 1-, 2-, 4-, 8-, 24-, 48-, 72-, 96-, 120-, 144- and 168-h. 1000 nmol/kg6.6 ± 0.9 (T1/2 Absorption) Naïve mice plasma proteaseFluorescence assayNaïve mice plasmaIn VivoPDB id: 7MLLNoneEC50 (nM) = 2.7 ± 0.5
4368
366308262023
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS 
Ex-POEGMAopt 39Fluorescently labelledPEGMAopt(54.7Kda)LinearLNoneExendin-4 analogsAntidiabetesTen μl of blood was collected from a tiny incision on the tail vein into tubes containing 90 μl of 1,000 U ml-1 heparin (Sigma) at 5-min, 1-, 2-, 4-, 8-, 24-, 48-, 72-, 96-, 120-, 144- and 168-h. 1000 nmol/kg9.1 ± 0.9 (T1/2 Absorption) Naïve mice plasma proteaseFluorescence assayNaïve mice plasmaIn VivoPDB id: 7MLLNoneEC50 (nM) = 2.8 ± 0.7
4369
366308262023
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
Exendin 39Fluorescently labelledAmidationLinearLNoneDerived from Gila monsterAntidiabetesTen μl of blood was collected from a tiny incision on the tail vein into tubes containing 90 μl of 1,000 U ml-1 heparin (Sigma) at 5-min, 1-, 2-, 4-, 8-, 24-, 48-, 72-, 96-, 120-, 144- and 168-h. 1000 nmol/kg0.77 ± 0.07 (T1/2 Absorption) Naïve mice plasma proteaseFluorescence assayNaïve mice plasmaIn VivoPDB id: 7MLLNoneEC50 (nM) = 0.04 ± 0.01
4370
366308262023
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
Ex-PEGRh 39Fluorescently labelledPEG RH(27.7KDa)LinearLNoneExendin-4 analogsAntidiabetesTen μl of blood was collected from a tiny incision on the tail vein into tubes containing 90 μl of 1,000 U ml-1 heparin (Sigma) at 5-min, 1-, 2-, 4-, 8-, 24-, 48-, 72-, 96-, 120-, 144- and 168-h. 1000 nmol/kgN.A.Immunized mice plasma proteaseFluorescence assayImmunized mice plasmaIn VivoPDB id: 7MLLNoneEC50 (nM) = 1.3 ± 0.2
4371
366308262023
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS 
Ex-POEGMAopt 39Fluorescently labelledPOEGMAopt(54.7Kda)LinearLNoneExendin-4 analogsAntidiabetesTen μl of blood was collected from a tiny incision on the tail vein into tubes containing 90 μl of 1,000 U ml-1 heparin (Sigma) at 5-min, 1-, 2-, 4-, 8-, 24-, 48-, 72-, 96-, 120-, 144- and 168-h. 1000 nmol/kg12.1 ± 1.0 (T1/2 Absorption)Immunized mice plasma proteaseFluorescence assayImmunized mice plasmaIn VivoPDB id: 7MLLNoneEC50 (nM) = 2.8 ± 0.7
4372
366308262023
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
Exendin39FreeAmidationLinearLFluorescently labeledIsolated from the saliva of the Gila monster lizard (Heloderma suspectum)AntidiabetesBlood collection at 5-min, 1-, 2-, 4-, 8-, 24-, 48-, 72-, 96-, 120-, 144- and 168-h1000 nmol/kg0.65 ± 0.04 (T1/2 Absorption)Naïve mice plasma proteaseFluorescence assayNaïve mice plasmaIn VivoPDB id: 1JRJNoneEC50 = 0.04 ± 0.01 nM for exendin
4373
366308262023
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
Ex-PEGRh39FreePEGylationLinearLFluorescently labeledSyntheticAntidiabetesBlood collection at 5-min, 1-, 2-, 4-, 8-, 24-, 48-, 72-, 96-, 120-, 144- and 168-h1000 nmol/kg6.59 ± 0.27 (T1/2 Absorption)Naïve mice plasma proteaseFluorescence assayNaïve mice plasmaIn VivoPDB id: 1JRJNoneEC50 = 1.3 ± 0.2 nM
4374
366308262023
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
Ex-PEGMw39FreePEGylationLinearLFluorescently labeledSyntheticAntidiabetesBlood collection at 5-min, 1-, 2-, 4-, 8-, 24-, 48-, 72-, 96-, 120-, 144- and 168-h1000 nmol/kg6.6 ± 0.9 (T1/2 Absorption)Naïve mice plasma proteaseFluorescence assayNaïve mice plasmaIn VivoPDB id: 1JRJNoneEC50 = 2.7 ± 0.5 nM
4375
366308262023
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
Ex-POEGMAopt39FreePOEGMA conjugationN.A.LFluorescently labeledSyntheticAntidiabetesBlood collection at 5-min, 1-, 2-, 4-, 8-, 24-, 48-, 72-, 96-, 120-, 144- and 168-h1000 nmol/kg9.1 ± 0.9 (T1/2 Absorption)Naïve mice plasma proteaseFluorescence assayNaïve mice plasmaIn VivoPDB id: 1JRJNoneEC50 = 2.8 ± 0.7 nM
4376
366308262023
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
Exendin39FreeAmidationLinearLFluorescently labeledIsolated from the saliva of the Gila monster lizard (Heloderma suspectum)AntidiabetesBlood collection at 5-min, 1-, 2-, 4-, 8-, 24-, 48-, 72-, 96-, 120-, 144- and 168-h1000 nmol/kg0.77 ± 0.07 (T1/2 Absorption)Naïve mice plasma proteaseFluorescence assayNaïve mice plasmaIn VivoPDB id: 1JRJNoneEC50 = 0.04 ± 0.01 nM for exendin
4377
380928942023
N.A.
tag-free rhMFG-E8387Cystatin SFreeLinearLGlycosylationDerived from Expi293F Human cellsantiinflammatoryBlood samples (100 μl per time point) were collected at 0, 3, 6, 9, 12 and 15 min, then every 15 min for the first 60 min till 2 hours50 µg11.55 (Distribution Half Life)SD rats plasma proteaseELISASD rats plasmaIn VivoNoneNoneLD50/30 (lethal dose, 50% at 30 days) falls between 14.5 Gy and 15 Gy after partial body irradiation (PBI) in mice treated with vehicle (normal saline),
4378
369970032023
Y-Aib-QGTFTSDYSKYLDERRAKEFVQWLMNTC
HM1513630IgG Fc linked at N terminus through MAL-PEG-ALD linkerFreeCyclic (lactam bridge between E16-K20)LAib2 modificationSyntheticTreatment of Hyperinsulinemic HypoglycemiaBlood (0.3 mL) was collected from the retro-orbital plexus at 0.25, 0.5, 1, 4, 8, 24, 48, 72, 96, 120, 144, 168, 192, 216, 240, 264, 288, 312, and 336 h after IV administration 260 μg/kg54.5Mouse serum proteaseModified ELISAMouse serumIn Vivohttps://www.nature.com/articles/s41598-022-21251-yNoneEC50 of HM15136 was 0.024 ± 0.006 nM while that of native glucagon was 0.003 ± 0.001 nM for hGCGR
4379
369970032023
Y-Aib-QGTFTSDYSKYLDERRAKEFVQWLMNTC
HM1513630IgG Fc linked at N terminus through MAL-PEG-ALD linkerFreeCyclic (lactam bridge between E16-K20)LAib2 modificationSyntheticTreatment of Hyperinsulinemic HypoglycemiaBlood (0.3 mL) was collected from the retro-orbital plexus at 1, 4, 8, 24, 48, 72, 96, 120, 144, 168, 192, 216, 240, 264, 288, 312, and 336 h after SC administration 260 μg/kg32.3Mouse serum proteaseModified ELISAMouse serumIn Vivohttps://www.nature.com/articles/s41598-022-21251-yNoneEC50 of HM15136 was 0.024 ± 0.006 nM while that of native glucagon was 0.003 ± 0.001 nM for hGCGR
4380
369970032023
Y-Aib-QGTFTSDYSKYLDERRAKEFVQWLMNTC
HM1513630IgG Fc linked at N terminus through MAL-PEG-ALD linkerFreeCyclic (lactam bridge between E16-K20)LAib2 modificationSyntheticTreatment of Hyperinsulinemic HypoglycemiaBlood (0.3 mL) was collected from the retro-orbital plexus at 0.25, 0.5, 1, 4, 8, 24, 48, 72, 96, 120, 144, 168, 192, 216, 240, 264, 288, 312, and 336 h after IV administration 260 μg/kg66.4 ± 33.0Rats serum proteaseModified ELISARats serumIn Vivohttps://www.nature.com/articles/s41598-022-21251-yNoneEC50 of HM15136 was 0.024 ± 0.006 nM while that of native glucagon was 0.003 ± 0.001 nM for hGCGR
4381
369970032023
Y-Aib-QGTFTSDYSKYLDERRAKEFVQWLMNTC
HM1513630IgG Fc linked at N terminus through MAL-PEG-ALD linkerFreeCyclic (lactam bridge between E16-K20)LAib2 modificationSyntheticTreatment of Hyperinsulinemic HypoglycemiaBlood (0.3 mL) was collected from the retro-orbital plexus at 1, 4, 8, 24, 48, 72, 96, 120, 144, 168, 192, 216, 240, 264, 288, 312, and 336 h after SC administration 260 μg/kg40.9 ± 17.7Rats serum proteaseModified ELISARats serumIn Vivohttps://www.nature.com/articles/s41598-022-21251-yNoneEC50 of HM15136 was 0.024 ± 0.006 nM while that of native glucagon was 0.003 ± 0.001 nM for hGCGR
4382
369970032023
Y-Aib-QGTFTSDYSKYLDERRAKEFVQWLMNTC
HM1513630IgG Fc linked at N terminus through MAL-PEG-ALD linkerFreeCyclic (lactam bridge between E16-K20)LAib2 modificationSyntheticTreatment of Hyperinsulinemic HypoglycemiaBlood (0.3 mL) was collected from the retro-orbital plexus at 0.25, 0.5, 1, 4, 8, 24, 48, 72, 96, 120, 144, 168, 192, 216, 240, 264, 288, 312, and 336 h after IV administration 52 μg/kg24.9 ± 2.2Dogs serum proteaseModified ELISADogs serumIn Vivohttps://www.nature.com/articles/s41598-022-21251-yNoneEC50 of HM15136 was 0.024 ± 0.006 nM while that of native glucagon was 0.003 ± 0.001 nM for hGCGR
4383
369970032023
Y-Aib-QGTFTSDYSKYLDERRAKEFVQWLMNTC
HM1513630IgG Fc linked at N terminus through MAL-PEG-ALD linkerFreeCyclic (lactam bridge between E16-K20)LAib2 modificationSyntheticTreatment of Hyperinsulinemic HypoglycemiaBlood (0.3 mL) was collected from the retro-orbital plexus at 1, 4, 8, 24, 48, 72, 96, 120, 144, 168, 192, 216, 240, 264, 288, 312, and 336 h after SC administration 52 μg/kg26.6 ± 1.5Dogs serum proteaseModified ELISADogs serumIn Vivohttps://www.nature.com/articles/s41598-022-21251-yNoneEC50 of HM15136 was 0.024 ± 0.006 nM while that of native glucagon was 0.003 ± 0.001 nM for hGCGR
4384
369970032023
HsQGTFTSDLSKQKDSRRAQDFIEWLKNGGPSSGAPPPS
Compound 1440FreeAmidationLinearMixD-Ser2 substiuition, Lys14 side chain linked to C16 fatty acid via linker yE-C16GLP-1 analogsDual GLP-1/Glucagon receptor agonistThe mice were sacrificed, and blood samples were collected after 0.083, 0.25, 1, 2, 4, 8, 16, and 24 h after application1 mg/kg3.2C57/B16 female mice plasma proteaseLC−MS/MSC57/B16 female mice plasmaIn Vivohttps://www.nature.com/articles/s41598-022-21251-yNoneGLP-1 receptor : EC50 = 3.9 pM
4385
369970032023
HsQGTFTSDLSKQMDSRRAQDFIEWLKNGGPSSGAPPPSK
Compound 1541FreeTerminal Lys side chain linked to C16 fatty acid via linker yE-C16 at C terminalLinearMixD-Ser2 substiuitionGLP-1 analogsDual GLP-1/Glucagon receptor agonistThe mice were sacrificed, and blood samples were collected after 0.083, 0.25, 1, 2, 4, 8, 16, and 24 h after application1 mg/kg2.2C57/B16 female mice plasma proteaseLC−MS/MSC57/B16 female mice plasmaIn Vivohttps://www.nature.com/articles/s41598-022-21251-yNoneGLP-1 receptor : EC50 = 5.2 pM
4386
369970032023
HAEGTFTSDVSSYLEGQAAKEFIAWLVRGRG
Liraglutide32FreeFreeLinearLLys20 side chain linked to C16 fatty acid via linker yE-C16GLP-1 analogsDual GLP-1/Glucagon receptor agonistThe mice were sacrificed, and blood samples were collected after 0.083, 0.25, 1, 2, 4, 8, 16, and 24 h after application1 mg/kg3.6C57/B16 female mice plasma proteaseLC−MS/MSC57/B16 female mice plasmaIn Vivohttps://www.nature.com/articles/s41598-022-21251-yNoneGLP-1 receptor : EC50 = 6.4 pM
4387
372426502023
RPVNLTMRRKLRKHNCLQRRCMPLHRSVPFP
ELA32pGlu = PyroglutamateFreeCyclic (C17-C22 disulfide bond)LNoneHuman derivedEndogenous Ligand of APJIncubated at 37°C for 2, 5 and 10 min1 mMAlmost completely degraded after 2 minRats plasma proteaseHPLC-MSRats plasmaIn Vitrohttps://pubmed.ncbi.nlm.nih.gov/26986036/NoneGαi1 EC50 (nM) = 5.3 ± 2.5
4388
373299002023
N.A.
KAN-101N.A.N.A.N.A.N.A.N.A.Liver-targeting glycosylation signature conjugated to a deaminated gliadin peptideN.A.Liver-Targeted Immune Tolerance TherapyN.A.0·15 mg/kg, 0·3 mg/kg, 0·6 mg/kg, 1·2 mg/kg, 1·5 mg/kg3·72 to 31·72 Human proteaseN.A.HumanIn VivoNoneNoneN.A.
4389
369970032023
Y-Aib-QGTFTSDYSKYLDERRAKEFVQWLMNTCLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSQEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKGLPSSIEKTISKAKGQPREPQVYTFPPSQEEMTKNQVSLRCLVKGFYPSDIAVEWESNGQPENNYKTTKPVLDSDGSFRLESRLTVDKSRWQEGNVFSCSVMHEALHNHYTQKSLSLS
HM15136240FreeHMC001Cyclic (E36-K40 lactam bridge in GCG analog)LAib, GC15136 and HMC001 are linked via a 10-kDa, bifunctional maleimide-polyethylene glycol-aldehyde (MAL-PEG-ALD) linkerGlucagon analogTreatment of Congenital HyperinsulinismBlood (0.3 mL) was collected from the retro-orbital plexus at 0.25, 0.5, 1, 4, 8, 24, 48, 72, 96, 120, 144, 168, 192, 216, 240, 264, 288, 312, and 336 h after IV administration and at 1, 4, 8, 24, 48, 72, 96, 120, 144, 168, 192, 216, 240, 264, 288, 312, and 336 h after SC administration of HM15136260 μg/kg54.5Mouse serum proteaseELISAMouse serumIn VivoPDB id: 5HVW, https://pubmed.ncbi.nlm.nih.gov/36202918/NoneKD (HM15136) = No binding for FcγRIA, FcγRIIA, FcγRIIB/C, FcγRIIIA, FcγRIIIB, C1q
4390
369970032023
Y-Aib-QGTFTSDYSKYLDERRAKEFVQWLMNTCLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSQEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKGLPSSIEKTISKAKGQPREPQVYTFPPSQEEMTKNQVSLRCLVKGFYPSDIAVEWESNGQPENNYKTTKPVLDSDGSFRLESRLTVDKSRWQEGNVFSCSVMHEALHNHYTQKSLSLS
HM15136240FreeHMC001Cyclic (E36-K40 lactam bridge in GCG analog)LAib, GC15136 and HMC001 are linked via a 10-kDa, bifunctional maleimide-polyethylene glycol-aldehyde (MAL-PEG-ALD) linkerGlucagon analogTreatment of Congenital HyperinsulinismBlood (0.3 mL) was collected from the retro-orbital plexus at 0.25, 0.5, 1, 4, 8, 24, 48, 72, 96, 120, 144, 168, 192, 216, 240, 264, 288, 312, and 336 h after IV administration and at 1, 4, 8, 24, 48, 72, 96, 120, 144, 168, 192, 216, 240, 264, 288, 312, and 336 h after SC administration of HM15136260 μg/kg32.3Mouse serum proteaseELISAMouse serumIn VivoPDB id: 5HVW, https://pubmed.ncbi.nlm.nih.gov/36202918/NoneKD (HM15136) = No binding for FcγRIA, FcγRIIA, FcγRIIB/C, FcγRIIIA, FcγRIIIB, C1q
4391
369970032023
Y-Aib-QGTFTSDYSKYLDERRAKEFVQWLMNTCLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSQEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKGLPSSIEKTISKAKGQPREPQVYTFPPSQEEMTKNQVSLRCLVKGFYPSDIAVEWESNGQPENNYKTTKPVLDSDGSFRLESRLTVDKSRWQEGNVFSCSVMHEALHNHYTQKSLSLS
HM15136240FreeHMC001Cyclic (E36-K40 lactam bridge in GCG analog)LAib, GC15136 and HMC001 are linked via a 10-kDa, bifunctional maleimide-polyethylene glycol-aldehyde (MAL-PEG-ALD) linkerGlucagon analogTreatment of Congenital HyperinsulinismBlood (0.3 mL) was collected from the retro-orbital plexus at 0.25, 0.5, 1, 4, 8, 24, 48, 72, 96, 120, 144, 168, 192, 216, 240, 264, 288, 312, and 336 h after IV administration and at 1, 4, 8, 24, 48, 72, 96, 120, 144, 168, 192, 216, 240, 264, 288, 312, and 336 h after SC administration of HM15136260 μg/kg66.4 ± 33.0Rats serum proteaseELISARats serumIn VivoPDB id: 5HVW, https://pubmed.ncbi.nlm.nih.gov/36202918/NoneKD (HM15136) = No binding for FcγRIA, FcγRIIA, FcγRIIB/C, FcγRIIIA, FcγRIIIB, C1q
4392
369970032023
Y-Aib-QGTFTSDYSKYLDERRAKEFVQWLMNTCLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSQEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKGLPSSIEKTISKAKGQPREPQVYTFPPSQEEMTKNQVSLRCLVKGFYPSDIAVEWESNGQPENNYKTTKPVLDSDGSFRLESRLTVDKSRWQEGNVFSCSVMHEALHNHYTQKSLSLS
HM15136240FreeHMC001Cyclic (E36-K40 lactam bridge in GCG analog)LAib, GC15136 and HMC001 are linked via a 10-kDa, bifunctional maleimide-polyethylene glycol-aldehyde (MAL-PEG-ALD) linkerGlucagon analogTreatment of Congenital HyperinsulinismBlood (0.3 mL) was collected from the retro-orbital plexus at 0.25, 0.5, 1, 4, 8, 24, 48, 72, 96, 120, 144, 168, 192, 216, 240, 264, 288, 312, and 336 h after IV administration and at 1, 4, 8, 24, 48, 72, 96, 120, 144, 168, 192, 216, 240, 264, 288, 312, and 336 h after SC administration of HM15136260 μg/kg40.9 ± 17.7Rats serum proteaseELISARats serumIn VivoPDB id: 5HVW, https://pubmed.ncbi.nlm.nih.gov/36202918/NoneKD (HM15136) = No binding for FcγRIA, FcγRIIA, FcγRIIB/C, FcγRIIIA, FcγRIIIB, C1q
4393
369970032023
Y-Aib-QGTFTSDYSKYLDERRAKEFVQWLMNTCLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSQEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKGLPSSIEKTISKAKGQPREPQVYTFPPSQEEMTKNQVSLRCLVKGFYPSDIAVEWESNGQPENNYKTTKPVLDSDGSFRLESRLTVDKSRWQEGNVFSCSVMHEALHNHYTQKSLSLS
HM15136240FreeHMC001Cyclic (E36-K40 lactam bridge in GCG analog)LAib, GC15136 and HMC001 are linked via a 10-kDa, bifunctional maleimide-polyethylene glycol-aldehyde (MAL-PEG-ALD) linkerGlucagon analogTreatment of Congenital HyperinsulinismBlood (0.3 mL) was collected from the retro-orbital plexus at 0.25, 0.5, 1, 4, 8, 24, 48, 72, 96, 120, 144, 168, 192, 216, 240, 264, 288, 312, and 336 h after IV administration and at 1, 4, 8, 24, 48, 72, 96, 120, 144, 168, 192, 216, 240, 264, 288, 312, and 336 h after SC administration of HM1513652 μg/kg24.9 ± 2.2Dogs serum proteaseELISADogs serumIn VivoPDB id: 5HVW, https://pubmed.ncbi.nlm.nih.gov/36202918/NoneKD (HM15136) = No binding for FcγRIA, FcγRIIA, FcγRIIB/C, FcγRIIIA, FcγRIIIB, C1q
4394
369970032023
Y-Aib-QGTFTSDYSKYLDERRAKEFVQWLMNTCLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSQEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKGLPSSIEKTISKAKGQPREPQVYTFPPSQEEMTKNQVSLRCLVKGFYPSDIAVEWESNGQPENNYKTTKPVLDSDGSFRLESRLTVDKSRWQEGNVFSCSVMHEALHNHYTQKSLSLS
HM15136240FreeHMC001Cyclic (E36-K40 lactam bridge in GCG analog)LAib, GC15136 and HMC001 are linked via a 10-kDa, bifunctional maleimide-polyethylene glycol-aldehyde (MAL-PEG-ALD) linkerGlucagon analogTreatment of Congenital HyperinsulinismBlood (0.3 mL) was collected from the retro-orbital plexus at 0.25, 0.5, 1, 4, 8, 24, 48, 72, 96, 120, 144, 168, 192, 216, 240, 264, 288, 312, and 336 h after IV administration and at 1, 4, 8, 24, 48, 72, 96, 120, 144, 168, 192, 216, 240, 264, 288, 312, and 336 h after SC administration of HM1513652 μg/kg26.6 ± 1.5Dogs serum proteaseELISADogs serumIn VivoPDB id: 5HVW, https://pubmed.ncbi.nlm.nih.gov/36202918/NoneKD (HM15136) = No binding for FcγRIA, FcγRIIA, FcγRIIB/C, FcγRIIIA, FcγRIIIB, C1q
4395
365887172022
GEPPPPGKPADDAGLV
BPC15715FreeFreeLinearLNoneIsolated from human gastric juiceTreatment of various wounds in rats and dogsBlood samples were collected from rats in groups one to four at the corresponding time points before (0 h) and within 6 h after BPC157 administration20 μg/kg15.2SD rats plasma proteaseLC-MS/MSSD rats plasma In VivoNoneNoneN.A.
4396
365887172022
GEPPPPGKPADDAGLV
BPC15715FreeFreeLinearLNoneIsolated from human gastric juiceTreatment of various wounds in rats and dogsBlood samples were collected from rats in group five before the last three doses and within 6 h after the last dose100 μg/kg18.5SD rats plasma proteaseLC-MS/MSSD rats plasma dosed with BPC once a day for seven consecutive daysIn VivoNoneNoneN.A.
4397
365887172022
GEPPPPGKPADDAGLV
BPC15715FreeFreeLinearLNoneIsolated from human gastric juiceTreatment of various wounds in rats and dogsBlood samples were collected from rats in groups one to four at the corresponding time points before (0 h) and within 6 h after BPC157 administration20 μg/kg7.87SD rats plasma proteaseLC-MS/MSSD rats plasma In VivoNoneNoneN.A.
4398
365887172022
GEPPPPGKPADDAGLV
BPC15715FreeFreeLinearLNoneIsolated from human gastric juiceTreatment of various wounds in rats and dogsBlood samples were collected from rats in group five before the last three doses and within 6 h after the last dose100 μg/kg17.1SD rats plasma proteaseLC-MS/MSSD rats plasma dosed with BPC once a day for seven consecutive daysIn VivoNoneNoneN.A.
4399
365887172022
GEPPPPGKPADDAGLV
BPC15715FreeFreeLinearLNoneIsolated from human gastric juiceTreatment of various wounds in rats and dogsBlood samples were collected from rats in groups one to four at the corresponding time points before (0 h) and within 6 h after BPC157 administration500 μg/kg29.7SD rats plasma proteaseLC-MS/MSSD rats plasma In VivoNoneNoneN.A.
4400
365887172022
GEPPPPGKPADDAGLV
BPC15715FreeFreeLinearLNoneIsolated from human gastric juiceTreatment of various wounds in rats and dogsBlood samples were collected at the corresponding time points before (0 h) and within 6 h of a single administration6 μg/kg5.27 ± 2.25Beagle Dogs Plasma ProteaseLC-MS/MSbeagle dogs plasmaIn VivoNoneNoneN.A.
4401
365887172022
GEPPPPGKPADDAGLV
BPC15715FreeFreeLinearLNoneIsolated from human gastric juiceTreatment of various wounds in rats and dogsBlood samples were collected from dogs administered multiple doses at corresponding time points before the first dosing (0 h), within 6 h after dosing, before the last three doses, and at corresponding time points after the last dosing30 μg/kg19.6 ± 3.72Beagle Dogs Plasma ProteaseLC-MS/MSbeagle dogs plasma with repeated dose of 30 μg/kg for seven consecutive daysIn VivoNoneNoneN.A.
4402
365887172022
GEPPPPGKPADDAGLV
BPC15715FreeFreeLinearLNoneIsolated from human gastric juiceTreatment of various wounds in rats and dogsBlood samples were collected at the corresponding time points before (0 h) and within 6 h of a single administration6 μg/kg20.0 ± 5.53Beagle Dogs Plasma ProteaseLC-MS/MSbeagle dogs plasmaIn VivoNoneNoneN.A.
4403
365887172022
GEPPPPGKPADDAGLV
BPC15715FreeFreeLinearLNoneIsolated from human gastric juiceTreatment of various wounds in rats and dogsBlood samples were collected at the corresponding time points before (0 h) and within 6 h of a single administration30 μg/kg25.5 ± 7.08Beagle Dogs Plasma ProteaseLC-MS/MSbeagle dogs plasmaIn VivoNoneNoneN.A.
4404
365887172022
GEPPPPGKPADDAGLV
BPC15715FreeFreeLinearLNoneIsolated from human gastric juiceTreatment of various wounds in rats and dogsBlood samples were collected at the corresponding time points before (0 h) and within 6 h of a single administration150 μg/kg29.3 ± 5.06Beagle Dogs Plasma ProteaseLC-MS/MSbeagle dogs plasmaIn VivoNoneNoneN.A.
4405
365887172022
GEPPPPGKPADDAGLV
[3H]BPC15715FreeFreeLinearLall Proline radiolabelled with [3H]Isolated from human gastric juiceTreatment of various wounds in rats and dogsWhole blood and plasma samples of six JVC rats were collected at 0.05, 0.167, 0.5, 1, 2, 4, 8, 24, 48, and 72 h after administration (three males and three females at each time point) for the examination of radio pharmacokinetics of total plasma100 µg/300 μCi/kg 102 ± 32 JVC rats plasma proteaseLiquid scintillation counterJVC Rats plasmaIn VivoNoneNoneN.A.
4406
365592782022
PCKNFFWKTFSSCK
Native CST14FreeFreeCyclic (C2-C13 Disulfide Linkage)LNoneNeuropeptideAntiinflammatory37 °C6 mg/mL2Human plasma proteaseN.A.Human plasmaIn Vitrohttps://pmc.ncbi.nlm.nih.gov/articles/PMC7994712/NoneIC50(nM) = 1.7 (relative affinities of CST for the different Somatostatin receptor SSTR1)
4407
365592782022
PCKNFFWKTFSSCK
Native CST14FreeFreeCyclic (C2-C13 Disulfide Linkage)LNoneNeuropeptideAntiinflammatory37 °C6 mg/mL2Human plasma proteaseN.A.Human plasmaIn VitroNoneNoneIC50(nM) = 0.09 (relative affinities of CST for the different Somatostatin receptor SSTR2)
4408
365592782022
PCKNFFWKTFSSCK
Native CST14FreeFreeCyclic (C2-C13 Disulfide Linkage)LNoneNeuropeptideAntiinflammatory37 °C6 mg/mL2Human plasma proteaseN.A.Human plasmaIn VitroNoneNoneIC50(nM) = 0.3 (relative affinities of CST for the different Somatostatin receptor SSTR3)
4409
365592782022
PCKNFFWKTFSSCK
Native CST14FreeFreeCyclic (C2-C13 Disulfide Linkage)LNoneNeuropeptideAntiinflammatory37 °C6 mg/mL2Human plasma proteaseN.A.Human plasmaIn VitroNoneNoneIC50(nM) = 0.2 (relative affinities of CST for the different Somatostatin receptor SSTR4)
4410
365592782022
PCKNFFWKTFSSCK
Native CST14FreeFreeCyclic (C2-C13 Disulfide Linkage)LNoneNeuropeptideAntiinflammatory37 °C6 mg/mL2Human plasma proteaseN.A.Human plasmaIn VitroNoneNoneIC50(nM) = 0.3 (relative affinities of CST for the different Somatostatin receptor SSTR1)
4411
365592782022
PCKN-Mesityl-AFwKTFSSCK
CST analogue 514N-octanoylFreeCyclic (C2-C13 Disulfide Linkage)Mixw=D-Trp,MesitylCST analogueAntiinflammatory37 °C6 mg/mL21Human plasma proteaseN.A.Human plasmaIn VitroNoneNoneIC50(nM) = 47.3 (relative affinities of A5 for the different Somatostatin receptor SSTR1)
4412
365592782022
PCKN-Mesityl-AFwKTFSSCK
CST analogue 514N-octanoylFreeCyclic (C2-C13 Disulfide Linkage)Mixw=D-Trp,MesitylCST analogueAntiinflammatory37 °C6 mg/mL21Human plasma proteaseN.A.Human plasmaIn VitroNoneNoneIC50(nM) = 35 (relative affinities of A5 for the different Somatostatin receptor SSTR2)
4413
365592782022
PCKN-Mesityl-AFwKTFSSCK
CST analogue 514N-octanoylFreeCyclic (C2-C13 Disulfide Linkage)Mixw=D-Trp,MesitylCST analogueAntiinflammatory37 °C6 mg/mL21Human plasma proteaseN.A.Human plasmaIn VitroNoneNoneIC50(nM) = 5.1 (relative affinities of A5 for the different Somatostatin receptor SSTR3)
4414
365592782022
PCKN-Mesityl-AFwKTFSSCK
CST analogue 514N-octanoylFreeCyclic (C2-C13 Disulfide Linkage)Mixw=D-Trp,MesitylCST analogueAntiinflammatory37 °C6 mg/mL21Human plasma proteaseN.A.Human plasmaIn VitroNoneNoneIC50(nM) = 4.1 (relative affinities of A5 for the different Somatostatin receptor SSTR4)
4415
365592782022
PCKN-Mesityl-AFwKTFSSCK
CST analogue 514N-octanoylFreeCyclic (C2-C13 Disulfide Linkage)Mixw=D-Trp,MesitylCST analogueAntiinflammatory37 °C6 mg/mL21Human plasma proteaseN.A.Human plasmaIn VitroNoneNoneIC50(nM) = 1.12 (relative affinities of A5 for the different Somatostatin receptor SSTR1)
4416
365578502022
pGlu-HWSYlLRP 
Leuprolide9pGlu = PyroglutamateNHEt (Ethylamine)LinearMixd-Leucine6 substituitions SyntheticAnticancer (Treatment of Advanced Prostate Cancer)Blood sample of approximately 0.3 mL was collected via femoral artery cannulation at various time points (0, 1, 3, 5, 10, 20, 30, 60, 90, 120, 180, 240, 360, 480, and 600 min)0.1 mg/kg38.2 ± 4.3 (Terminal Elimination Half Life)Male SD Rats Plasma ProteaseUPLC-MS/MSMale SD rats plasmaIn VivoNoneNoneN.A.
4417
365578502022
HWSYlLRP
LOC9FreeLeuprolide acetate with the hydroxyl groups of leuprolide acetateLinearMixOle = oleic acid conjugationSyntheticAnticancer (Treatment of Advanced Prostate Cancer)Blood sample of approximately 0.3 mL was collected via femoral artery cannulation at various time points (0, 1, 3, 5, 10, 20, 30, 60, 90, 120, 180, 240, 360, 480, and 600 min)0.122 mg/kg172 ± 66 (Terminal Elimination Half Life)Male SD Rats Plasma ProteaseUPLC-MS/MSMale SD rats plasmaIn VivoNoneNoneN.A.
4418
365578502022
pGlu-HWSYlLRP 
Leuprolide9pGlu = PyroglutamateNHEt (Ethylamine)LinearMixd-Leucine6 substituitions SyntheticAnticancer (Treatment of Advanced Prostate Cancer)Blood sample of approximately 0.3 mL was collected via femoral artery cannulation at various time points (0, 1, 3, 5, 10, 20, 30, 60, 90, 120, 180, 240, 360, 480, and 600 min)0.1 mg/kg166 ± 38Male SD Rats Plasma ProteaseUPLC-MS/MSMale SD rats plasma after LOC peptide administrationIn VivoNoneNoneN.A.
4419
364993572022
ILRWSRKLPCVS
JM#2112FreeFreeLinearLCysteine was introduced at position 10SyntheticAnticancer, AntiinflammatoryFive microliter aliquots were separated after 0, 5, 10, 20, 30, 45, 60, 90, and 120 min7 µM1.7Human plasma proteaseFlow cytometry-based functional assay and mass spectrometryHuman plasmaIn VitroNoneNoneN.A.
4420
364993572022
IVRWSKKVPCVS
WSC0212FreeFreeLinearLCysteine was introduced in the sequence of both peptides at position 10SyntheticAnticancer, AntiinflammatoryFive microliter aliquots were separated after 0, 5, 10, 20, 30, 45, 60, 90, and 120 min7 µM0.7Human plasma proteaseFlow cytometry-based functional assay and mass spectrometryHuman plasmaIn VitroNoneNoneN.A.
4421
364993572022
ILRWSRKLPCVS
JM#2112FreeFreeLinearLCysteine was introduced at position 10SyntheticAnticancer, AntiinflammatoryFive microliter aliquots were separated after 0, 5, 10, 20, 30, 45, 60, 90, and 120 min7 µM7Human plasma proteaseAntibody-competition assayHuman plasmaIn VitroNoneNoneN.A.
4422
364993572022
IVRWSKKVPCVS
WSC0212FreeFreeLinearLCysteine was introduced in the sequence of both peptides at position 10SyntheticAnticancer, AntiinflammatoryFive microliter aliquots were separated after 0, 5, 10, 20, 30, 45, 60, 90, and 120 min7 µM9Human plasma proteaseFunctional stability assayHuman plasmaIn VitroNoneNoneN.A.
4423
364993572022
IVRWSKKVPCVS
WSC02 12FreeFreeLinearLCysteine was introduced in the sequence of both peptides at position 10SyntheticAnticancer, AntiinflammatoryFive microliter aliquots were separated after 0, 5, 10, 20, 30, 45, 60, 90, and 120 min7 µM6Human plasma proteaseFunctional stability assayHuman plasma after GuHCl + DTT treatmentIn VitroNoneNoneN.A.
4424
364993572022
ILRWSRKLPCVS
JM#2112FreeFreeLinearLCysteine was introduced at position 10SyntheticAnticancer, AntiinflammatoryFive microliter aliquots were separated after 0, 5, 10, 20, 30, 45, 60, 90, and 120 min7 µM5Human plasma proteaseMass spectrometryHuman plasma after GuHCl + DTT treatmentIn VitroNoneNoneN.A.
4425
364993572022
IVRWSKKVPSVS
WSC02 (C10S)12FreeFreeLinearLCys10 replaced by Ser10SyntheticAnticancer, AntiinflammatoryFive microliter aliquots were separated after 0, 5, 10, 20, 30, 45, 60, 90, and 120 min7 µM4Human plasma proteaseMass spectrometryHuman plasmaIn VitroNoneNoneN.A.
4426
364993572022
IVRWSKKVPCVS
WSC02 (Cdm)12FreeFreeLinearLCarbamidomethylation of Cys10 residue = CdmSyntheticAnticancer, AntiinflammatoryFive microliter aliquots were separated after 0, 5, 10, 20, 30, 45, 60, 90, and 120 min7 µM5Human plasma proteaseMass spectrometryHuman plasmaIn VitroNoneNoneN.A.
4427
364993572022
ILRWSRKLPSVS
JM#21 (C10S)12FreeFreeLinearLCys replaced by SerSyntheticAnticancer, AntiinflammatoryFive microliter aliquots were separated after 0, 5, 10, 20, 30, 45, 60, 90, and 120 min7 µM4Human plasma proteaseMass spectrometryHuman plasmaIn VitroNoneNoneN.A.
4428
364993572022
ILRWSRKLPCVS
JM#21 (Cdm)12FreeFreeLinearLCarbamidomethylation of Cys residue = CdmSyntheticAnticancer, AntiinflammatoryFive microliter aliquots were separated after 0, 5, 10, 20, 30, 45, 60, 90, and 120 min7 µM3Human plasma proteaseMass spectrometryHuman plasmaIn VitroNoneNoneN.A.
4429
364993572022
IVRWSKKVPCVS
WSC02 (Cdm)12FreeFreeLinearLCarbamidomethylation of Cys residue = CdmSyntheticAnticancer, AntiinflammatoryFive microliter aliquots were separated after 0, 5, 10, 20, 30, 45, 60, 90, and 120 min20 µM6Human plasma proteaseFunctional stability assayHuman plasmaIn VitroNoneNoneN.A.
4430
364993572022
IVRWSKKVPSVS
WSC02 (C10S)12FreeFreeLinearLCys replaced by SerSyntheticAnticancer, AntiinflammatoryFive microliter aliquots were separated after 0, 5, 10, 20, 30, 45, 60, 90, and 120 min20 µM7Human plasma proteaseFunctional stability assayHuman plasmaIn VitroNoneNoneN.A.
4431
364993572022
ILRWSRKLPCVS
JM#21 (Cdm)12FreeFreeLinearLCarbamidomethylation of Cys residue = CdmSyntheticAnticancer, AntiinflammatoryFive microliter aliquots were separated after 0, 5, 10, 20, 30, 45, 60, 90, and 120 min20 µM3Human plasma proteaseFunctional stability assayHuman plasmaIn VitroNoneNoneN.A.
4432
364993572022
ILRWSRKLPSVS
JM#21 (C10S)12FreeFreeLinearLCys replaced by SerSyntheticAnticancer, AntiinflammatoryFive microliter aliquots were separated after 0, 5, 10, 20, 30, 45, 60, 90, and 120 min20 µM4Human plasma proteaseFunctional stability assayHuman plasmaIn VitroNoneNoneN.A.
4433
364714332022
EVQLVESGGGLYQPGNSLTLSCVASGFTFSNYGMHWIRQAPKKGLEWIAMITYDSSKMNYADTVKGRFTISRDNSKNTLYEMNSLRSEDTAMYYCAYPTSHYVVDVWGQGYSVTVSSGSTSGGGSGGGSGGGGSSDIQMTQSPASLSASLEEIVTITCQASQDIGNWLAWTQQKPGKSPQLLIYGATSLADGVPSRFSQSRSGTQFSLKISRYQVEDIGIYYCLQAYNTPWTFGGGTKLELKRASAPGSGGGSAPGEPRYPITQNPSPPLKECPPCAAPDLLGGPSYFIFPPKIKDVLMISLSPMYTCVVVDVSEDDPDYQISWFVNNYEVHTAQTQTHREDYNSTLRVVSALPIQHQDWMSGKEFKCKYNNRALPSPIEKTISKPRGPVRAPQVYVLPPPAEEMTKKEFSLTCMITGFLPAEIAVDWTSNGRTEQNYKNTATYLDSDGSYFMYSKLRVQKSTWERGSLFACSVVHEGLHNHLTTKTISRSLGPGGGGSGGGGSGGGGSEPRYPITQNPSPPLKECPPCAAPDLLGGPSVFIFPPKIKDVLMISLSPMVTCVVVDVSEDDPDYQISWFVNNVEVHTAQTQTHREDYNSTLRYVSALPIQHQDWMSGKEFKCKVNNRALPSPIEKTISKPRGPYRAPQVYVLPPPAEEMTKKEFSLTCMITGFLPAEIAVDWTSNGRTEQNYKNTATVLDSDGSYFMYSKLRVQKSTWERGSLFACSVVHEGLHNHLTTKTISRSLG-APGSGGGSAPG-YDDGICKSSDCIKSAARLIQNMDASVEPCTDFFKYACGGWLKRNVIPETSSRYSNFDILRDELEVILKDVLQEPKTEDIVAVQKAKTLYRSCINESAIDSRGGQPLLKLLPDIYGWPVASDNWDQTYGTSWTAEKSIAQLNSKYGKKVLINFFVGTDDKNSTQHIIHFDQPRLGLPSRDYYECTGIYKEACTAYVDFMISVARLIRQEQSLPIDENQLSLEMNKVMELEKEIANATTKPEDRNDPMLLYNKMTLAKLQNNFSLEYNGKSFSWSNFTNEIMSTVNINIQNEEEVVVYAPEYLTKLKPILTKYSPRDLQNLMSWRFIMDLVSSLSRNYKESRNAFRKALYGTTSETATWRRCANYVNGNMENAVGRLYVEAAFAGESKHVVEDLIAQIREVFIQTLDDLTWMDAETKKKAEEKALAIKERIGYPDDIISNENKLNNEYLELNYREDEYFENIIQNLKFSQSKQLKKLREKVDKDEWISGAAVVNAFYSSGRNQIVFPAGILQPPFFSAQQSNSLNYGGIGMVIGHEITHGFDDNGRNFNKDGDLVDWWTQQSANNFKDQSQCMVYQYGNFSWDLAGGQHLNGINTLGENIADNGGIGQAYRAYQNYVKKNGEEKLLPGLDLNHKQLFFLNFAQVWCGTYRPEYAYNSIKTDVHSPGNFRIIGTLQNSAEFADAFHCRKNSYMNPERKCRVW
[125I]sNEP-scFv8D3-scFc 1456sNEP (amino acid 52–749 of NEP) recombinantly linked to a single-chain fragment constant (scFc) of mouse IgG2c antibody at N terminus using linkerScFc then attached to the BBB transporter (scFv8D3) at C terminus using linkerLinearL125I labeledFusion protein of sNEP-scFc-scFv8D3 Treatment of Alzheimer's diseasesBlood samples collected from the tail vein at 1, 4, 6, 24, 48 and 72 h post-administration5 mg/kg16Tg-Arcswe Mice Plasma Proteaseinstant thin layer chromatography (iTLC)Tg-ArcSwe mice plasma In VivoNoneNoneN.A.
4434
364714332022
EVQLVESGGGLYQPGNSLTLSCVASGFTFSNYGMHWIRQAPKKGLEWIAMITYDSSKMNYADTVKGRFTISRDNSKNTLYEMNSLRSEDTAMYYCAYPTSHYVVDVWGQGYSVTVSSGSTSGGGSGGGSGGGGSSDIQMTQSPASLSASLEEIVTITCQASQDIGNWLAWTQQKPGKSPQLLIYGATSLADGVPSRFSQSRSGTQFSLKISRYQVEDIGIYYCLQAYNTPWTFGGGTKLELKRASAPGSGGGSAPGEPRYPITQNPSPPLKECPPCAAPDLLGGPSYFIFPPKIKDVLMISLSPMYTCVVVDVSEDDPDYQISWFVNNYEVHTAQTQTHREDYNSTLRVVSALPIQHQDWMSGKEFKCKYNNRALPSPIEKTISKPRGPVRAPQVYVLPPPAEEMTKKEFSLTCMITGFLPAEIAVDWTSNGRTEQNYKNTATYLDSDGSYFMYSKLRVQKSTWERGSLFACSVVHEGLHNHLTTKTISRSLGPG-GGGSGGGGSGGGGS-EPRYPITQNPSPPLKECPPCAAPDLLGGPSVFIFPPKIKDVLMISLSPMVTCVVVDVSEDDPDYQISWFVNNVEVHTAQTQTHREDYNSTLRYVSALPIQHQDWMSGKEFKCKVNNRALPSPIEKTISKPRGPYRAPQVYVLPPPAEEMTKKEFSLTCMITGFLPAEIAVDWTSNGRTEQNYKNTATVLDSDGSYFMYSKLRVQKSTWERGSLFACSVVHEGLHNHLTTKTISRSLG-APGSGGGSAPG-YDDGICKSSDCIKSAARLIQNMDASVEPCTDFFKYACGGWLKRNVIPETSSRYSNFDILRDELEVILKDVLQEPKTEDIVAVQKAKTLVRSCINESAIDSRGGQPLLKLLPDIYGWPVASDNWDQTYGTSWTAEKSIAQLNSKYGKKVLINFFVGTDDKNSTQHIIHFDQPRLGLPSRDYYECTGIYKEACTAYVDFMISVARLIRQEQSLPIDENQLSLEMNKVMELEKEIANATTKPEDRNDPMLLYNKMTLAKLQNNFSLEYNGKSFSWSNFTNEIMSTVNINIQNEEEVVVYAPEYLTKLKPILTKYSPRDLQNLMSWRFIMDLVSSLSRNYKESRNAFRKALYVTTSETATWRRCANYVNGNMENAVGRLYVEAAFAGESKHVVEDLIAQIREVFIQTLDDLTWMDAETKKKAEEKALAIKERIGYPDDIISNENKLNNEYLELNYREDEYFENIIQNLKFSQSKQLKKLREKVDKDEWISGAAVVNAFYSSGRNQIVFPAGILQPPFFSAQQSNSLNYGGIGMVIGHEITHGFDDNGRNFNKDGDLVDWWTQQSANNFKDQSQCMVYQYGNFSWDLAGGQHLNGINTLGENIADNGGIGQAYRAYQNYVKKNGEEKLLPGLDLNHKQLFFLNFAQVWCGTYRPEYAYNSIKTDVHSPKNFRIIGTLQNSAEFADAFHCRKNSYMNPERKCRVW
[125I]muNEP-scFv8D3-scFc1456sNEP (amino acid 52–749 of NEP) recombinantly linked to a single-chain fragment constant (scFc) of mouse IgG2c antibody at N terminus using linkerScFc then attached to the BBB transporter (scFv8D3) at C terminus using linkerLinearL125I labeledFusion protein of sNEP-scFc-scFv8D3 Treatment of Alzheimer's diseasesBlood samples collected from the tail vein at 1, 4, 6, 24, 48 and 72 h post-administration2.5 mg/kg 18Tg-Arcswe Mice Plasma Proteaseinstant thin layer chromatography (iTLC)Tg-ArcSwe mice plasma In VivoNoneNoneN.A.
4435
364433812022
LEGREKVRAKI-Aib-Aib-EG-Nle-STWS-Aib-RKKK
SA10SC-RLX 25AcetylationAmidationLinearLAttachment of a lipid moiety (C18-γ-Glu-PEG2) at K25 position, Aib, Nle,acetylation of Lys10SyntheticTreatment for Chronic Fibrotic and Cardiovascular DiseasesBlood samples were collected from individual animals at the following time points: 0.083, 0.25, 0.5, 1, 3, 6, 8, 24, 48 and 72 h (IV route) and 0.25, 0.5, 1, 2, 4, 8, 12, 24, 48 and 72 h (SC route)1 mg/kg4 (Terminal Half Life)Rats plasma proteaseLC-HRMSRats plasmaIn VivoNoneNoneEC50 (nM) = 0.8 for EA.hy926_hRXFP1 
4436
364433812022
LEGREKVRAKI-Aib-Aib-EG-Nle-STWS-Aib-RKKK
SA10SC-RLX 25AcetylationAmidationLinearLAttachment of a lipid moiety (C18-γ-Glu-PEG2) at K34 position, Aib, NleSyntheticTreatment for Chronic Fibrotic and Cardiovascular DiseasesBlood samples were collected from individual animals at the following time points: 0.083, 0.25, 0.5, 2, 4, 6, 8, 24, 48, 72, 96 and 168 h (IV route) and 0.25, 0.5, 2, 4, 6, 8, 24, 48, 72, 96 and 168 h (SC route)1 mg/kg7 (Terminal Half Life)Göttingen minipigs plasma proteaseLC-MS/MSGöttingen minipigs plasmaIn VivoNoneNoneEC50 (nM) = 0.8 for EA.hy926_hRXFP1 
4437
364432912022
FSSE
Entry 1 (aka P5779)4FreeAmidationLinearLNoneSyntheticInhibitor of Hmgb1/Md-2/Tlr4 Complex FormationAliquots (200 μL) were taken at each time point (0, 5, 10, 15, 20, 30, 60 and 120 minutes)0.1 mg/ml2.0 ± 0.1C57Bl/6 J mouse serum proteaseLC-MS/MSC57BL/6 J male mouse serumIn VitroNoneNoneHMGb1:MD-2 inhibition (IC50) = 68.5 nM
4438
364432912022
azaF-SS-azaE
Entry 2 (Azapeptide 51)4Aza-Phe at postion 1Amidation, Aza-glutamic acid (azaE4) modification at position 4 (E4)LinearLNoneP5779 analoguesInhibitor of Hmgb1/Md-2/Tlr4 Complex FormationAliquots (200 μL) were taken at each time point (0, 5, 10, 15, 20, 30, 60 and 120 minutes)0.1 mg/ml>120C57Bl/6 J mouse serum proteaseLC-MS/MSC57BL/6 J male mouse serumIn VitroNoneNoneHMGb1:MD-2 inhibition (IC50) = 90 nM
4439
364432912022
azaF-SSE
Entry 3 (Azapeptide 52)4Aza-Phe at postion 1AmidationLinearLNoneP5779 analoguesInhibitor of Hmgb1/Md-2/Tlr4 Complex FormationAliquots (200 μL) were taken at each time point (0, 5, 10, 15, 20, 30, 60 and 120 minutes)0.1 mg/ml>120C57Bl/6 J mouse serum proteaseLC-MS/MSC57BL/6 J male mouse serumIn VitroNoneNoneHMGb1:MD-2 inhibition (IC50) = 249 nM
4440
364432912022
FSS-azaE
Entry 4 (Azapeptide 53)4FreeAza-glutamic acid (azaE4) modification at position 4 (E4)LinearLNoneP5779 analoguesInhibitor of Hmgb1/Md-2/Tlr4 Complex FormationAliquots (200 μL) were taken at each time point (0, 5, 10, 15, 20, 30, 60 and 120 minutes)0.1 mg/ml2.6 ± 0.11C57Bl/6 J mouse serum proteaseLC-MS/MSC57BL/6 J male mouse serumIn VitroNoneNoneHMGb1:MD-2 inhibition (IC50) = 396.8 nM
4441
364432912022
azaF-SSE
Entry 5 (Azapeptide 54)4Aza-Phe at postion 1AmidationLinearLNoneP5779 analoguesInhibitor of Hmgb1/Md-2/Tlr4 Complex FormationAliquots (200 μL) were taken at each time point (0, 5, 10, 15, 20, 30, 60 and 120 minutes)0.1 mg/ml>120C57Bl/6 J mouse serum proteaseLC-MS/MSC57BL/6 J male mouse serumIn VitroNoneNoneHMGb1:MD-2 inhibition (IC50) = 127.4 nM
4442
364432912022
azaF-SSQ
Entry 6 (Azapeptide 55)4Aza-Phe at postion 1Amidation, Q amino acid subtituition at place of E at C terminalLinearLNoneP5779 analoguesInhibitor of Hmgb1/Md-2/Tlr4 Complex FormationAliquots (200 μL) were taken at each time point (0, 5, 10, 15, 20, 30, 60 and 120 minutes)0.1 mg/ml24.4 ± 1.6C57Bl/6 J mouse serum proteaseLC-MS/MSC57BL/6 J male mouse serumIn VitroNoneNoneHMGb1:MD-2 inhibition (IC50) = 159.3 nM
4443
364432912022
azaF-SSQ
Entry 7 (Azapeptide 56)4Aza-Phe at postion 1Amidation, Q amino acid subtituition at place of E at C terminalLinearLNoneP5779 analoguesInhibitor of Hmgb1/Md-2/Tlr4 Complex FormationAliquots (200 μL) were taken at each time point (0, 5, 10, 15, 20, 30, 60 and 120 minutes)0.1 mg/ml>120C57Bl/6 J mouse serum proteaseLC-MS/MSC57BL/6 J male mouse serumIn VitroNoneNoneHMGb1:MD-2 inhibition (IC50) = 348.7 nM
4444
364432912022
azaF-SS-azaQ
Entry 8 (Azapeptide 57)4Aza-Phe at postion 1Amidation, Aza-glutamine (azaQ4) LinearLNoneP5779 analoguesInhibitor of Hmgb1/Md-2/Tlr4 Complex FormationAliquots (200 μL) were taken at each time point (0, 5, 10, 15, 20, 30, 60 and 120 minutes)0.1 mg/ml>120C57Bl/6 J mouse serum proteaseLC-MS/MSC57BL/6 J male mouse serumIn VitroNoneNoneHMGb1:MD-2 inhibition (IC50) = 83 nM
4445
364432912022
FSS-azaQ
Entry 9 (Azapeptide 58)4FreeAmidation, Aza-glutamine (azaQ4) LinearLNoneP5779 analoguesInhibitor of Hmgb1/Md-2/Tlr4 Complex FormationAliquots (200 μL) were taken at each time point (0, 5, 10, 15, 20, 30, 60 and 120 minutes)0.1 mg/ml2.9 ± 0.20C57Bl/6 J mouse serum proteaseLC-MS/MSC57BL/6 J male mouse serumIn VitroNoneNoneHMGb1:MD-2 inhibition (IC50) = 422.9 nM
4446
364432912022
RPPGFSPFR
Entry 1 (Bradykinin)9FreeFreeLinearLNoneDerived from kininogen Effects on Pain, Inflammation, Edema/Vasodilation and Blood PressureAliquots (200 μL) were taken at each time point (0, 5, 10, 15, 20, 30, 60 and 120 minutes)0.1 mg/ml5.29 ± 0.5C57Bl/6 J mouse serum proteaseLC-MS/MSC57BL/6 J male mouse serumIn VitroNoneNoneEC50(nM) = 44.4 (PEG2 induction in Fibroblasts)
4447
364432912022
azaR-PPGFSPFR
Entry 2 (azaR1-BK)9Modified at position 1 with an aza-amino acid (aza-arginine)FreeLinearLNoneAza-bradykinin analoguesEffects on Pain, Inflammation, Edema/Vasodilation and Blood PressureAliquots (200 μL) were taken at each time point (0, 5, 10, 15, 20, 30, 60 and 120 minutes)0.1 mg/ml2.46 ± 0.05C57Bl/6 J mouse serum proteaseLC-MS/MSC57BL/6 J male mouse serumIn VitroNoneNoneN.A.
4448
364432912022
R-azaP-PGFSPFR
Entry 3(azaP2-BK)9FreeFreeLinearLModified at position 2 with an aza-amino acid (aza-proline)Aza-bradykinin analoguesEffects on Pain, Inflammation, Edema/Vasodilation and Blood PressureAliquots (200 μL) were taken at each time point (0, 5, 10, 15, 20, 30, 60 and 120 minutes)0.1 mg/ml5.40 ± 1.1C57Bl/6 J mouse serum proteaseLC-MS/MSC57BL/6 J male mouse serumIn VitroNoneNoneEC50(nM) = 61.1 (PEG2 induction in Fibroblasts)
4449
364432912022
RP-azaP-GFSPFR
Entry 4 (azaP3-BK)9FreeFreeLinearLModified at position 3 with an aza-amino acid (aza-proline)Aza-bradykinin analoguesEffects on Pain, Inflammation, Edema/Vasodilation and Blood PressureAliquots (200 μL) were taken at each time point (0, 5, 10, 15, 20, 30, 60 and 120 minutes)0.1 mg/ml2.63 ± 0.25C57Bl/6 J mouse serum proteaseLC-MS/MSC57BL/6 J male mouse serumIn VitroNoneNoneN.A.
4450
364432912022
RPP-azaG-FSPFR
Entry 5 (azaG4-BK)9FreeFreeLinearLModified at position 4 with an aza-amino acid (aza-glycine)Aza-bradykinin analoguesEffects on Pain, Inflammation, Edema/Vasodilation and Blood PressureAliquots (200 μL) were taken at each time point (0, 5, 10, 15, 20, 30, 60 and 120 minutes)0.1 mg/ml4.33 ± 1.3C57Bl/6 J mouse serum proteaseLC-MS/MSC57BL/6 J male mouse serumIn VitroNoneNoneN.A.
4451
364432912022
RPPG-azaF-SPFR
Entry 6 (azaF5-BK)9FreeFreeLinearLModified at position 5 with an aza-amino acid (aza-phenylalanine)Aza-bradykinin analoguesEffects on Pain, Inflammation, Edema/Vasodilation and Blood PressureAliquots (200 μL) were taken at each time point (0, 5, 10, 15, 20, 30, 60 and 120 minutes)0.1 mg/ml14.7 ± 1.6C57Bl/6 J mouse serum proteaseLC-MS/MSC57BL/6 J male mouse serumIn VitroNoneNoneN.A.
4452
364432912022
RPPGFS-azaP-FR
Entry 7 (azaP7-BK)9FreeFreeLinearLModified at position 7 with an aza-amino acid (aza-proline)Aza-bradykinin analoguesEffects on Pain, Inflammation, Edema/Vasodilation and Blood PressureAliquots (200 μL) were taken at each time point (0, 5, 10, 15, 20, 30, 60 and 120 minutes)0.1 mg/ml2.38 ± 0.03C57Bl/6 J mouse serum proteaseLC-MS/MSC57BL/6 J male mouse serumIn VitroNoneNoneN.A.
4453
364432912022
RPPGFSP-azaF-R
Entry 8 (azaF8-BK)9FreeFreeLinearLModified at position 8 with an aza-amino acid (aza-phenylalanine)Aza-bradykinin analoguesEffects on Pain, Inflammation, Edema/Vasodilation and Blood PressureAliquots (200 μL) were taken at each time point (0, 5, 10, 15, 20, 30, 60 and 120 minutes)0.1 mg/ml39.3 ± 2.5C57Bl/6 J mouse serum proteaseLC-MS/MSC57BL/6 J male mouse serumIn VitroNoneNoneEC50(nM) = 99.6 (PEG2 induction in Fibroblasts)
4454
364432912022
RPPGFSPF-azaR
Entry 9 (azaR9-BK)9FreeFreeLinearLModified at position 9 with an aza-amino acid (aza-arginine)Aza-bradykinin analoguesEffects on Pain, Inflammation, Edema/Vasodilation and Blood PressureAliquots (200 μL) were taken at each time point (0, 5, 10, 15, 20, 30, 60 and 120 minutes)0.1 mg/ml42.6 ± 0.8C57Bl/6 J mouse serum proteaseLC-MS/MSC57BL/6 J male mouse serumIn VitroNoneNoneN.A.
4455
364432912022
R-azaP-PGFSP-azaF-R
Entry 10 ([azaP2, azaF8]-BK)9FreeFreeLinearLModified at both positions 2 and 8 with aza-amino acids (aza-proline and aza-phenylalanine, respectively)Aza-bradykinin analoguesEffects on Pain, Inflammation, Edema/Vasodilation and Blood PressureAliquots (200 μL) were taken at each time point (0, 5, 10, 15, 20, 30, 60 and 120 minutes)0.1 mg/ml29.2 ± 3.8C57Bl/6 J mouse serum proteaseLC-MS/MSC57BL/6 J male mouse serumIn VitroNoneNoneEC50(nM) = 80.6 (PEG2 induction in Fibroblasts)
4456
364432912022
RPPG-azaF-SP-azaF-R
Entry 11 ([azaF5, azaF8]-BK)9FreeFreeLinearLModified at both positions 5 and 8 with aza-amino acids (aza-phenylalanine)Aza-bradykinin analoguesEffects on Pain, Inflammation, Edema/Vasodilation and Blood PressureAliquots (200 μL) were taken at each time point (0, 5, 10, 15, 20, 30, 60 and 120 minutes)0.1 mg/ml105.8 ± 1.8C57Bl/6 J mouse serum proteaseLC-MS/MSC57BL/6 J male mouse serumIn VitroNoneNoneN.A.
4457
363809172022
HAEGTFTSDVSSYLEGQAAKEFIAWLVKGRG
GLP-131FreeFreeLinearLNoneGlucagonAntidiabetes37 °C0.3 nmol10.2 ± 0.4 DPP-IVRP-HPLC50 mM Tris–HCl (pH 7.4) buffer + 10 ng μL−1 DPPIV In VitroPDB id: 5VAINoneBGLmax (mmol L−1) = 19.27 ± 1.41 (In vivo glucose stabilizing capability) 
4458
363809172022
HAEGTFTSDVSSYLEGQAAKEFIAWLVKGRG
GLP-131FreeFreeLinearLNoneGlucagonAntidiabetes37 °C6 nmol55.7 ± 12.1Mouse serum proteaseRP-HPLCMouse serumIn VitroPDB id: 5VAINoneBGLmax (mmol L−1) = 19.27 ± 1.41 (In vivo glucose stabilizing capability)
4459
363809172022
HAEGTFTSNVSSYLEGQAAKEFIAWLVKGRG
Glc-GLP-1-131FreeFreeLinearLGlucosylation at Asn15GLP-1 analogsAntidiabetes37 °C0.3 nmol 30.2 ± 2.4 DPP-IVRP-HPLC50 mM Tris–HCl (pH 7.4) buffer + 10 ng μL−1 DPPIV In VitroNoneNoneN.A.
4460
363809172022
HAEGTFTSNVSSYLEGQAAKEFIAWLVKGRG
Glc-GLP-1-131FreeFreeLinearLGlucosylation at Asn15GLP-1 analogsAntidiabetes37 °C6 nmol94.1 ± 7.6Mouse serum proteaseRP-HPLCMouse serumIn VitroNoneNoneN.A.
4461
363809172022
HAEGTFTSDVSSYLEGQAANESIAWLVKGRG
Glc-GLP-1-331FreeFreeLinearLGlucosylation at Asn26GLP-1 analogsAntidiabetes37 °C0.3 nmol 46.1 ± 3.5 DPP-IVRP-HPLC50 mM Tris–HCl (pH 7.4) buffer + 10 ng μL−1 DPPIV In VitroNoneNoneN.A.
4462
363809172022
HAEGTFTSDVSSYLEGQAANESIAWLVKGRG
Glc-GLP-1-331FreeFreeLinearLGlucosylation at Asn26GLP-1 analogsAntidiabetes37 °C6 nmol138.8 ± 14.5Mouse serum proteaseRP-HPLCMouse serumIn VitroNoneNoneN.A.
4463
363809172022
HAEGTFTSDVSSYLEGQAAKEFIAWLVNGTG
Glc-GLP-1-531FreeFreeLinearLGlucosylation at Asn34GLP-1 analogsAntidiabetes37 °C0.3 nmol 32.5 ± 1.4 DPP-IVRP-HPLC50 mM Tris–HCl (pH 7.4) buffer + 10 ng μL−1 DPPIV In VitroNoneNoneN.A.
4464
363809172022
HAEGTFTSDVSSYLEGQAAKEFIAWLVNGTG
Glc-GLP-1-531FreeFreeLinearLGlucosylation at Asn34GLP-1 analogsAntidiabetes37 °C6 nmol113.3 ± 11.8Mouse serum proteaseRP-HPLCMouse serumIn VitroNoneNoneN.A.
4465
363809172022
HAEGTFTSNVSSYLEGQAAKEFIAWLVKGRG
Glycan-GLP-1-1(G2)31FreeFreeLinearLN-glycosylation with biantennary complex-type N-glycan at Asn15 (G2 glycoform = glycan)GLP-1 analogsAntidiabetes37 °C0.3 nmol 49.1 ± 5.7 DPP-IVRP-HPLC50 mM Tris–HCl (pH 7.4) buffer + 10 ng μL−1 DPPIV In VitroNoneNoneBGLmax (mmol L−1) = 24.44 ± 2.37 (In vivo glucose stabilizing capability) 
4466
363809172022
HAEGTFTSNVSSYLEGQAAKEFIAWLVKGRG
Glycan-GLP-1-1(G2)31FreeFreeLinearLN-glycosylation with biantennary complex-type N-glycan at Asn15 (G2 glycoform = glycan)GLP-1 analogsAntidiabetes37 °C6 nmol355.5 ± 9.3Mouse serum proteaseRP-HPLCMouse serumIn VitroNoneNoneBGLmax (mmol L−1) = 24.44 ± 2.37 (In vivo glucose stabilizing capability) 
4467
363809172022
HAEGTFTSNVSSYLEGQAAKEFIAWLVKGRG
Glycan-GLP-1-1(G2S2)31FreeFreeLinearLN-glycosylation with sialylated biantennary complex-type N-glycan at Asn15 (G2S2 glycoform = sialylated glycan)GLP-1 analogsAntidiabetes37 °C0.3 nmol 145.7 ± 4.3 DPP-IVRP-HPLC50 mM Tris–HCl (pH 7.4) buffer + 10 ng μL−1 DPPIV In VitroNoneNoneBGLmax (mmol L−1) = 28.71 ± 2.63 (In vivo glucose stabilizing capability) 
4468
363809172022
HAEGTFTSNVSSYLEGQAAKEFIAWLVKGRG
Glycan-GLP-1-1(G2S2)31FreeFreeLinearLN-glycosylation with sialylated biantennary complex-type N-glycan at Asn15 (G2S2 glycoform = sialylated glycan)GLP-1 analogsAntidiabetes37 °C6 nmol736.6 ± 12.3Mouse serum proteaseRP-HPLCMouse serumIn VitroNoneNoneBGLmax (mmol L−1) = 28.71 ± 2.63 (In vivo glucose stabilizing capability) 
4469
363809172022
HAEGTFTSDVSSYLEGQAANESIAWLVKGRG
Glycan-GLP-1-3(G2)31FreeFreeLinearLN-glycosylation with biantennary complex-type N-glycan at Asn26 (G2 glycoform = glycan)GLP-1 analogsAntidiabetes37 °C0.3 nmol 185.3 ± 1.1 DPP-IVRP-HPLC50 mM Tris–HCl (pH 7.4) buffer + 10 ng μL−1 DPPIV In VitroNoneNoneBGLmax (mmol L−1) = 24.07 ± 3.79 (In vivo glucose stabilizing capability) 
4470
363809172022
HAEGTFTSDVSSYLEGQAANESIAWLVKGRG
Glycan-GLP-1-3(G2)31FreeFreeLinearLN-glycosylation with biantennary complex-type N-glycan at Asn26 (G2 glycoform = glycan)GLP-1 analogsAntidiabetes37 °C6 nmol738.6 ± 9.7Mouse serum proteaseRP-HPLCMouse serumIn VitroNoneNoneBGLmax (mmol L−1) = 24.07 ± 3.79 (In vivo glucose stabilizing capability) 
4471
363809172022
HAEGTFTSDVSSYLEGQAANESIAWLVKGRG
Glycan-GLP-1-3(G2S2)31FreeFreeLinearLN-glycosylation with sialylated biantennary complex-type N-glycan at Asn26 (G2S2 glycoform = sialylated glycan)GLP-1 analogsAntidiabetes37 °C0.3 nmol 374.7 ± 1.8 DPP-IVRP-HPLC50 mM Tris–HCl (pH 7.4) buffer + 10 ng μL−1 DPPIV In VitroNoneNoneBGLmax (mmol L−1) = 25.71 ± 3.19 (In vivo glucose stabilizing capability) 
4472
363809172022
HAEGTFTSDVSSYLEGQAANESIAWLVKGRG
Glycan-GLP-1-3(G2S2)31FreeFreeLinearLN-glycosylation with sialylated biantennary complex-type N-glycan at Asn26(G2S2 glycoform = sialylated glycan)GLP-1 analogsAntidiabetes37 °C6 nmol1393.1 ± 8.9Mouse serum proteaseRP-HPLCMouse serumIn VitroNoneNoneBGLmax (mmol L−1) = 25.71 ± 3.19 (In vivo glucose stabilizing capability) 
4473
363809172022
HAEGTFTSDVSSYLEGQAAKEFIAWLVNGTG
Glycan-GLP-1-5(G2)31FreeFreeLinearLN-glycosylation with biantennary complex-type N-glycan at Asn34 (G2 glycoform = glycan)GLP-1 analogsAntidiabetes37 °C0.3 nmol 182.0 ± 0.1 DPP-IVRP-HPLC50 mM Tris–HCl (pH 7.4) buffer + 10 ng μL−1 DPPIV In VitroNoneNoneBGLmax (mmol L−1) = 14.50 ± 1.62 (In vivo glucose stabilizing capability) 
4474
363809172022
HAEGTFTSDVSSYLEGQAAKEFIAWLVNGTG
Glycan-GLP-1-5(G2)31FreeFreeLinearLN-glycosylation with biantennary complex-type N-glycan at Asn34 (G2 glycoform = glycan)GLP-1 analogsAntidiabetes37 °C6 nmol390.4 ± 13.5Mouse serum proteaseRP-HPLCMouse serumIn VitroNoneNoneBGLmax (mmol L−1) = 14.50 ± 1.62 (In vivo glucose stabilizing capability) 
4475
363809172022
HAEGTFTSDVSSYLEGQAAKEFIAWLVNGTG
Glycan-GLP-1-5(G2S2) 31FreeFreeLinearLN-glycosylation with sialylated biantennary complex-type N-glycan at Asn34 (G2S2 glycoform = sialylated glycan)GLP-1 analogsAntidiabetes37 °C0.3 nmol 245.3 ± 1.3 DPP-IVRP-HPLC50 mM Tris–HCl (pH 7.4) buffer + 10 ng μL−1 DPPIV In VitroNoneNoneBGLmax (mmol L−1) = 15.50 ± 3.74 (In vivo glucose stabilizing capability) 
4476
363809172022
HAEGTFTSDVSSYLEGQAAKEFIAWLVNGTG
Glycan-GLP-1-5(G2S2) 31FreeFreeLinearLN-glycosylation with sialylated biantennary complex-type N-glycan at Asn34 (G2S2 glycoform = sialylated glycan)GLP-1 analogsAntidiabetes37 °C6 nmol777.0 ± 10.2Mouse serum proteaseRP-HPLCMouse serumIn VitroNoneNoneBGLmax (mmol L−1) = 15.50 ± 3.74 (In vivo glucose stabilizing capability) 
4477
363239882022
HADGSFSDEMNTILDNLAARDFINWLIQTKITD
Glepaglutide 33FreeFreeLinearLNoneGLP-2 analogueTreatment of Short Bowel Syndrome blood sampling in subjects receiving 5 and 10 mg of glepaglutide once weekly occurred at the day 1 visit (pre-dose and 0.5, 1, 2, 4, 8, 12, 16, 20, 24, 36, 48, 60, 72, 96 and 120 h post-dose); pre-dose on days 8, 15, 22 and 29; and in connection with the last dosing visit on day 36 (pre-dose and 0.5, 1, 2, 4, 8, 12, 16, 20, 24, 36, 48, 72, 120, 168, 336, 504, 672 and 840 h post-dose)5 mg228Human plasma proteaseLC-MSHuman plasma after SC glepaglutide 5 mg after 6 once-weekly dosesIn VivoNoneNoneEC50 = 0.12 nM In vitro potency
4478
363239882022
HGEGTFSSELATILDALAARDFIAWLIATKITDKKKKKK
Glepaglutide parent39FreeSix lysines has been added at C terminal LinearLNoneGLP-2 analogueTreatment of Short Bowel Syndrome blood sampling in subjects receiving 5 and 10 mg of glepaglutide once weekly occurred at the day 1 visit (pre-dose and 0.5, 1, 2, 4, 8, 12, 16, 20, 24, 36, 48, 60, 72, 96 and 120 h post-dose); pre-dose on days 8, 15, 22 and 29; and in connection with the last dosing visit on day 36 (pre-dose and 0.5, 1, 2, 4, 8, 12, 16, 20, 24, 36, 48, 72, 120, 168, 336, 504, 672 and 840 h post-dose)5 mg3.8Human plasma proteaseLC-MSHuman plasma after SC glepaglutide 5 mg after 6 once-weekly dosesIn VivoNoneNoneEC50 = 0.12 nM In vitro potency
4479
363239882022
HGEGTFSSELATILDALAARDFIAWLIATKITDKK
Glepaglutide M135FreeTwo lysines has been added at C terminal LinearLNoneGLP-2 analogueTreatment of Short Bowel Syndrome blood sampling in subjects receiving 5 and 10 mg of glepaglutide once weekly occurred at the day 1 visit (pre-dose and 0.5, 1, 2, 4, 8, 12, 16, 20, 24, 36, 48, 60, 72, 96 and 120 h post-dose); pre-dose on days 8, 15, 22 and 29; and in connection with the last dosing visit on day 36 (pre-dose and 0.5, 1, 2, 4, 8, 12, 16, 20, 24, 36, 48, 72, 120, 168, 336, 504, 672 and 840 h post-dose)5 mg17Human plasma proteaseLC-MSHuman plasma after SC glepaglutide 5 mg after 6 once-weekly dosesIn VivoNoneNoneEC50 = 0.068 nM In vitro potency
4480
363239882022
HGEGTFSSELATILDALAARDFIAWLIATKITDK
Glepaglutide M234Free1 lysines has been added at C terminalLinearLNoneGLP-2 analogueTreatment of Short Bowel Syndrome blood sampling in subjects receiving 5 and 10 mg of glepaglutide once weekly occurred at the day 1 visit (pre-dose and 0.5, 1, 2, 4, 8, 12, 16, 20, 24, 36, 48, 60, 72, 96 and 120 h post-dose); pre-dose on days 8, 15, 22 and 29; and in connection with the last dosing visit on day 36 (pre-dose and 0.5, 1, 2, 4, 8, 12, 16, 20, 24, 36, 48, 72, 120, 168, 336, 504, 672 and 840 h post-dose)5 mg231Human plasma proteaseLC-MSHuman plasma after SC glepaglutide 5 mg after 6 once-weekly dosesIn VivoNoneNoneEC50 = 0.044 nM In vitro potency
4481
363239882022
HADGSFSDEMNTILDNLAARDFINWLIQTKITD
Glepaglutide 33FreeFreeLinearLNoneGLP-2 analogueTreatment of Short Bowel Syndrome blood sampling in subjects receiving 5 and 10 mg of glepaglutide once weekly occurred at the day 1 visit (pre-dose and 0.5, 1, 2, 4, 8, 12, 16, 20, 24, 36, 48, 60, 72, 96 and 120 h post-dose); pre-dose on days 8, 15, 22 and 29; and in connection with the last dosing visit on day 36 (pre-dose and 0.5, 1, 2, 4, 8, 12, 16, 20, 24, 36, 48, 72, 120, 168, 336, 504, 672 and 840 h post-dose)10 mg254Human plasma proteaseLC-MSHuman plasma after SC glepaglutide 5 mg after 6 once-weekly dosesIn VivoNoneNoneEC50 = 0.12 nM In vitro potency
4482
363239882022
HGEGTFSSELATILDALAARDFIAWLIATKITDKKKKKK
Glepaglutide parent39FreeSix lysines has been added at C terminal , AmidationLinearLNoneGLP-2 analogueTreatment of Short Bowel Syndrome blood sampling in subjects receiving 5 and 10 mg of glepaglutide once weekly occurred at the day 1 visit (pre-dose and 0.5, 1, 2, 4, 8, 12, 16, 20, 24, 36, 48, 60, 72, 96 and 120 h post-dose); pre-dose on days 8, 15, 22 and 29; and in connection with the last dosing visit on day 36 (pre-dose and 0.5, 1, 2, 4, 8, 12, 16, 20, 24, 36, 48, 72, 120, 168, 336, 504, 672 and 840 h post-dose)10 mg2.8Human plasma proteaseLC-MSHuman plasma after SC glepaglutide 5 mg after 6 once-weekly dosesIn VivoNoneNoneEC50 = 0.12 nM In vitro potency
4483
363239882022
HGEGTFSSELATILDALAARDFIAWLIATKITDKK
Glepaglutide M135FreeTwo lysines has been added at C terminal LinearLNoneGLP-2 analogueTreatment of Short Bowel Syndrome blood sampling in subjects receiving 5 and 10 mg of glepaglutide once weekly occurred at the day 1 visit (pre-dose and 0.5, 1, 2, 4, 8, 12, 16, 20, 24, 36, 48, 60, 72, 96 and 120 h post-dose); pre-dose on days 8, 15, 22 and 29; and in connection with the last dosing visit on day 36 (pre-dose and 0.5, 1, 2, 4, 8, 12, 16, 20, 24, 36, 48, 72, 120, 168, 336, 504, 672 and 840 h post-dose)10 mg37.7Human plasma proteaseLC-MSHuman plasma after SC glepaglutide 5 mg after 6 once-weekly dosesIn VivoNoneNoneEC50 = 0.068 nM In vitro potency
4484
363239882022
HGEGTFSSELATILDALAARDFIAWLIATKITDK
Glepaglutide M234Free1 lysines has been added at C terminalLinearLNoneGLP-2 analogueTreatment of Short Bowel Syndrome blood sampling in subjects receiving 5 and 10 mg of glepaglutide once weekly occurred at the day 1 visit (pre-dose and 0.5, 1, 2, 4, 8, 12, 16, 20, 24, 36, 48, 60, 72, 96 and 120 h post-dose); pre-dose on days 8, 15, 22 and 29; and in connection with the last dosing visit on day 36 (pre-dose and 0.5, 1, 2, 4, 8, 12, 16, 20, 24, 36, 48, 72, 120, 168, 336, 504, 672 and 840 h post-dose)10 mg255Human plasma proteaseLC-MSHuman plasma after SC glepaglutide 5 mg after 6 once-weekly dosesIn VivoNoneNoneEC50 = 0.044 nM In vitro potency
4485
363239882022
HADGSFSDEMNTILDNLAARDFINWLIQTKITD
Glepaglutide 33FreeFreeLinearLNoneGLP-2 analogueTreatment of Short Bowel Syndrome blood sampling in subjects receiving 5 and 10 mg of glepaglutide once weekly occurred at the day 1 visit (pre-dose and 0.5, 1, 2, 4, 8, 12, 16, 20, 24, 36, 48, 60, 72, 96 and 120 h post-dose); pre-dose on days 8, 15, 22 and 29; and in connection with the last dosing visit on day 36 (pre-dose and 0.5, 1, 2, 4, 8, 12, 16, 20, 24, 36, 48, 72, 120, 168, 336, 504, 672 and 840 h post-dose)10 mg88.3Human plasma proteaseLC-MSHuman plasma after SC glepaglutide 5 mg after 6 once-weekly dosesIn VivoNoneNoneEC50 = 0.044 nM In vitro potency
4486
363239882022
HADGSFSDEMNTILDNLAARDFINWLIQTKITD
Glepaglutide 33FreeFreeLinearLNoneGLP-2 analogueTreatment of Short Bowel Syndrome Blood sampling for a pharmacokineticanalysis in these subjects was conducted pre-dose and at 5,10, 15, 20, 25, 35, 45, 60, 75 and 90 min and 2, 3, 4, 8, 12,16, 20, 24, 36 and 48 h after the start of the IV infusion, and again on day 221 mg10.4Human plasma proteaseLC-MSHuman plasmaIn VivoNoneNoneEC50 = 0.12 nM In vitro potency
4487
363239882022
HGEGTFSSELATILDALAARDFIAWLIATKITDKKKKKK
Glepaglutide parent39FreeSix lysines has been added at C terminal , AmidationLinearLNoneGLP-2 analogueTreatment of Short Bowel Syndrome Blood sampling for a pharmacokineticanalysis in these subjects was conducted pre-dose and at 5,10, 15, 20, 25, 35, 45, 60, 75 and 90 min and 2, 3, 4, 8, 12,16, 20, 24, 36 and 48 h after the start of the IV infusion, and again on day 221 mg11.7Human plasma proteaseLC-MSHuman plasmaIn VivoNoneNoneEC50 = 0.12 nM In vitro potency
4488
363239882022
HGEGTFSSELATILDALAARDFIAWLIATKITDKK
Glepaglutide M135FreeTwo lysines has been added at C terminal LinearLNoneGLP-2 analogueTreatment of Short Bowel Syndrome Blood sampling for a pharmacokineticanalysis in these subjects was conducted pre-dose and at 5,10, 15, 20, 25, 35, 45, 60, 75 and 90 min and 2, 3, 4, 8, 12,16, 20, 24, 36 and 48 h after the start of the IV infusion, and again on day 221 mg1.2Human plasma proteaseLC-MSHuman plasmaIn VivoNoneNoneEC50 = 0.068 nM In vitro potency
4489
363239882022
HGEGTFSSELATILDALAARDFIAWLIATKITDK
Glepaglutide M234Free1 lysines has been added at C terminalLinearLNoneGLP-2 analogueTreatment of Short Bowel Syndrome Blood sampling for a pharmacokineticanalysis in these subjects was conducted pre-dose and at 5,10, 15, 20, 25, 35, 45, 60, 75 and 90 min and 2, 3, 4, 8, 12,16, 20, 24, 36 and 48 h after the start of the IV infusion, and again on day 221 mg2.6Human plasma proteaseLC-MSHuman plasmaIn VivoNoneNoneEC50 = 0.044 nM In vitro potency
4490
362325502022
CYIQNCGKG
ASK21319FreeFreeCyclic (C1-C6 Disulfide Bond)LNative oxytocin peptide was modified with a substitution of the Leu8 to a Lys appended with a polyethylene glycol space and a palmitoyl group and with a substitution of Gly for the Pro7 OXT analogsAntiobesitySerial blood samples (200 µL per time point) were obtained via tail nick using K3EDTA microvettes prior to and 1, 2, 4, 6, 12, and 24-h post-drug administration300 nmol/kg2.3Rats plasma proteaseLC-MS/MS Rats plasmaIn VivoNoneNoneEC50 = 1.1 nM (ASK2131 profile against OXTR )
4491
362325502022
CYIQNCGKG
ASK21319FreeFreeCyclic (C1-C6 Disulfide Bond)LNative oxytocin peptide was modified with a substitution of the Leu8 to a Lys appended with a polyethylene glycol space and a palmitoyl group and with a substitution of Gly for the Pro7 OXT analogsAntiobesitySerial blood samples (200 µL per time point) were obtained via tail nick using K3EDTA microvettes prior to and 1, 2, 4, 6, 12, and 24-h post-drug administration300 nmol/kg2.3Rats plasma proteaseLC-MS/MS Rats plasmaIn VivoNoneNonehV1aR, EC50 (nM) > 1000
4492
362325502022
CYIQNCGKG
ASK21319FreeFreeCyclic (C1-C6 Disulfide Bond)LNative oxytocin peptide was modified with a substitution of the Leu8 to a Lys appended with a polyethylene glycol space and a palmitoyl group and with a substitution of Gly for the Pro7 OXT analogsAntiobesitySerial blood samples (200 µL per time point) were obtained via tail nick using K3EDTA microvettes prior to and 1, 2, 4, 6, 12, and 24-h post-drug administration300 nmol/kg2.3Rats plasma proteaseLC-MS/MS Rats plasmaIn VivoNoneNonehV2R, EC50 (nM) = 0.36
4493
361427492022
Dmt-kFFKKPFTL
PK2010Replacing tyrosine (Tyr) with 2,6-dimethyltyrosine (Dmt) at position 1FreeLinearMixD-amino acid residue (D-Lys) inserted at position 2opioid–neurotensin hybrid peptideAnalgesic 37°C for 24 h50 μg/mL204.4N.A.LC-MS1M HClIn VitroNoneNoneEmax = 149.17% ± 2.9 for PK20 (intrinsic activity of the receptor)
4494
361427492022
Dmt-kFFKKPFTL
PK2010Replacing tyrosine (Tyr) with 2,6-dimethyltyrosine (Dmt) at position 1FreeLinearMixD-amino acid residue (D-Lys) inserted at position 2opioid–neurotensin hybrid peptideAnalgesic 37°C for 24 h50 μg/mL11.36N.A.LC-MS1M NaOHIn VitroNoneNoneEC50 = 79 nM (potency at mu opioid receptor)
4495
361427492022
Dmt-kFFKKPFIL
[Ile9]PK2010Replacing tyrosine (Tyr) with 2,6-dimethyltyrosine (Dmt) at position 1FreeLinearMixD-amino acid residue (D-Lys) inserted at position 2PK20 derivativeAnalgesic 37°C for 24 h50 μg/mL117.7N.A.LC-MS1M HClIn VitroNoneNoneEmax = 151.2% ± 74.5 for [Ile9]PK20 (intrinsic activity of the receptor)
4496
361427492022
Dmt-kFFKKPFIL
[Ile9]PK2010Replacing tyrosine (Tyr) with 2,6-dimethyltyrosine (Dmt) at position 1FreeLinearMixD-amino acid residue (D-Lys) inserted at position 2PK20 derivativeAnalgesic 37°C for 24 h50 μg/mL4.69N.A.LC-MS1M NaOHIn VitroNoneNoneEC50 = 1244 nM (potency at mu opioid receptor)
4497
361350982022
QDTDTWA
GNRs-AAP1-Cy57FreeFreeLinearLCy5 conjugationAAP1/AAP1-1/AAP1-2 modified GNRsAntiadhesive propertyAt 0, 0.08, 0.16, 0.33, 0.5, 1, 2, 6, 12, 24, 48, 72 h, adding 40 μL termination solution 1 mg/ml0.29 (T1/2 a)Mouse serum proteaseHPLC1 mL mouse serum In VitroNoneNoneN.A.
4498
361350982022
QDTDTWA
GNRs-AAP1-Cy57FreeFreeLinearLCy5 conjugationAAP1/AAP1-1/AAP1-2 modified GNRsAntiadhesive propertyAt 0, 0.08, 0.16, 0.33, 0.5, 1, 2, 6, 12, 24, 48, 72 h, adding 40 μL termination solution 1 mg/ml37.81 (T1/2 b )Mouse serum proteaseHPLC1 mL mouse serum In VitroNoneNoneN.A.
4499
361350982022
WTDAQTD
GNRs-AAP1-1-Cy57FreeFreeLinearLCy5 conjugationAAP1/AAP1-1/AAP1-2 modified GNRsAntiadhesive propertyAt 0, 0.08, 0.16, 0.33, 0.5, 1, 2, 6, 12, 24, 48, 72 h, adding 40 μL termination solution 1 mg/ml0.18 (T1/2 a)Mouse serum proteaseHPLC1 mL mouse serum In VitroNoneNoneN.A.
4500
361350982022
WTDAQTD
GNRs-AAP1-1-Cy57FreeFreeLinearLCy5 conjugationAAP1/AAP1-1/AAP1-2 modified GNRsAntiadhesive propertyAt 0, 0.08, 0.16, 0.33, 0.5, 1, 2, 6, 12, 24, 48, 72 h, adding 40 μL termination solution 1 mg/ml7.7 (T1/2 b)Mouse serum proteaseHPLC1 mL mouse serum In VitroNoneNoneN.A.
4501
361350982022
TADWTDQ
GNRs-AAP1-2-Cy57FreeFreeLinearLCy5 conjugationAAP1/AAP1-1/AAP1-2 modified GNRsAntiadhesive propertyAt 0, 0.08, 0.16, 0.33, 0.5, 1, 2, 6, 12, 24, 48, 72 h, adding 40 μL termination solution 1 mg/ml0.2 (T1/2 a)Mouse serum proteaseHPLC1 mL mouse serum In VitroNoneNoneN.A.
4502
361350982022
TADWTDQ
GNRs-AAP1-2-Cy57FreeFreeLinearLCy5 conjugationAAP1/AAP1-1/AAP1-2 modified GNRsAntiadhesive propertyAt 0, 0.08, 0.16, 0.33, 0.5, 1, 2, 6, 12, 24, 48, 72 h, adding 40 μL termination solution 1 mg/ml5 (T1/2 Β )Mouse serum proteaseHPLC1 mL mouse serum In VitroNoneNoneN.A.
4503
361127712022
CP-1Nal-dCM-HArg-DWSTP-HyP-WC
BT800916AcetylationConjugation to MMAE cytotoxin via a valine–citrulline (V-Citr) cleavable linker,Val-Citriline linker and BTC joined by spacer Sar10Bicyclic Mixcyclised on TATA (1,3,5-Triacryloylhexahydro-1,3,5-triazine), 1Nal - 3-(1-naphthyl)-L-alanine, HArg – homo-arginine, HyP – hydroxyproline, MMAE = Monomethyl auristatin E, Cys16 with amidation modification, D-Asp4 modificationBT8009 and MMAE cytotoxin hybridAnticancerN.A.1 mg/kg1Mouse plasma proteaseLC-MS/MSMouse plasmaIn VivoNoneNoneKD(nM) = 2.9±1.1 (Binding affinity for BT8009 binding to extracellular domains of Nectin-4 in Mouse)
4504
361127712022
CP-1Nal-dCM-HArg-DWSTP-HyP-WC
BT800916AcetylationConjugation to MMAE cytotoxin via a valine–citrulline (V-Citr) cleavable linker,Val-Citriline linker and BTC joined by spacer Sar10Bicyclic Mixcyclised on TATA (1,3,5-Triacryloylhexahydro-1,3,5-triazine), 1Nal - 3-(1-naphthyl)-L-alanine, HArg – homo-arginine, HyP – hydroxyproline, MMAE = Monomethyl auristatin E, Cys16 with amidation modification, D-Asp4 modificationBT8009 and MMAE cytotoxin hybridAnticancerN.A.1 mg/kg0.9Rats plasma proteaseLC-MS/MSRats plasmaIn VivoNoneNoneKD(nM) = 6.0±1.2 (Binding affinity for BT8009 binding to extracellular domains of Nectin-4 in Rat)
4505
361127712022
CP-1Nal-dCM-HArg-DWSTP-HyP-WC
BT800916AcetylationConjugation to MMAE cytotoxin via a valine–citrulline (V-Citr) cleavable linker,Val-Citriline linker and BTC joined by spacer Sar10Bicyclic Mixcyclised on TATA (1,3,5-Triacryloylhexahydro-1,3,5-triazine), 1Nal - 3-(1-naphthyl)-L-alanine, HArg – homo-arginine, HyP – hydroxyproline, MMAE = Monomethyl auristatin E, Cys16 with amidation modification, D-Asp4 modificationBT8009 and MMAE cytotoxin hybridAnticancerN.A.1.25 mg/kg1.7NHP plasma proteaseLC-MS/MSNHP plasmaIn VivoNoneNoneKD(nM) = 6.3±1.3 (Binding affinity for BT8009 binding to extracellular domains of Nectin-4 in NHP)
4506
361127712022
CP-1Nal-dCM-HArg-DWSTP-HyP-WC
BT800916AcetylationConjugation to MMAE cytotoxin via a valine–citrulline (V-Citr) cleavable linker,Val-Citriline linker and BTC joined by spacer Sar10Bicyclic Mixcyclised on TATA (1,3,5-Triacryloylhexahydro-1,3,5-triazine), 1Nal - 3-(1-naphthyl)-L-alanine, HArg – homo-arginine, HyP – hydroxyproline, MMAE = Monomethyl auristatin E, Cys16 with amidation modification, D-Asp4 modificationBT8009 and MMAE cytotoxin hybridAnticancer24 hours2 µM>57.8Human plasma proteaseLC-MS/MSHuman plasmaIn VitroNoneNoneKD(nM) = 2.5±1.3 (Binding affinity for BT8009 binding to extracellular domains of Nectin-4 in human)
4507
361127712022
CP-1Nal-dCM-HArg-DWSTP-HyP-WC
BT800916AcetylationConjugation to MMAE cytotoxin via a valine–citrulline (V-Citr) cleavable linker,Val-Citriline linker and BTC joined by spacer Sar10Bicyclic Mixcyclised on TATA (1,3,5-Triacryloylhexahydro-1,3,5-triazine), 1Nal - 3-(1-naphthyl)-L-alanine, HArg – homo-arginine, HyP – hydroxyproline, MMAE = Monomethyl auristatin E, Cys16 with amidation modification, D-Asp4 modificationBT8009 and MMAE cytotoxin hybridAnticancer24 hours2 µM>57.8NHP plasma proteaseLC-MS/MSNHP plasmaIn VitroNoneNoneKD(nM) = 6.3±1.3 (Binding affinity for BT8009 binding to extracellular domains of Nectin-4 in NHP)
4508
361127712022
CP-1Nal-dCM-HArg-DWSTP-HyP-WC
BT800916AcetylationConjugation to MMAE cytotoxin via a valine–citrulline (V-Citr) cleavable linker,Val-Citriline linker and BTC joined by spacer Sar10Bicyclic Mixcyclised on TATA (1,3,5-Triacryloylhexahydro-1,3,5-triazine), 1Nal - 3-(1-naphthyl)-L-alanine, HArg – homo-arginine, HyP – hydroxyproline, MMAE = Monomethyl auristatin E, Cys16 with amidation modification, D-Asp4 modificationBT8009 and MMAE cytotoxin hybridAnticancer24 hours2 µM60.7Rats plasma proteaseLC-MS/MSRats plasmaIn VitroNoneNoneKD(nM) = 6.0±1.2 (Binding affinity for BT8009 binding to extracellular domains of Nectin-4 in Rat)
4509
361127712022
CP-1Nal-dCM-HArg-DWSTP-HyP-WC
BT800916AcetylationConjugation to MMAE cytotoxin via a valine–citrulline (V-Citr) cleavable linker,Val-Citriline linker and BTC joined by spacer Sar10Bicyclic Mixcyclised on TATA (1,3,5-Triacryloylhexahydro-1,3,5-triazine), 1Nal - 3-(1-naphthyl)-L-alanine, HArg – homo-arginine, HyP – hydroxyproline, MMAE = Monomethyl auristatin E, Cys16 with amidation modification, D-Asp4 modificationBT8009 and MMAE cytotoxin hybridAnticancer24 hours2 µM2.3 - 4.4Mouse plasma proteaseLC-MS/MSMouse plasmaIn VitroNoneNoneKD(nM) = 2.9±1.1 (Binding affinity for BT8009 binding to extracellular domains of Nectin-4 in Mouse)
4510
361127712022
CP-1Nal-dCM-HArg-DWSTP-HyP-WC
BT800916AcetylationConjugation to MMAE cytotoxin via a valine–citrulline (V-Citr) cleavable linker,Val-Citriline linker and BTC joined by spacer Sar10Bicyclic Mixcyclised on TATA (1,3,5-Triacryloylhexahydro-1,3,5-triazine), 1Nal - 3-(1-naphthyl)-L-alanine, HArg – homo-arginine, HyP – hydroxyproline, MMAE = Monomethyl auristatin E, Cys16 with amidation modification, D-Asp4 modificationBT8009 and MMAE cytotoxin hybridAnticancer24 hours2 µM26.1Human blood ProteaseLC-MS/MSHuman blood sampleIn VitroNoneNoneKD(nM) = 2.5±1.3 (Binding affinity for BT8009 binding to extracellular domains of Nectin-4 in human)
4511
361127712022
CP-1Nal-dCM-HArg-DWSTP-HyP-WC
BT800916AcetylationConjugation to MMAE cytotoxin via a valine–citrulline (V-Citr) cleavable linker,Val-Citriline linker and BTC joined by spacer Sar10Bicyclic Mixcyclised on TATA (1,3,5-Triacryloylhexahydro-1,3,5-triazine), 1Nal - 3-(1-naphthyl)-L-alanine, HArg – homo-arginine, HyP – hydroxyproline, MMAE = Monomethyl auristatin E, Cys16 with amidation modification, D-Asp4 modificationBT8009 and MMAE cytotoxin hybridAnticancer24 hours2 µM28.3NHP blood proteaseLC-MS/MSNHP blood sampleIn VitroNoneNoneKD(nM) = 6.3±1.3 (Binding affinity for BT8009 binding to extracellular domains of Nectin-4 in NHP)
4512
361127712022
CP-1Nal-dCM-HArg-DWSTP-HyP-WC
BT800916AcetylationConjugation to MMAE cytotoxin via a valine–citrulline (V-Citr) cleavable linker,Val-Citriline linker and BTC joined by spacer Sar10Bicyclic Mixcyclised on TATA (1,3,5-Triacryloylhexahydro-1,3,5-triazine), 1Nal - 3-(1-naphthyl)-L-alanine, HArg – homo-arginine, HyP – hydroxyproline, MMAE = Monomethyl auristatin E, Cys16 with amidation modification, D-Asp4 modificationBT8009 and MMAE cytotoxin hybridAnticancer24 hours2 µM8.5Rats blood proteaseLC-MS/MSRats blood sampleIn VitroNoneNoneKD(nM) = 6.0±1.2 (Binding affinity for BT8009 binding to extracellular domains of Nectin-4 in Rat)
4513
361127712022
CP-1Nal-dCM-HArg-DWSTP-HyP-WC
BT800916AcetylationConjugation to MMAE cytotoxin via a valine–citrulline (V-Citr) cleavable linker,Val-Citriline linker and BTC joined by spacer Sar10Bicyclic Mixcyclised on TATA (1,3,5-Triacryloylhexahydro-1,3,5-triazine), 1Nal - 3-(1-naphthyl)-L-alanine, HArg – homo-arginine, HyP – hydroxyproline, MMAE = Monomethyl auristatin E, Cys16 with amidation modification, D-Asp4 modificationBT8009 and MMAE cytotoxin hybridAnticancer24 hours2 µM5Mouse blood proteaseLC-MS/MSMouse blood sampleIn VitroNoneNoneKD(nM) = 2.9±1.1 (Binding affinity for BT8009 binding to extracellular domains of Nectin-4 in Mouse)
4514
361014522022
NNFQGLRSFGCRFGTCTVQKLAHQIYQFTDKDKDNVAPRSKISPQGY
IgG1 S-AM (6-52)47IgG1 Fc linked with hAM using linker (GGGGS)3AmidationCyclic (C16-C21 Disulfide Bond In Ham)LNonehAM-IgG Fc fusion proteinAntiiInflammatoryBlood was collected before injection (day 0), and then 1, 2, 4, 6, 8, 10, 12, and 14 days after administration30 nmol/kg2.11Wistar rats plasma proteaseELISA (measure mAM)Wistar rats plasmaIn VivoNoneNoneAfter treatment with IgG4-AM (6-52), SBP (Systolic Blood Pressure) decreased significantly over time, showing reductions of 24.3 ± 4.8 mmHg on day 3, 32.2 ± 6.9 mmHg on day 6, 40.7 ± 3.1 mmHg on day 9, and 56.6 ± 4.5 mmHg on day 12, compared to the control group
4515
361014522022
NNFQGLRSFGCRFGTCTVQKLAHQIYQFTDKDKDNVAPRSKISPQGY
IgG4 S-AM (6-52)47IgG4 Fc linked with hAM using linker (GGGGS)3AmidationLinearLNonehAM-IgG Fc fusion proteinAntiiInflammatoryBlood was collected before injection (day 0), and then 1, 2, 4, 6, 8, 10, 12, and 14 days after administration30 nmol/kg2.37Wistar rats plasma proteaseELISA (measure mAM )Wistar rats plasmaIn VivoNoneNoneAfter treatment with IgG4-AM (6-52), SBP (Systolic Blood Pressure) decreased significantly over time, showing reductions of 24.3 ± 4.8 mmHg on day 3, 32.2 ± 6.9 mmHg on day 6, 40.7 ± 3.1 mmHg on day 9, and 56.6 ± 4.5 mmHg on day 12, compared to the control group
4516
361014522022
NNFQGLRSFGCRFGTCTVQKLAHQIYQFTDKDKDNVAPRSKISPQGY
IgG1 S-AM (6-52)47IgG1 Fc linked with hAM using linker (GGGGS)3AmidationCyclic (C16-C21 Disulfide Bond In Ham)LNonehAM-IgG Fc fusion proteinAntiiInflammatoryBlood was collected before injection (day 0), and then 1, 2, 4, 6, 8, 10, 12, and 14 days after administration30 nmol/kg2.885Wistar rats plasma proteaseELISA (measure tAM )Wistar rats plasmaIn VivoNoneNoneAfter treatment with IgG4-AM (6-52), SBP (Systolic Blood Pressure) decreased significantly over time, showing reductions of 24.3 ± 4.8 mmHg on day 3, 32.2 ± 6.9 mmHg on day 6, 40.7 ± 3.1 mmHg on day 9, and 56.6 ± 4.5 mmHg on day 12, compared to the control group
4517
361014522022
NNFQGLRSFGCRFGTCTVQKLAHQIYQFTDKDKDNVAPRSKISPQGY
IgG4 S-AM (6-52)47IgG4 Fc linked with hAM using linker (GGGGS)3AmidationLinearLNonehAM-IgG Fc fusion proteinAntiiInflammatoryBlood was collected before injection (day 0), and then 1, 2, 4, 6, 8, 10, 12, and 14 days after administration30 nmol/kg3.23Wistar rats plasma proteaseELISA (measure tAM )Wistar rats plasmaIn VivoNoneNoneAfter treatment with IgG4-AM (6-52), SBP (Systolic Blood Pressure) decreased significantly over time, showing reductions of 24.3 ± 4.8 mmHg on day 3, 32.2 ± 6.9 mmHg on day 6, 40.7 ± 3.1 mmHg on day 9, and 56.6 ± 4.5 mmHg on day 12, compared to the control group
4518
361014522022
YRQSMNNFQGLRSFGCRFGTCTVQKLAHQIYQFTDKDKDNVAPRSKISPQGY
AM52FreeAmidationCyclic (C16-C21 Disulfide Bond)LNoneIsolated from Human pheochromocytomaVasodilator and Cardiovascular ProtectionBlood was collected before injection (0 min), and then 15, 30, 60 and 120 min after administration50 nmol/kg32.3Wistar rats plasma proteaseELISA (measure mAM )Wistar rats plasmaIn VivoNoneNoneAfter treatment with IgG4-AM (6-52), SBP (Systolic Blood Pressure) decreased significantly over time, showing reductions of 24.3 ± 4.8 mmHg on day 3, 32.2 ± 6.9 mmHg on day 6, 40.7 ± 3.1 mmHg on day 9, and 56.6 ± 4.5 mmHg on day 12, compared to the control group
4519
361014522022
YRQSMNNFQGLRSFGCRFGTCTVQKLAHQIYQFTDKDKDNVAPRSKISPQGY
AM52FreeAmidationCyclic (C16-C21 Disulfide Bond)LNoneIsolated from Human pheochromocytomaVasodilator and Cardiovascular ProtectionBlood was collected before injection (0 min), and then 15, 30, 60 and 120 min after administration50 nmol/kg27.5Wistar rats plasma proteaseELISA (measure tAM )Wistar rats plasmaIn VivoNoneNoneAfter treatment with IgG4-AM (6-52), SBP (Systolic Blood Pressure) decreased significantly over time, showing reductions of 24.3 ± 4.8 mmHg on day 3, 32.2 ± 6.9 mmHg on day 6, 40.7 ± 3.1 mmHg on day 9, and 56.6 ± 4.5 mmHg on day 12, compared to the control group
4520
360758992022
N.A.
S-20-1N.A.N.A.N.A.CyclicLModified by adding negative chargeSyntheticAntiviral (Against Infection By Sars-Cov-2 )Blood samples were collected at 10 min, 20 min, 30 min, 1 h, 2 h, 4 h, 8 h, 24 h and 48 h50 mg/kg14.53 (Terminal Elimination Half Life)C57Bl/6 mice plasma proteaseLC-MS/MSC57BL/6 mice plasmaIn VivoNoneNoneIC50 (μM) = 0.8 in HUH 7 cells
4521
360758992022
N.A.
S-20-1N.A.N.A.N.A.CyclicLModified by adding negative chargeSyntheticAntiviral (Against Infection By Sars-Cov-2 )Blood samples were collected at 10 min, 20 min, 30 min, 1 h, 2 h, 4 h, 8 h, 24 h and 48 h50 mg/kg24.29 (Terminal Elimination Half Life)C57Bl/6 mice plasma proteaseLC-MS/MSC57BL/6 mice plasmaIn VivoNoneNoneIC50 (μM) = 0.8 in HUH 7 cells
4522
360472552022
H-r-Dmt-KF-PEG-DSPE, c(RGD)-PEG-DSPE
MTP/RGD-CAL/TAN NS4 for MTP, 3 for cRGDFreeMTP/RGD comodified with CAL/TAN NS LinearL(cRGD), Mix(MTP)Dmt: 2',6'-dimethyltyrosineSyntheticTreatment of Acute Myocardial Infarction (Ami) Blood samples were obtained at determined times until 72 h after injection and 15 μL of heparin (1000 U/mL) was added to each sample10 mg/kg8.22AMI rats plasma proteaseN.A.AMI rats plasmaIn VivoNoneNoneBlank MTP/RGD NS and RGD-PEG-DSPE groups showed over 85% of cell viability. In contrast, drugs contained formulations exhibited cytotoxicity to some extent
4523
360472552022
Hr-Dmt-KF
MTP-CAL/TAN NS5FreeMTP/RGD comodified with CAL/TAN NS (PEG-DSPE)LinearMixDmt: 2',6'-dimethyltyrosine at position 3, D-Arg2 modificationSyntheticTreatment of Acute Myocardial Infarction (Ami) Blood samples were obtained at determined times until 72 h after injection and 15 μL of heparin (1000 U/mL) was added to each sample10 mg/kg4.59AMI rats plasma proteaseN.A.AMI rats plasmaIn VivoNoneNoneBlank MTP/RGD NS and RGD-PEG-DSPE groups showed over 85% of cell viability. In contrast, drugs contained formulations exhibited cytotoxicity to some extent.
4524
360348082022
MGHPPLLPLLLLLHTCVPASWGLRCMQCKTNGDCRVEECALGQDLCRTTIVRLWEEGEELELVEKSCTHSEKTNRTLSYRTGLKITSLTEVVCGLDLCNQGNSGRAVTYSRSRYLECISCGSSDMSCERGRHQSLQCRSPEEQCLDVVTHWIQEGEEGRPKDDRHLRGCGYLPGCPGSNGFHNNDTFHFLKCCNTTKCNEGPILELENLPQNGRQCYSCKGNSTHGCSSEETFLIDCRGPMNQCLVATGTHEPKNQSYMVRGCATASMCQHAHLGDAFSMNHIDVSCCTKSGCNHPDLDVQYRSGAAPQPGPAHLSLTITLLMTARLWGGTLLWT
uPAR335FreeFreeLinearLNoneDerived from PLAUR genePlays role in thrombosisN.A.N.A.209.6 ± 0.2 BEAS-2B cells lysate proteaseDensitometry analysis using NIH Image JBEAS-2B cells lysate with UK treatment +H/R (Hypoxia/Reoxygenation) + CycloheximideIn VivoNoneNoneN.A.
4525
360348082022
MGHPPLLPLLLLLHTCVPASWGLRCMQCKTNGDCRVEECALGQDLCRTTIVRLWEEGEELELVEKSCTHSEKTNRTLSYRTGLKITSLTEVVCGLDLCNQGNSGRAVTYSRSRYLECISCGSSDMSCERGRHQSLQCRSPEEQCLDVVTHWIQEGEEGRPKDDRHLRGCGYLPGCPGSNGFHNNDTFHFLKCCNTTKCNEGPILELENLPQNGRQCYSCKGNSTHGCSSEETFLIDCRGPMNQCLVATGTHEPKNQSYMVRGCATASMCQHAHLGDAFSMNHIDVSCCTKSGCNHPDLDVQYRSGAAPQPGPAHLSLTITLLMTARLWGGTLLWT
uPAR335FreeFreeLinearLNoneDerived from PLAUR genePlays role in thrombosisN.A.N.A.48.2 ± 2.3 BEAS-2B cells lysate proteaseDensitometry analysis using NIH Image JBEAS-2B cells lysate with UK treatment +H/R (Hypoxia/Reoxygenation) + CycloheximideIn VivoNoneNoneN.A.
4526
359996122022
RGD
cRGD-Exo/TP3DSPE-PEGFreeCyclic (RGD)LDiR labeledSyntheticTargeted delivery of triptolide against malignant melanomaScanned at interval times (1, 2, 4, 6, 12, and 24 h)N.A.27.14 ± 2.55Mice plasma proteaseIVIS at 750/780 nmBALB/c nude mice plasmaIn VivoNoneNoneTumor inhibition rate of 65.73 ± 3.29% in the cRGD-Exo/TP 
4527
359900072022
desH-AEGTFTSDVSSYLEEQAAREFIAWLVRGRKX
Peptides 131desH indicates the non-natural amino acid deamino-histidineFreeLinearLX = R1, R2 = H (R2 group present in R1)GLP-1R agonistAntidiabetes, Antiobesity200 µL blood samples were taken at 2, 6, 10, 24, 30 and 48 h20 nmol/kg10.9Rats plasma proteaseUPLC-MSRats plasmaIn VivoNoneNoneN.A.
4528
359900072022
desH-AEGTFTSDVSSYLEEQAAREFIAWLVRGRKX
Peptides 131desH indicates the non-natural amino acid deamino-histidineFreeLinearLX = R1, R2 = H (R2 group present in R1)GLP-1R agonistAntidiabetes, Antiobesity200 µL blood samples were taken at 2, 6, 10, 24, 30 and 48 h18059 pmol/kg12.2Rats plasma proteaseUPLC-MSRats plasmaIn VivoNoneNoneN.A.
4529
359900072022
desH-AEGTFTSDVSSYLEEQAAREFIAWLVRGRKX
Peptides 131desH indicates the non-natural amino acid deamino-histidineFreeLinearLX = R1, R2 = H (R2 group present in R1)GLP-1R agonistAntidiabetes, Antiobesity200 µL blood samples were taken at 2, 6, 10, 24, 30 and 48 h18058 pmol/kg10.7Rats plasma proteaseUPLC-MSRats plasmaIn VivoNoneNoneN.A.
4530
359900072022
desH-AEGTFTSDVSSYLEEQAAREFIAWLVRGRKX
Peptides 131desH indicates the non-natural amino acid deamino-histidineFreeLinearLX = R1, R2 = H (R2 group present in R1)GLP-1R agonistAntidiabetes, Antiobesity200 µL blood samples were taken at 2, 6, 10, 24, 30 and 48 h17872 pmol/kg18.6Rats plasma proteaseUPLC-MSRats plasmaIn VivoNoneNoneN.A.
4531
359900072022
desH-AEGTFTSDVSSYLEEQAAREFIAWLVRGRKX
Peptides 131desH indicates the non-natural amino acid deamino-histidineFreeLinearLX = R1, R2 = H (R2 group present in R1)GLP-1R agonistAntidiabetes, Antiobesity200 µL blood samples were taken at 2, 6, 10, 24, 30 and 48 h18052 pmol/kg12.9Rats plasma proteaseUPLC-MSRats plasmaIn VivoNoneNoneN.A.
4532
359900072022
AEGTFTSDVSSYLEEQAAREFIAWLVRGRK-R1-GGSK-R3
Peptides 235desH indicates the non-natural amino acid deamino-histidine at position 1FreeLinearLX = R1, R2 = H (R2 group present in R1), Y = R3, R4 = Zr (R4 group present within R3)GLP-1R agonistAntidiabetes, Antiobesity200 µL blood samples were taken at 2, 6, 10, 24, 30 and 48 h17838 pmol/kg8.5Rats plasma proteaseUPLC-MSRats plasmaIn VivoNoneNoneN.A.
4533
359900072022
AEGTFTSDVSSYLEEQAAREFIAWLVRGRK-R1-GGSK-R3
Peptides 235desH indicates the non-natural amino acid deamino-histidine at position 1FreeLinearLX = R1, R2 = H (R2 group present in R1), Y = R3, R4 = Zr (R4 group present within R3)GLP-1R agonistAntidiabetes, Antiobesity200 µL blood samples were taken at 2, 6, 10, 24, 30 and 48 h17881 pmol/kg8Rats plasma proteaseUPLC-MSRats plasmaIn VivoNoneNoneN.A.
4534
359900072022
AEGTFTSDVSSYLEEQAAREFIAWLVRGRK-R1-GGSK-R3
Peptides 235desH indicates the non-natural amino acid deamino-histidine at position 1FreeLinearLX = R1, R2 = H (R2 group present in R1), Y = R3, R4 = Zr (R4 group present within R3)GLP-1R agonistAntidiabetes, Antiobesity200 µL blood samples were taken at 2, 6, 10, 24, 30 and 48 h17833 pmol/kg8.6Rats plasma proteaseUPLC-MSRats plasmaIn VivoNoneNoneN.A.
4535
359900072022
AEGTFTSDVSSYLEEQAAREFIAWLVRGRK-R1-GGSK-R3
Peptides 235desH indicates the non-natural amino acid deamino-histidine at position 1FreeLinearLX = R1, R2 = H (R2 group present in R1), Y = R3, R4 = Zr (R4 group present within R3)GLP-1R agonistAntidiabetes, Antiobesity200 µL blood samples were taken at 2, 6, 10, 24, 30 and 48 h17941 pmol/kg7.7Rats plasma proteaseUPLC-MSRats plasmaIn VivoNoneNoneN.A.
4536
359900072022
AEGTFTSDVSSYLEEQAAREFIAWLVRGRK-R1-GGSK-R3
Peptides 235desH indicates the non-natural amino acid deamino-histidine at position 1FreeLinearLX = R1, R2 = H (R2 group present in R1), Y = R3, R4 = Zr (R4 group present within R3)GLP-1R agonistAntidiabetes, Antiobesity200 µL blood samples were taken at 2, 6, 10, 24, 30 and 48 h18000 pmol/kg7.9Rats plasma proteaseUPLC-MSRats plasmaIn VivoNoneNoneN.A.
4537
359900072022
AEGTFTSDVSSYLEEQAAREFIAWLVRGRK-R1-GGSK-R3
Peptides 235desH indicates the non-natural amino acid deamino-histidine at position 1FreeLinearLX = R1, R2 = H (R2 group present in R1), Y = R3, R4 = Zr (R4 group present within R3)GLP-1R agonistAntidiabetes, Antiobesity200 µL blood samples were taken at 2, 6, 10, 24, 30 and 48 h17890 pmol/kg8.7Rats plasma proteaseUPLC-MSRats plasmaIn VivoNoneNoneN.A.
4538
359900072022
AEGTFTSDVSSYLEEQAAREFIAWLVRGRK-R1-GGSK-R3
Peptides 235desH indicates the non-natural amino acid deamino-histidine at position 1FreeLinearLX = R1, R2 = H (R2 group present in R1), Y = R3, R4 = Zr (R4 group present within R3)GLP-1R agonistAntidiabetes, Antiobesity200 µL blood samples were taken at 2, 6, 10, 24, 30 and 48 h18117 pmol/kg8.6Rats plasma proteaseUPLC-MSRats plasmaIn VivoNoneNoneN.A.
4539
359711652022
YLCSSNNNRERDKFRRGGSGGTSFEQFWAWLWP
Au‐AR pep‐PROTAC33FreeFreeLinearLNoneSyntheticAnticancer (Prostate Cancer Therapy)N.A.N.A.26.3Mouse serum proteaseICP‐MSmouse serumIn VivoNoneNoneN.A.
4540
359711652022
YLCSSNNNRERDKFRRGGSGGTSFEQFWAWLWP
Au‐AR pep‐PROTAC33FreeFreeLinearLNoneSyntheticAnticancer (Prostate Cancer Therapy)N.A.N.A.25.1PBS containing 10% serum proteaseHPLCPBS containing 10% serum In VitroNoneNoneIC50 of Au‐AR pep‐PROTAC on AML 12 cells is 2.41 µM 
4541
359711652022
YLCSSNNNRERDKFRRGGSGGTSFEQFWAWLWP
AR pep‐PROTAC33FreeFreeLinearLNoneSyntheticAnticancer (Prostate Cancer Therapy)N.A.N.A.1.9PBS containing 10% serum proteaseHPLCPBS containing 10% serum In VitroNoneNoneIC50 of Au‐AR pep‐PROTAC on AML 12 cells is 2.41 µM 
4542
358922562022
GIVEQCCTSICSLYQLENYCN/FVNQHLCGSHLVEALYLVCGERGFFYTPKT
RA1512734351FreeFreeLinearLAlbumin binding fatty-acid side chain is coupled to lysine (B29)Insulin analogueAntidiabetesBlood samples were collected before RA15127343 administration (baseline) and 1–4 times per day until study end.10 nmol/kg47Göttingen minipigs plasma proteaseLC-MS/MSGöttingen minipigs plasmaIn Vivohttps://sci-hub.st/10.1016/j.jpba.2018.07.009None(Activity values of RA15127343) IC50 for IR-A: 19.9 μM, IC50 for IR-B: 6.31 μM, EC50 for IR-A: 2.054 μM, EC50 for IR-B: 669.6 nM
4543
358922562022
GIVEQCCTSICSLYQLENYCN/FVNQHLCGSHLVEALYLVCGERGFFYTPKT
RA1512734351FreeFreeLinearLAlbumin binding fatty-acid side chain is coupled to lysine (B29)Insulin analogueAntidiabetesBlood samples were collected before RA15127343 administration (baseline) and 1–4 times per day until study end.10,30,45,60 nmol/kg48 - 59Göttingen minipigs plasma proteaseLC-MS/MSGöttingen minipigs plasmaIn Vivohttps://sci-hub.st/10.1016/j.jpba.2018.07.009None(Activity values of RA15127343) IC50 for IR-A: 19.9 μM, IC50 for IR-B: 6.31 μM, EC50 for IR-A: 2.054 μM, EC50 for IR-B: 669.6 nM
4544
358922562022
GIVEQCCTSICSLYQLENYCN/FVNQHLCGSHLVEALYLVCGERGFFYTPKT
RA1512734351FreeFreeLinearLAlbumin binding fatty-acid side chain is coupled to lysine (B29)Insulin analogueAntidiabetesN.A.200 nmol/kg11Rats plasma proteaseLC-MS/MSRats plasmaIn Vivohttps://sci-hub.st/10.1016/j.jpba.2018.07.009None(Activity values of RA15127343) IC50 for IR-A: 19.9 μM, IC50 for IR-B: 6.31 μM, EC50 for IR-A: 2.054 μM, EC50 for IR-B: 669.6 nM
4545
358922562022
GIVEQCCTSICSLYQLENYCN/FVNQHLCGSHLVEALYLVCGERGFFYTPKT
RA1512734351FreeFreeLinearLAlbumin binding fatty-acid side chain is coupled to lysine (B29)Insulin analogueAntidiabetesN.A.200, 400 nmol/kg21 - 22Rats plasma proteaseLC-MS/MSRats plasmaIn Vivohttps://sci-hub.st/10.1016/j.jpba.2018.07.009None(Activity values of RA15127343) IC50 for IR-A: 19.9 μM, IC50 for IR-B: 6.31 μM, EC50 for IR-A: 2.054 μM, EC50 for IR-B: 669.6 nM
4546
358902242022
K-(PEG)4-E
177Lu-Palm-3PRGD22Lys1 linked with (palmitoyl-Glu-OH)Glu3 linked with (PEG4-c(RGDfK))2Cyclic (3PRGD2)Mix177Lu radiolabeling at PEG4, Lys1 and Glu2 linked with PEG4 in betweenSyntheticAntitumorN.A.0.74 MBq4.49 (T1/2a)KM mice blood proteaseGamma counterKM mice blood sampleIn VivoNoneNoneN.A.
4547
358902242022
E
177Lu-3PRGD21PEG4Glu linked with [PEG4-c(RGDfK)]2Cyclic (3PRGD2)Mix177Lu radiolabeling at PEG4SyntheticAntitumorN.A.0.74 MBq1.94 (T1/2a)KM mice blood proteaseGamma counterKM mice blood sampleIn VivoNoneNoneN.A.
4548
358902242022
K-(PEG)4-E
177Lu-Palm-3PRGD22Lys1 linked with (palmitoyl-Glu-OH)Glu3 linked with (PEG4-c(RGDfK))2Cyclic (3PRGD2)Mix177Lu radiolabeling at PEG4, Lys1 and Glu2 linked with PEG4 in betweenSyntheticAntitumorN.A.0.74 MBq73.42 (T1/2Β) KM mice blood proteaseGamma counterKM mice blood sampleIn VivoNoneNoneN.A.
4549
358902242022
E
177Lu-3PRGD21PEG4Glu linked with [PEG4-c(RGDfK)]2Cyclic (3PRGD2)Mix177Lu radiolabeling at PEG4SyntheticAntitumorN.A.0.74 MBq11.81 (T1/2Β) KM mice blood proteaseGamma counterKM mice blood sampleIn VivoNoneNoneN.A.
4550
358902242022
K-(PEG)4-E
177Lu-Palm-3PRGD22Lys1 linked with (palmitoyl-Glu-OH)Glu3 linked with (PEG4-c(RGDfK))2Cyclic (3PRGD2)Mix177Lu radiolabeling at PEG4, Lys1 and Glu2 linked with PEG4 in betweenSyntheticAntitumorN.A.0.74 MBq63.71 (Slow)C57Bl/6 mice blood proteaseGamma counterC57BL/6 mice blood sampleIn VivoNoneNoneN.A.
4551
358902242022
E
177Lu-3PRGD21PEG4Glu linked with [PEG4-c(RGDfK)]2Cyclic (3PRGD2)Mix177Lu radiolabeling at PEG4SyntheticAntitumorN.A.0.74 MBq14.54 (Slow)C57Bl/6 mice blood proteaseGamma counterC57BL/6 mice blood sampleIn VivoNoneNoneN.A.
4552
358902242022
K-(PEG)4-E
177Lu-Palm-3PRGD22Lys1 linked with (palmitoyl-Glu-OH)Glu3 linked with (PEG4-c(RGDfK))2Cyclic (3PRGD2)Mix177Lu radiolabeling at PEG4, Lys1 and Glu2 linked with PEG4 in betweensyntheticAntitumorN.A.0.74 MBq2.08 (Fast)C57Bl/6 mice blood proteaseGamma counterC57BL/6 mice blood sampleIn VivoNoneNoneN.A.
4553
358902242022
E
177Lu-3PRGD21PEG4Glu linked with [PEG4-c(RGDfK)]2Cyclic (3PRGD2)Mix177Lu radiolabeling at PEG4syntheticAntitumorN.A.0.74 MBq1.06 (Fast)C57Bl/6 mice blood proteaseGamma counterC57BL/6 mice blood sampleIn VivoNoneNoneN.A.
4554
358584232022
LQEHPQARKYKGAQKKGLSKGCFGLKLDRIGSMSGLGC
4A383A coupled to bicyclononyne-modified MSs (MS-N-hydroxysuccinymidocarbonates)FreeLinearLGln 6,14 modification, Mod = (CH3)2CHSO2-, N3-linker N-hydroxysuccinymidocarbonates containing isopropyl sulfone (1A) and N,N-dimethyl-sulfonamide (1B) modulatorsMS-[Gln6,14]CNP-38 conjugateTreatment of AchondroplasiaBlood samples (~100 μL) were drawn from the tail vein at 8, 24, 48, 72, 120, 168, 240, 336, 432, 504, 600 and 672 h on a staggered schedule from 12 mice to give 4 replicates at each time-point20 nmol40 (T1/2,a -Elimination Half Life)CD1 mice plasma proteaseELISA, LC-MS/MSCD1 mice plasmaIn VivoNoneNoneQWk 50 nmol of 4A caused significantly increased growth, with mice becoming about 25% longer than the vehicle control over the study period
4555
358584232022
LQEHPQARKYKGAQKKGLSKGCFGLKLDRIGSMSGLGC
4B383B coupled to bicyclononyne-modified MSs (MS-N-hydroxysuccinymidocarbonates)FreeLinearLGln 6,14 modification, Mod = (CH3)2CHSO2-, N3-linker N-hydroxysuccinymidocarbonates containing N,N-dimethyl-sulfonamide (1B) modulatorsMS-[Gln6,14]CNP-38 conjugateTreatment of AchondroplasiaBlood samples (~100 μL) were drawn from the tail vein at 8, 24, 24, 96, 168, 240, 336, 408, 504, 576, 672, 840, 1008, 1176, 1344, and 1512 h from 8 mice on a staggered schedule to give 4 replicates at each time-point700 nmol60 ( T1/2,a - Elimination Half Life)CD1 mice plasma proteaseELISA, LC-MS/MSCD1 mice plasmaIn VivoNoneNoneSingle dose of 85 nmol of 4B showed similar growth stimulation as QD administration of [Gln6,14]CNP-38 for 3 weeks, but growth plateaued afterward
4556
358584232022
LQEHPQARKYKGAQKKGLSKGCFGLKLDRIGSMSGLGC
4A383A coupled to bicyclononyne-modified MSs (MS-N-hydroxysuccinymidocarbonates)FreeLinearLGln 6,14 modification, Mod = (CH3)2CHSO2-MS-[Gln6,14]CNP-38 conjugateTreatment of AchondroplasiaBlood samples (~100 μL) were drawn from the tail vein at 8, 24, 48, 72, 120, 168, 240, 336, 432, 504, 600 and 672 h on a staggered schedule from 12 mice to give 4 replicates at each time-point20 nmol212 (T1/2,b-Elimination Half Life)CD1 mice plasma proteaseELISA, LC-MS/MSCD1 mice plasmaIn VivoNoneNoneQWk 50 nmol of 4A caused significantly increased growth, with mice becoming about 25% longer than the vehicle control over the study period
4557
358584232022
LQEHPQARKYKGAQKKGLSKGCFGLKLDRIGSMSGLGC
4B383B coupled to bicyclononyne-modified MSs (MS-N-hydroxysuccinymidocarbonates)FreeLinearLGln 6,14 modification, Mod = (CH3)2NSO2-MS-[Gln6,14]CNP-38 conjugateTreatment of AchondroplasiaBlood samples (~100 μL) were drawn from the tail vein at 8, 24, 24, 96, 168, 240, 336, 408, 504, 576, 672, 840, 1008, 1176, 1344, and 1512 h from 8 mice on a staggered schedule to give 4 replicates at each time-point700 nmol610 ( T1/2,b-Elimination Half Life)CD1 mice plasma proteaseELISA, LC-MS/MSCD1 mice plasmaIn VivoNoneNoneSingle dose of 85 nmol of 4B showed similar growth stimulation as QD administration of [Gln6,14]CNP-38 for 3 weeks, but growth plateaued afterward
4558
358505712022
WYVYPSM
dTBP2 7FreeFreeLinearLNonedTCTP-binding peptide-2AntiinflammatoryBlood samples were collected from the orbital sinus at 0.083, 0.25, 0.5, 1, 2, 4, and 8 h after dosing with dTBP2 or PEG-dTBP210 mg/kg1.01 ± 0.25ICR male mice orbital sinus plasma proteaseLC-MS/MSICR Male mice orbital sinus plasma In VivoNoneNonedTBP2 results in 30% inhibition of inflammatory cell infiltration in BALF compared to the OVA-challenged group
4559
358505712022
WYVYPSM
PEG-dTBP27PEGylation (mPEG)FreeLinearLNonedTCTP-binding peptide-2AntiinflammatoryBlood samples were collected from the orbital sinus at 0.083, 0.25, 0.5, 1, 2, 4, and 8 h after dosing with dTBP2 or PEG-dTBP210 mg/kg2.57 ± 1.11ICR male mice orbital sinus plasma proteaseLC-MS/MSICR Male mice orbital sinus plasma In VivoNoneNonePEG-dTBP2 results in 45% inhibition, indicating that PEGylation enhances the anti-inflammatory effects of dTBP2
4560
358492142022
DAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLVAASQAALGL
HSA585FreeFreeCyclic (17 Disulfide Bond)LNoneHuman derivedCarrier Protein30 minutes3 mL/kg of 20% albumin 8Human intravascular sample proteaseN.A.Human intravascular sampleIn VivoNoneNoneN.A.
4561
358492142022
DAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLVAASQAALGL
HSA585FreeFreeCyclic (17 Disulfide Bond)LNoneHuman derivedCarrier Protein120 minutes3 mL/kg of 20% albumin 6.3Human intravascular sample proteaseN.A.Human intravascular sampleIn VivoNoneNoneN.A.
4562
358403382022
FVNQHLCGSHLVEALELVCGERGFHYGGGGGGSGGGGGIVEQCCTSTCSLDQLENYCGGGGGQGGGGQGGGGQGGGGGECPPCPAPPVAGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTFRVVSVLTVVHQDWLNGKEYKCKVSNKGLPAPIEKTISKTKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPMLDSDGSFFLYSVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPG
BIF296Single-chain variant of insulin has modifications:TyrB16Glu,PheB25His,ThrB27Gly,ProB28Gly,LysB29Gly,ThrB30Gly,IleA10Thr,TyrA14Asp,AsnA21Gly, single-chain variant of insulin with B-chain linked to A-chain by a short linker (Linker 1)Interdomain linker (Linker 2) connecting the A-chain of insulin to the Fc and the Fc domain from IgG2LinearLNoneFc-fusion proteinAntidiabetesBlood samples for glucose measurements were collected by tail bleed conducted under brief restraint. Blood glucose was measured preinjection, 1, 2, 4, 6, 8, 10, 12, 24, 48, 72, 96, 120,144, 168, 240, and 336 hours postdose3 nmol/kg128 ± 10Streptozotocin STZ-treated diabetic SD rats blood proteaseInsulin receptor ELISAStreptozotocin STZ-treated diabetic SD rats blood sampleIn VivoNoneNoneReceptor Phosphorylation EC50, nM = 4241 (Functional activity of BIF as determined by phosphorylation of hIR-A expressed in 293 cells)
4563
358403382022
FVNQHLCGSHLVEALELVCGERGFHYGGGGGGSGGGGGIVEQCCTSTCSLDQLENYCGGGGGQGGGGQGGGGQGGGGGECPPCPAPPVAGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTFRVVSVLTVVHQDWLNGKEYKCKVSNKGLPAPIEKTISKTKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPMLDSDGSFFLYSVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPG
BIF296Single-chain variant of insulin has modifications:TyrB16Glu,PheB25His,ThrB27Gly,ProB28Gly,LysB29Gly,ThrB30Gly,IleA10Thr,TyrA14Asp,AsnA21Gly, single-chain variant of insulin with B-chain linked to A-chain by a short linker (Linker 1)Interdomain linker (Linker 2) connecting the A-chain of insulin to the Fc and the Fc domain from IgG2LinearLNoneFc-fusion proteinAntidiabetesBlood samples for glucose measurements were collected by tail bleed conducted under brief restraint. Blood glucose was measured preinjection, 1, 2, 4, 6, 8, 10, 12, 24, 48, 72, 96, 120,144, 168, 240, and 336 hours postdose10 nmol/kg104 ± 4 Streptozotocin STZ-treated diabetic SD rats blood proteaseInsulin receptor ELISAStreptozotocin STZ-treated diabetic SD rats blood sampleIn VivoNoneNoneReceptor Phosphorylation EC50, nM = 391 (Functional activity of BIF as determined by phosphorylation of hIR-B expressed in 293 cells)
4564
358403382022
FVNQHLCGSHLVEALELVCGERGFHYGGGGGGSGGGGGIVEQCCTSTCSLDQLENYCGGGGGQGGGGQGGGGQGGGGGECPPCPAPPVAGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTFRVVSVLTVVHQDWLNGKEYKCKVSNKGLPAPIEKTISKTKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPMLDSDGSFFLYSVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPG
BIF296single-chain variant of insulin has modifications:TyrB16Glu,PheB25His,ThrB27Gly,ProB28Gly,LysB29Gly,ThrB30Gly,IleA10Thr,TyrA14Asp,AsnA21Gly, single-chain variant of insulin with B-chain linked to A-chain by a short linker (Linker 1)interdomain linker (Linker 2) connecting the A-chain of insulin to the Fc and the Fc domain from IgG2LinearLNoneFc-fusion proteinAntidiabetesBlood samples for glucose measurements were collected by tail bleed conducted under brief restraint. Blood glucose was measured preinjection, 1, 2, 4, 6, 8, 10, 12, 24, 48, 72, 96, 120,144, 168, 240, and 336 hours postdose30 nmol/kg120 ± 21Streptozotocin STZ-treated diabetic SD rats blood proteaseInsulin receptor ELISAStreptozotocin STZ-treated diabetic SD rats blood sampleIn VivoNoneNoneReceptor Phosphorylation EC50, nM > 10,000 (Functional activity of BIF as determined by phosphorylation of hIGF-1R expressed in 293 cells)
4565
358403382022
FVNQHLCGSHLVEALELVCGERGFHYGGGGGGSGGGGGIVEQCCTSTCSLDQLENYCGGGGGQGGGGQGGGGQGGGGGECPPCPAPPVAGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTFRVVSVLTVVHQDWLNGKEYKCKVSNKGLPAPIEKTISKTKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPMLDSDGSFFLYSVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPG
BIF296single-chain variant of insulin has modifications:TyrB16Glu,PheB25His,ThrB27Gly,ProB28Gly,LysB29Gly,ThrB30Gly,IleA10Thr,TyrA14Asp,AsnA21Gly, single-chain variant of insulin with B-chain linked to A-chain by a short linker (Linker 1)interdomain linker (Linker 2) connecting the A-chain of insulin to the Fc and the Fc domain from IgG2LinearLNoneFc-fusion proteinAntidiabetesBlood samples for glucose measurements were collected by tail bleed conducted under brief restraint. Blood glucose was measured preinjection, 1, 2, 4, 6, 8, 10, 12, 24, 48, 72, 96, 120,144, 168, 240, and 336 hours postdose30 nmol/kg120 ± 21Streptozotocin STZ-treated diabetic SD rats blood proteaseInsulin receptor ELISAStreptozotocin STZ-treated diabetic SD rats blood sampleIn VivoNoneNoneLipogenesis in 3T3-L1 Adipocytes, EC50 nM = 19 (Functional activity of BIF as assessed by lipogenesis and cellular proliferation)
4566
358403382022
FVNQHLCGSHLVEALELVCGERGFHYGGGGGGSGGGGGIVEQCCTSTCSLDQLENYCGGGGGQGGGGQGGGGQGGGGGECPPCPAPPVAGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTFRVVSVLTVVHQDWLNGKEYKCKVSNKGLPAPIEKTISKTKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPMLDSDGSFFLYSVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPG
BIF296single-chain variant of insulin has modifications:TyrB16Glu,PheB25His,ThrB27Gly,ProB28Gly,LysB29Gly,ThrB30Gly,IleA10Thr,TyrA14Asp,AsnA21Gly, single-chain variant of insulin with B-chain linked to A-chain by a short linker (Linker 1)interdomain linker (Linker 2) connecting the A-chain of insulin to the Fc and the Fc domain from IgG2LinearLNoneFc-fusion proteinAntidiabetesBlood samples for glucose measurements were collected by tail bleed conducted under brief restraint. Blood glucose was measured preinjection, 1, 2, 4, 6, 8, 10, 12, 24, 48, 72, 96, 120,144, 168, 240, and 336 hours postdose30 nmol/kg120 ± 21Streptozotocin STZ-treated diabetic SD rats blood proteaseInsulin receptor ELISAStreptozotocin STZ-treated diabetic SD rats blood sampleIn VivoNoneNoneProliferation in Saos-2 Cells,EC50 nM = 134 (Functional activity of BIF as assessed by cellular proliferation)
4567
358403382022
FVNQHLCGSHLVEALELVCGERGFHYGGGGGGSGGGGGIVEQCCTSTCSLDQLENYCGGGGGQGGGGQGGGGQGGGGGECPPCPAPPVAGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTFRVVSVLTVVHQDWLNGKEYKCKVSNKGLPAPIEKTISKTKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPMLDSDGSFFLYSVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPG
BIF296single-chain variant of insulin has modifications:TyrB16Glu,PheB25His,ThrB27Gly,ProB28Gly,LysB29Gly,ThrB30Gly,IleA10Thr,TyrA14Asp,AsnA21Gly, single-chain variant of insulin with B-chain linked to A-chain by a short linker (Linker 1)interdomain linker (Linker 2) connecting the A-chain of insulin to the Fc and the Fc domain from IgG2LinearLNoneFc-fusion proteinAntidiabetesBlood samples for glucose measurements were collected by tail bleed conducted under brief restraint. Blood glucose was measured preinjection, 1, 2, 4, 6, 8, 10, 12, 24, 48, 72, 96, 120,144, 168, 240, and 336 hours postdose30 nmol/kg120 ± 21Streptozotocin STZ-treated diabetic SD rats blood proteaseInsulin receptor ELISAStreptozotocin STZ-treated diabetic SD rats blood sampleIn VivoNoneNoneProliferation in H4IIE Cells,EC50 nM = 20 (Functional activity of BIF as assessed by cellular proliferation)
4568
358075002022
AEWCP
TIPP5FreeFreeLinearLNoneFrom calf thymus extractsTreatment of AsthmaAt 0.5, 1, 2, 5, 10, 15, 20, and 40 min post administration (eight mice at each time points), blood samples were taken from an inner canthus 50 mg/kg5.99 ± 1.82Mice plasma proteaseLC-MS/MSMice plasmaIn VivoNoneNoneTIPP inhibits degranulation and inflammation in RBL-2H3 cells and pretreatment with 200 microgram/mL of TIPP for 20 minutes reduces the level of biomarkers of allergic response and inflammation i.e β-hexosaminidase, Histamine, IL-4
4569
357791892022
WSGWSSCSRSCG
NX21012FreeFreeLinearLNoneDerived from the subcommissural organ (SCO)-spondinTreatment of Neurodegenerative Diseases Blood PK samples (4 mL) for the analysis of NX210 via its metabolite NX210c were collected prior to dosing, immediately after bolus injection or termination of the infusion and at 5, 10, 15, 20, 25, 30, 70, 120, and 180 min after bolus injection or termination of infusion2.5 mg/kg13.3Human plasma proteaseHPLC–MS/MSHuman plasma In Vivohttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3965545/NoneN.A.
4570
357791892022
WSGWSSCSRSCG
NX21012FreeFreeLinearLNoneDerived from the subcommissural organ (SCO)-spondinTreatment of Neurodegenerative Diseases Blood PK samples (4 mL) for the analysis of NX210 via its metabolite NX210c were collected prior to dosing, immediately after bolus injection or termination of the infusion and at 5, 10, 15, 20, 25, 30, 70, 120, and 180 min after bolus injection or termination of infusion5 mg/kg6.19Human plasma proteaseHPLC–MS/MSHuman plasma In VivoNoneNoneN.A.
4571
357791892022
WSGWSSCSRSCG
NX21012FreeFreeLinearLNoneDerived from the subcommissural organ (SCO)-spondinTreatment of Neurodegenerative Diseases Blood PK samples (4 mL) for the analysis of NX210 via its metabolite NX210c were collected prior to dosing, immediately after bolus injection or termination of the infusion and at 5, 10, 15, 20, 25, 30, 70, 120, and 180 min after bolus injection or termination of infusion10 mg/kg20Human plasma proteaseHPLC–MS/MSHuman plasma In VivoNoneNoneN.A.
4572
357727832022
DHNNPQaR
DR7dA8FreeAmidationLinearMixReplacing the isoleucine (Ile7) residue with D-alanine7 (D-Ala)DR8 analogAmeliorated Tumor Growth Factor (Tgf)-B1-Induced Fibrogenesis And Bleomycin-Induced PfAn aliquot of 40 ml was taken at 0, 15, 30, 60, 120 and 240 min10 mM201.08 ± 58.86Mouse serum proteaseRP-HPLCMouse serumIn VitroNoneNoneDR7dA showed no cytotoxic effects in A549 and NIH3T3 cells even at high concentrations (up to 160 μM)
4573
357727832022
DHNNPQIR
DR88FreeAmidationLinearLNoneDerived from rapeseed proteinAmeliorated Tumor Growth Factor (Tgf)-B1-Induced Fibrogenesis And Bleomycin-Induced PfAn aliquot of 40 ml was taken at 0, 15, 30, 60, 120 and 240 min10 mM70.19 ± 6.83Mouse serum proteaseRP-HPLCMouse serumIn VitroNoneNoneThe effective concentration of DR8 was higher than that of DR7dA in both cell lines, indicating that DR7dA is more potent in inhibiting fibrosis
4574
357101412022
EGTFISDYSIAMDKIKQQDFVNWLLAQKGKKNDWKHN
mGIPAnt‐137FreeFreeLinearLC16-diacid acylation at Lysine16GIP analogueAntiobesityRetro‐orbital blood samples (50 μl) were taken using EDTA coated glass capillaries at (1) t = 0, 0.5, 1, 1.5, 2 and 2.5 h, (2) t = 2.5, 3, 4, 6, 8 and 22 h, or (3) t = 22, 24, 26, 28, 30 and 32 h and immediately300 nmol/kg7.2Mouse Retro-Orbital Blood Plasma ProteaseRIAMouse retro-orbital blood plasmaIn VivoNoneNonemGIPAnt‐1 inhibited the mouse GIP receptor with IC50 of 269 nM
4575
357034632022
TVRTSAD
MT2187FreeZD2 conjugated to a clinical contrast agent gadoteridol Gd(HP-DO3A) using N3 linkerLinearLNoneZD2 analogCancer targeting contrast agentBlood samples were collected from jugular veins at predose and at 2, 5, 10, 15, 30, and 45 minutes and 1, 2, 3, and 4 hours after dosing from group 1 to 30.04 mmol/kg0.3 (Elimination Half Life)Male SD rats plasma proteaseICP-MSMale SD rats plasmaIn VivoNoneNoneMT218 did not inhibit the enzyme activities of CYP1A2, CYP2B6, CYP2C9, CYP2C19, CYP2D6, or CYP3A4 at concentrations up to 100 μM
4576
357034632022
TVRTSAD
MT2187FreeZD2 conjugated to a clinical contrast agent gadoteridol Gd(HP-DO3A) using N3 linkerLinearLNoneZD2 analogCancer targeting contrast agentBlood samples were collected from jugular veins at predose and at 2, 5, 10, 15, 30, and 45 minutes and 1, 2, 3, and 4 hours after dosing from group 1 to 30.04 mmol/kg0.28 (Elimination Half Life)Female SD rats plasma proteaseICP-MSFemale SD rats plasmaIn VivoNoneNoneMT218 did not inhibit the enzyme activities of CYP1A2, CYP2B6, CYP2C9, CYP2C19, CYP2D6, or CYP3A4 at concentrations up to 100 μM
4577
357034632022
TVRTSAD
MT2187FreeZD2 conjugated to a clinical contrast agent gadoteridol Gd(HP-DO3A) using N3 linkerLinearLNoneZD2 analogCancer targeting contrast agentBlood samples were collected from jugular veins at predose and at 2, 5, 10, 15, 30, and 45 minutes and 1, 2, 3, and 4 hours after dosing from group 1 to 30.04 mmol/kg0.57(Elimination Half Life)(P) SD rats plasma proteaseICP-MS(P) SD rats plasmaIn VivoNoneNoneMT218 did not inhibit the enzyme activities of CYP1A2, CYP2B6, CYP2C9, CYP2C19, CYP2D6, or CYP3A4 at concentrations up to 100 μM
4578
357034632022
TVRTSAD
MT2187FreeZD2 conjugated to a clinical contrast agent gadoteridol Gd(HP-DO3A) using N3 linkerLinearLNoneZD2 analogCancer targeting contrast agentBlood samples were collected from jugular veins at predose and at 2, 5, 10, 15, 30, and 45 minutes and 1, 2, 3, and 4 hours after dosing from group 1 to 30.1 mmol/kg0.31 (Elimination Half Life)Male SD rats plasma proteaseICP-MSMale SD rats plasmaIn VivoNoneNoneMT218 did not inhibit the enzyme activities of CYP1A2, CYP2B6, CYP2C9, CYP2C19, CYP2D6, or CYP3A4 at concentrations up to 100 μM
4579
357034632022
TVRTSAD
MT2187FreeZD2 conjugated to a clinical contrast agent gadoteridol Gd(HP-DO3A) using N3 linkerLinearLNoneZD2 analogCancer targeting contrast agentBlood samples were collected from jugular veins at predose and at 2, 5, 10, 15, 30, and 45 minutes and 1, 2, 3, and 4 hours after dosing from group 1 to 30.1 mmol/kg0.32 (Elimination Half Life)Female SD rats plasma proteaseICP-MSFemale SD rats plasmaIn VivoNoneNoneMT218 did not inhibit the enzyme activities of CYP1A2, CYP2B6, CYP2C9, CYP2C19, CYP2D6, or CYP3A4 at concentrations up to 100 μM
4580
357034632022
TVRTSAD
MT2187FreeZD2 conjugated to a clinical contrast agent gadoteridol Gd(HP-DO3A) using N3 linkerLinearLNoneZD2 analogCancer targeting contrast agentBlood samples were collected from jugular veins at predose and at 2, 5, 10, 15, 30, and 45 minutes and 1, 2, 3, and 4 hours after dosing from group 1 to 30.1 mmol/kg0.65 (Elimination Half Life)(P) SD rats plasma proteaseICP-MS(P) SD rats plasmaIn VivoNoneNoneMT218 did not inhibit the enzyme activities of CYP1A2, CYP2B6, CYP2C9, CYP2C19, CYP2D6, or CYP3A4 at concentrations up to 100 μM
4581
357034632022
TVRTSAD
MT2187FreeZD2 conjugated to a clinical contrast agent gadoteridol Gd(HP-DO3A) using N3 linkerLinearLNoneZD2 analogCancer targeting contrast agentBlood samples were collected from jugular veins at predose and at 2, 5, 10, 15, 30, and 45 minutes and 1, 2, 3, and 4 hours after dosing from group 1 to 30.2 mmol/kg0.3 (Elimination Half Life)Male SD rats plasma proteaseICP-MSMale SD rats plasmaIn VivoNoneNoneMT218 did not inhibit the enzyme activities of CYP1A2, CYP2B6, CYP2C9, CYP2C19, CYP2D6, or CYP3A4 at concentrations up to 100 μM
4582
357034632022
TVRTSAD
MT2187FreeZD2 conjugated to a clinical contrast agent gadoteridol Gd(HP-DO3A) using N3 linkerLinearLNoneZD2 analogCancer targeting contrast agentBlood samples were collected from jugular veins at predose and at 2, 5, 10, 15, 30, and 45 minutes and 1, 2, 3, and 4 hours after dosing from group 1 to 30.2 mmol/kg0.32 (Elimination Half Life)Female SD rats plasma proteaseICP-MSFemale SD rats plasmaIn VivoNoneNoneMT218 did not inhibit the enzyme activities of CYP1A2, CYP2B6, CYP2C9, CYP2C19, CYP2D6, or CYP3A4 at concentrations up to 100 μM
4583
357034632022
TVRTSAD
MT2187FreeZD2 conjugated to a clinical contrast agent gadoteridol Gd(HP-DO3A) using N3 linkerLinearLNoneZD2 analogCancer targeting contrast agentBlood samples were collected from jugular veins at predose and at 2, 5, 10, 15, 30, and 45 minutes and 1, 2, 3, and 4 hours after dosing from group 1 to 30.2 mmol/kg0.22 (Elimination Half Life)(P) SD rats plasma proteaseICP-MS(P) SD rats plasmaIn VivoNoneNoneMT218 did not inhibit the enzyme activities of CYP1A2, CYP2B6, CYP2C9, CYP2C19, CYP2D6, or CYP3A4 at concentrations up to 100 μM
4584
357034632022
TVRTSAD
MT2187FreeZD2 conjugated to a clinical contrast agent gadoteridol Gd(HP-DO3A) using N3 linkerLinearLNoneZD2 analogCancer targeting contrast agentBlood samples were collected from fore limb veins at predose and at 5, 10, 15, 30, and 45 minutes and 1, 1.5, 2, 3, 4, and 6 hours after dosing from group 1 to 3.0.04 mmol/kg0.76 (Elimination Half Life)Male dogs plasma proteaseICP-MSMale dogs plasmaIn VivoNoneNoneMT218 did not inhibit the enzyme activities of CYP1A2, CYP2B6, CYP2C9, CYP2C19, CYP2D6, or CYP3A4 at concentrations up to 100 μM
4585
357034632022
TVRTSAD
MT2187FreeZD2 conjugated to a clinical contrast agent gadoteridol Gd(HP-DO3A) using N3 linkerLinearLNoneZD2 analogCancer targeting contrast agentBlood samples were collected from fore limb veins at predose and at 5, 10, 15, 30, and 45 minutes and 1, 1.5, 2, 3, 4, and 6 hours after dosing from group 1 to 3.0.04 mmol/kg0.74 (Elimination Half Life)Female dogs plasma proteaseICP-MSFemale dogs plasmaIn VivoNoneNoneMT218 did not inhibit the enzyme activities of CYP1A2, CYP2B6, CYP2C9, CYP2C19, CYP2D6, or CYP3A4 at concentrations up to 100 μM
4586
357034632022
TVRTSAD
MT2187FreeZD2 conjugated to a clinical contrast agent gadoteridol Gd(HP-DO3A) using N3 linkerLinearLNoneZD2 analogCancer targeting contrast agentBlood samples were collected from fore limb veins at predose and at 5, 10, 15, 30, and 45 minutes and 1, 1.5, 2, 3, 4, and 6 hours after dosing from group 1 to 3.0.04 mmol/kg0.8 (Elimination Half Life)(P) dogs plasma proteaseICP-MS(P) dogs plasmaIn VivoNoneNoneMT218 did not inhibit the enzyme activities of CYP1A2, CYP2B6, CYP2C9, CYP2C19, CYP2D6, or CYP3A4 at concentrations up to 100 μM
4587
357034632022
TVRTSAD
MT2187FreeZD2 conjugated to a clinical contrast agent gadoteridol Gd(HP-DO3A) using N3 linkerLinearLNoneZD2 analogCancer targeting contrast agentBlood samples were collected from fore limb veins at predose and at 5, 10, 15, 30, and 45 minutes and 1, 1.5, 2, 3, 4, and 6 hours after dosing from group 1 to 3.0.1 mmol/kg0.7 (Elimination Half Life)Male dogs plasma proteaseICP-MSMale dogs plasmaIn VivoNoneNoneMT218 did not inhibit the enzyme activities of CYP1A2, CYP2B6, CYP2C9, CYP2C19, CYP2D6, or CYP3A4 at concentrations up to 100 μM
4588
357034632022
TVRTSAD
MT2187FreeZD2 conjugated to a clinical contrast agent gadoteridol Gd(HP-DO3A) using N3 linkerLinearLNoneZD2 analogCancer targeting contrast agentBlood samples were collected from fore limb veins at predose and at 5, 10, 15, 30, and 45 minutes and 1, 1.5, 2, 3, 4, and 6 hours after dosing from group 1 to 3.0.1 mmol/kg0.67 (Elimination Half Life)Female dogs plasma proteaseICP-MSFemale dogs plasmaIn VivoNoneNoneMT218 did not inhibit the enzyme activities of CYP1A2, CYP2B6, CYP2C9, CYP2C19, CYP2D6, or CYP3A4 at concentrations up to 100 μM
4589
357034632022
TVRTSAD
MT2187FreeZD2 conjugated to a clinical contrast agent gadoteridol Gd(HP-DO3A) using N3 linkerLinearLNoneZD2 analogCancer targeting contrast agentBlood samples were collected from fore limb veins at predose and at 5, 10, 15, 30, and 45 minutes and 1, 1.5, 2, 3, 4, and 6 hours after dosing from group 1 to 3.0.1 mmol/kg0.33 (Elimination Half Life)(P) dogs plasma proteaseICP-MS(P) dogs plasmaIn VivoNoneNoneMT218 did not inhibit the enzyme activities of CYP1A2, CYP2B6, CYP2C9, CYP2C19, CYP2D6, or CYP3A4 at concentrations up to 100 μM
4590
357034632022
TVRTSAD
MT2187FreeZD2 conjugated to a clinical contrast agent gadoteridol Gd(HP-DO3A) using N3 linkerLinearLNoneZD2 analogCancer targeting contrast agentBlood samples were collected from fore limb veins at predose and at 5, 10, 15, 30, and 45 minutes and 1, 1.5, 2, 3, 4, and 6 hours after dosing from group 1 to 3.0.2 mmol/kg0.69 (Elimination Half Life)Male dogs plasma proteaseICP-MSMale dogs plasmaIn VivoNoneNoneMT218 did not inhibit the enzyme activities of CYP1A2, CYP2B6, CYP2C9, CYP2C19, CYP2D6, or CYP3A4 at concentrations up to 100 μM
4591
357034632022
TVRTSAD
MT2187FreeZD2 conjugated to a clinical contrast agent gadoteridol Gd(HP-DO3A) using N3 linkerLinearLNoneZD2 analogCancer targeting contrast agentBlood samples were collected from fore limb veins at predose and at 5, 10, 15, 30, and 45 minutes and 1, 1.5, 2, 3, 4, and 6 hours after dosing from group 1 to 3.0.2 mmol/kg0.63 (Elimination Half Life)Female dogs plasma proteaseICP-MSFemale dogs plasmaIn VivoNoneNoneMT218 did not inhibit the enzyme activities of CYP1A2, CYP2B6, CYP2C9, CYP2C19, CYP2D6, or CYP3A4 at concentrations up to 100 μM
4592
357034632022
TVRTSAD
MT2187FreeZD2 conjugated to a clinical contrast agent gadoteridol Gd(HP-DO3A) using N3 linkerLinearLNoneZD2 analogCancer targeting contrast agentBlood samples were collected from fore limb veins at predose and at 5, 10, 15, 30, and 45 minutes and 1, 1.5, 2, 3, 4, and 6 hours after dosing from group 1 to 3.0.2 mmol/kg0.048 (Elimination Half Life)(P) dogs plasma proteaseICP-MS(P) dogs plasmaIn VivoNoneNoneMT218 did not inhibit the enzyme activities of CYP1A2, CYP2B6, CYP2C9, CYP2C19, CYP2D6, or CYP3A4 at concentrations up to 100 μM
4593
356884762022
DNPSLSIDLTFHLLRTLLELEKQEKEKQQACQNRIIFDSV
PEG-hUCN140FreeAmidationLinearLInsertion of a cysteine residue at position 31 for pegylation PEG20 acetamideHuman UCN1 derivativeTreating Autoimmune diseaseN.A.0.3 mg/kg13C57Bl/6J mice plasma proteaseLaser capture/mass spectrometryC57BL/6J mice plasmaIn VivoNoneNoneAt the CRHR1 receptor, the PEG-hUCN1 peptide was less potent than native CRH or UCN1 peptides with EC50 values of 47, 15, and 10 nM, respectively
4594
356884762022
DNPSLSIDLTFHLLRTLLELEKQEKEKQQACQNRIIFDSV
PEG-hUCN140FreeAmidationLinearLInsertion of a cysteine residue at position 31 for pegylation Human UCN1 derivativeTreating Autoimmune diseaseN.A.1 mg/kg17C57Bl/6J mice plasma proteaseLaser capture/mass spectrometryC57BL/6J mice plasmaIn VivoNoneNoneAt the CRHR2 receptor, the PEG-hUCN1 peptide was also less potent than UCN2 or UCN1 peptides with EC50 values of 80, 10, and 6.6 nM, respectively 
4595
356773072022
MTPLGPASSLPQSFLLKCLEQVRKIQADGAALLANQVRQVGDGAALQEKLVSELGNALENALPDTLDTLQLDVKDYFSLRAALLAALPTRLRYLQEADAFQRRAGGVLVASHLGTSLQRLALADSGVLRQLLYYIESGPHQAPLGTGGADQGAMNVTCSKELQAYREQILHDCWLPKDLKDLQLLIEMNVTVLVDIDKLVEVLRLRQGVLHGVHVC
rhG-CSF175FreeFreeLinearLNoneRecombinant human methionyl-granulocyte colonystimulating factorN.A.Sampling time - 0, 0.083, 0.25, 0.5, 1, 2, 4, 8, 12, 24 h1.0 mg/kg2.74 ± 0.33Mice Serum ProteaseELISAMice serum In VivoNoneNoneN.A.
4596
356773072022
MTPLGPASSLPQSFLLKCLEQVRKIQADGAALLANQVRQVGDGAALQEKLVSELGNALENALPDTLDTLQLDVKDYFSLRAALLAALPTRLRYLQEADAFQRRAGGVLVASHLGTSLQRLALADSGVLRQLLYYIESGPHQAPLGTGGADQGAMNVTCSKELQAYREQILHDCWLPKDLKDLQLLIEMNVTVLVDIDKLVEVLRLRQGVLHGVHVC
PEG10k-rhG-CSF175FreeFreeLinearLPEG10K-MAL fatty chain-modification of rhG-CSF at Cys18 positionrhG-CSF derivativeN.A.sampling time - 0, 0.5, 2, 4, 8, 12, 24, 48, 72, 96, 120, 144, 168h1.0 mg/kg13.05 ± 0.45Mice Serum ProteaseELISAMice serum In VivoNoneNoneN.A.
4597
356773072022
MTPLGPASSLPQSFLLKCLEQVRKIQADGAALLANQVRQVGDGAALQEKLVSELGNALENALPDTLDTLQLDVKDYFSLRAALLAALPTRLRYLQEADAFQRRAGGVLVASHLGTSLQRLALADSGVLRQLLYYIESGPHQAPLGTGGADQGAMNVTCSKELQAYREQILHDCWLPKDLKDLQLLIEMNVTVLVDIDKLVEVLRLRQGVLHGVHVC
C15-rhG-CSF175FreeFreeLinearLC15-MAL fatty chain-modification of rhG-CSF at Cys18 positionrhG-CSF derivativeN.A.sampling time - 0, 0.5, 2, 4, 8, 12, 24, 48, 72, 96, 120, 144, 168 h1.0 mg/kg5.72 ± 0.43Mice Serum ProteaseELISAMice serum In VivoNoneNoneN.A.
4598
356748802022
Y-Aib-EGTFTSDYSI-Aib-LDKIAQKAFVQWLIAGGPSSGAPPPS
Tirzepatide39FreeFreeLinearLC20 fatty diacid conjugation at the side chain of the Lys20, Aib = alpha-amino isobutyric acid at position 2,13GLP-1 analogsAntidiabetesPlasma concentrations of tirzepatide measured pre-dose, and at 8, 12, 24, 48, 72, 96, 168, and 336 hours post-dose5 mg124Human Plasma Protease LC-MSHuman plasma with Normal hepatic functionIn VivoNoneNoneN.A.
4599
356748802022
Y-Aib-EGTFTSDYSI-Aib-LDKIAQKAFVQWLIAGGPSSGAPPPS
Tirzepatide39FreeFreeLinearLC20 fatty diacid conjugation at the side chain of the Lys20, Aib = alpha-amino isobutyric acid at position 2,13GLP-1 analogsAntidiabetesPlasma concentrations of tirzepatide measured pre-dose, and at 8, 12, 24, 48, 72, 96, 168, and 336 hours post-dose5 mg131Human Plasma Protease LC-MSHuman plasma with Mild hepatic impairmentIn VivoNoneNoneN.A.
4600
356748802022
Y-Aib-EGTFTSDYSI-Aib-LDKIAQKAFVQWLIAGGPSSGAPPPS
Tirzepatide39FreeFreeLinearLC20 fatty diacid conjugation at the side chain of the Lys20, Aib = alpha-amino isobutyric acid at position 2,13GLP-1 analogsAntidiabetesPlasma concentrations of tirzepatide measured pre-dose, and at 8, 12, 24, 48, 72, 96, 168, and 336 hours post-dose5 mg116Human Plasma Protease LC-MSHuman plasma with Moderate hepatic impairmentIn VivoNoneNoneN.A.
4601
356748802022
Y-Aib-EGTFTSDYSI-Aib-LDKIAQKAFVQWLIAGGPSSGAPPPS
Tirzepatide39FreeFreeLinearLC20 fatty diacid conjugation at the side chain of the Lys20, Aib = alpha-amino isobutyric acid at position 2,13GLP-1 analogsAntidiabetesPlasma concentrations of tirzepatide measured pre-dose, and at 8, 12, 24, 48, 72, 96, 168, and 336 hours post-dose5 mg122Human Plasma Protease LC-MSHuman plasma with Severe hepatic impairmentIn VivoNoneNoneN.A.
4602
356597202022
LPLTPLP
DTX-P77DTXFreeLinearLNoneDocetaxel (DTX) and heptapeptide (P7) Fusion protein Anticancer (Treatment Of Non-Small Cell Lung Cancer)1, 2, 4, 12, 24, 48 and 72 h after injection, the mice were anesthetized, and approximately 0.5 ml of blood was collected60 mg/kgLonger Half LifeBALB/c mice plasma proteaseHPLCBALB/c mice bearing A549 tumors plasmaIn VivoNoneNoneIC50 = 11.4 nM for DTX-P7 in A549 cells
4603
356597202022
LPLTPLP
DTX-P77DTXFreeLinearLNoneDocetaxel (DTX) and heptapeptide (P7) Fusion protein Anticancer (Treatment Of Non-Small Cell Lung Cancer)1, 2, 4, 12, 24, 48 and 72 h after injection, the mice were anesthetized, and approximately 0.5 ml of blood was collected60 mg/kgLonger Half LifeBALB/c mice plasma proteaseHPLCBALB/c mice bearing A549 tumors plasmaIn VivoNoneNoneIC50 = 0.62 nM for DTX-P7 in H1975 cells
4604
356536952022
GCTRQYPCGKG
KLK5 inhibitor11FreeA short linker GKG was attached at C terminal and then ALbumin tag was linked with Lys via PEG2Cyclic (C2-C8 Disulfide Bond)LNoneSyntheticTreatment for Netherton syndromeN.A.6.2 mg/kg4.4 ± 0.3 (Terminal Half Life)Mice plasma proteaseHPLC analysis with fluorescence detectionMice plasmaIn VivoNoneNoneKi(KLK5)(nM) = 1.2, Kd(albumin)(nM) = 119 (for KLK5(1)-tag)
4605
356536952022
PCLYLARCSGKG
KLK7 inhibitor11FreeA short linker GKG was attached at C terminal and then ALbumin tag was linked with Lys via PEG2Cyclic (C2-C8 Disulfide Bond)LNoneSyntheticTreatment for Netherton syndromeN.A.6.2 mg/kg6.2 ± 0.9 (Terminal Half Life)Mice plasma proteaseHPLC analysis with fluorescence detectionMice plasmaIn VivoNoneNoneKi(KLK7)(nM) = 32, Kd(albumin)(nM) = 164 (for KLK7(1)-tag)
4606
356536952022
GCTRQYPCGKG
KLK5 inhibitor11FreeA short linker GKG was attached at C terminal and then ALbumin tag was linked with Lys via PEG2Cyclic (C2-C8 Disulfide Bond)LNoneSyntheticTreatment for Netherton syndromeN.A.6.2 mg/kg5.1 ± 0.7 (Terminal Half Life)Mice plasma proteaseHPLC analysis with fluorescence detectionMice plasmaIn VivoNoneNoneKi(KLK5)(nM) = 1.2, Kd(albumin)(nM) = 119 (for KLK5(1)-tag)
4607
356536952022
GCTRQYPCGKG
KLK5 inhibitor11freeA short linker GKG was attached at C terminal and then ALbumin tag was linked with Lys via PEG2Cyclic (C2-C8 Disulfide Bond)LNoneSyntheticTreatment for Netherton syndromeN.A.6.2 mg/kg5.8 ± 0.4 (Terminal Half Life)Mice plasma proteaseHPLC analysis with fluorescence detectionMice plasmaIn VivoNoneNoneKi(KLK5)(nM) = 1.2, Kd(albumin)(nM) = 119 (for KLK5(1)-tag)
4608
356465432022
HsQGTFTSDYSKYLDKRRAQDFVQWLLNTGGPSSGAPPPS
TB00140FreeAmidation, GGPSSGAPPPS introduced in the C-terminalCyclic (R17-D21 Lactam Bridge)MixD serine modifcation at 2, side chain modification at Lysine (n=12, R=CH3)GLP-1 and GCG chimera analogTreatment of Multiple Causes of Hepatic FibrosisN.A.15.3 μg/kg0.498 ± 0.0100Rhesus monkeys plasma proteaseHPLC–MS/MSRhesus monkeys plasmaIn VivoNoneNoneGCGR EC50(nmol/L) = 0.01, GLP-1R EC50(nmol/L) = 0.04 
4609
356465432022
HsQGTFTSDYSKYLDKRRAQDFVQWLLNTGGPSSGAPPPS
TB00140FreeAmidation, GGPSSGAPPPS introduced in the C-terminalCyclic (R17-D21 Lactam Bridge)MixD serine modifcation at 2, side chain modification at Lysine (n=12, R=CH3)GLP-1 and GCG chimera analogTreatment of Multiple Causes of Hepatic FibrosisN.A.5 μg/kg3.33 ± 1.57Rhesus monkeys plasma proteaseHPLC–MS/MSRhesus monkeys plasmaIn VivoNoneNoneGCGR EC50(nmol/L) = 0.01, GLP-1R EC50(nmol/L) = 0.04 
4610
356465432022
HsQGTFTSDYSKYLDKRRAQDFVQWLLNTGGPSSGAPPPS
TB00140FreeAmidation, GGPSSGAPPPS introduced in the C-terminalCyclic (R17-D21 Lactam Bridge)MixD serine modifcation at 2, side chain modification at Lysine (n=12, R=CH3)GLP-1 and GCG chimera analogTreatment of Multiple Causes of Hepatic FibrosisN.A.20 μg/kg2.83 ± 1.42Rhesus monkeys plasma proteaseHPLC–MS/MSRhesus monkeys plasmaIn VivoNoneNoneGCGR EC50(nmol/L) = 0.01, GLP-1R EC50(nmol/L) = 0.04 
4611
356465432022
HsQGTFTSDYSKYLDKRRAQDFVQWLLNTGGPSSGAPPPS
TB00140FreeAmidation, GGPSSGAPPPS introduced in the C-terminalCyclic (R17-D21 Lactam Bridge)MixD serine modifcation at 2, side chain modification at Lysine (n=12, R=CH3)GLP-1 and GCG chimera analogTreatment of Multiple Causes of Hepatic FibrosisN.A.60 μg/kg2.47 ± 0.571Rhesus monkeys plasma proteaseHPLC–MS/MSRhesus monkeys plasmaIn VivoNoneNoneGCGR EC50(nmol/L) = 0.01, GLP-1R EC50(nmol/L) = 0.04 
4612
356465432022
HsQGTFTSDYSKYLDKRRAQDFVQWLLNTGGPSSGAPPPS
TB00140FreeAmidation, GGPSSGAPPPS introduced in the C-terminalCyclic (R17-D21 Lactam Bridge)MixD serine modifcation at 2, side chain modification at Lysine (n=12, R=CH3)GLP-1 and GCG chimera analogTreatment of Multiple Causes of Hepatic Fibrosis1 day20 μg/kg3.07 ± 1.28Rhesus monkeys plasma proteaseHPLC–MS/MSRhesus monkeys plasmaIn VivoNoneNoneGCGR EC50(nmol/L) = 0.01, GLP-1R EC50(nmol/L) = 0.04 
4613
356465432022
HsQGTFTSDYSKYLDKRRAQDFVQWLLNTGGPSSGAPPPS
TB00140FreeAmidation, GGPSSGAPPPS introduced in the C-terminalCyclic (R17-D21 Lactam Bridge)MixD serine modifcation at 2, side chain modification at Lysine (n=12, R=CH3)GLP-1 and GCG chimera analogTreatment of Multiple Causes of Hepatic Fibrosis7 days20 μg/kg1.94 ± 0.305Rhesus monkeys plasma proteaseHPLC–MS/MSRhesus monkeys plasmaIn VivoNoneNoneGCGR EC50(nmol/L) = 0.01, GLP-1R EC50(nmol/L) = 0.04 
4614
355828522022
lKlW
CP8FreePNAM37 linked through NH2 groupCyclic(N-C terminal bond)MixD-leucine at position 1 and 3SyntheticDrug delivery vectorsBlood samples (0.2 mL) were taken prior to dose administration and at 1, 5, 10, 20, 30, 60, 120, 180, 240, 360, 480, and 1440 min after dose administratio1 μCi14.6 ± 2.9 (Elimination Half Life)Rats plasma proteaseLiquid scintillation counterRats plasmaIn VivoNoneNoneFor concentrations of 1 mg/mL CP , cell viabilities drop to about 75% for the 4T1 cell line
4615
354583852022
RDLEVVAATPTSLLISWDAPAVTVRYYRITYGETGGNSPVQEFTVPGSKSTATISGLKPGVDYTITVYAVTGRGDSPASSKPISINYRTEIGGGGSGGGGSGGGGSGGGGSGGGGSGGGGSGGGGSSLDQINVTFLDLEYEMKKLEEAIKKLEESYIDLKEL
FL-EK1162Flexible 35-mer linker (L35) connects the FN3 domain to the EK1 peptide at N terminusFreeLinearLNoneEK1 and 10th FN3 unit conjugatePan-cov fusion inhibitorSerum samples were collected before (0 h) and after injection of EK1 (0.5 h, 1 h, 3 h, 7 h, and 12 h) or FL-EK1 (0.5 h, 1 h, 3 h, 7 h, 24 h, 48 h, 72 h, and 96 h)40 mg/kg 30.0 ± 12.8Mice serum proteaseSandwich ELISAMice serumIn VivoNoneNoneIC50(nM) = 114.5 ± 33.4 against B.1.1.7 (Alpha), IC50(nM) = 201.2 ± 16.8 against B.1.351 (Beta), IC50(nM) = 373.1 ± 16.9 against P.1 (Gamma), IC50(nM) = 133.0 ± 16.5 against B.1.617.2 (Delta), IC50(nM) = 179.2 ± 38.3 against B.1.525 (Eta), IC50(nM) = 230.9 ± 49.3 against B.1.617.1 (Kappa), IC50(nM) = 88.5 ± 58.2 against C.37 (Lambda), IC50(nM) = 297.5 ± 188.2 against B.1.1.529 (Omicron)
4616
354583852022
SLDQINVTFLDLEYEMKKLEEAIKKLEESYIDLKEL
EK136FreeFreeLinearLNoneExpression in E. coliPan-cov fusion inhibitorSerum samples were collected before (0 h) and after injection of EK1 (0.5 h, 1 h, 3 h, 7 h, and 12 h) or FL-EK1 (0.5 h, 1 h, 3 h, 7 h, 24 h, 48 h, 72 h, and 96 h)8.25 mg/kg1.8 ± 1.0Mice serum proteaseSandwich ELISAMice serumIn VivoNoneNoneIC50(nM) = 69.0 ± 20.8 against B.1.1.7 (Alpha), IC50(nM) = 109.9 ± 25.3 against B.1.351 (Beta), IC50(nM) = 191.3 ± 17.0 against P.1 (Gamma), IC50(nM) = 190.6 ± 29.0 against B.1.617.2 (Delta), IC50(nM) = 135.6 ± 11.2 against B.1.525 (Eta), IC50(nM) = 107.1 ± 7.3 against B.1.617.1 (Kappa), IC50(nM) = 68.7 ± 25.4 against C.37 (Lambda), IC50(nM) = 236.8 ± 10.6 against B.1.1.529 (Omicron)
4617
354554212022
RDLEVVAATPTSLLISWDAPAVTVRYYRITYGETGGNSPVQEFTVPGSKSTATISGLKPGVDYTITVYAVTGRGDSPASSKPISINYRTEIGGGGSGGGGSGGGGSGGGGSGGGGSGGGGSGGGGSTTWEAWDRAIAEYAARIEALLRALQEQQEKNEAALRE
FLT163FN3 domainFreeLinearLNoneFN3 ,T1144 fusion proteinAntiviral (HIV fusion inhibitor)Blood samples were collected from the orbital sinus at 0, 0.5, 1.5, 3, 6, 9, 12, 24, 48, 72, 96 and 120 h after injection of the inhibitors tested5.94 mg/kg27.09 ± 6.9Rats serum proteaseSandwich ELISARats serum In VivoNoneNoneIC50(nM)= 65.3 ± 2.6 against HIV-1 96USSN20 (X4/R5, A), IC50(nM) = 9.8 ± 0.9 against HIV-1 96USNG17 (X4, A), IC50(nM) = 6.5 ± 0.2 against HIV-1 90US_873 (R5, B), IC50(nM) = 8.8 ± 0.3 against HIV-1 BZ167 (X4, B), IC50(nM) = 12.5 ± 0.5 against HIV-1 SE364 (R5, C), IC50(nM) = 9.3 ± 0.5 against HIV-1 PBL288 (R5, C), IC50(nM) = 11.7 ± 0.8 against HIV-1 92UG001 (X4/R5, D), IC50(nM) = 6.4 ± 0.3 against HIV-1 J32228M4 (R5, D), IC50(nM) = 7.5 ± 0.3 against HIV-1 DJ263 (R5, CRF02_AG), IC50(nM) = 10.2 ± 0.6 against HIV-1 CAM1475MV (R5, CRF02_AG) (Infection on MT-4 cells) 
4618
354554212022
TTWEAWDRAIAEYAARIEALLRALQEQQEKNEAALRE
T1144 37FreeFreeLinearLNoneFully or partially derived from the HIV-1 gp41 CHR domainAntiviral (HIV fusion inhibitor)Blood samples were collected from the orbital sinus at 0, 0.5, 1.5, 3, 6, 9, 12, 24, 48, 72, 96 and 120 h after injection of the inhibitors tested1.28 mg/kg7.48 ± 0.4Rats serum proteaseSandwich ELISARats serum In VivoNoneNoneIC50(nM) = 3.9 against infection of HIV-1 IIIB (X4 tropic) strain
4619
354554212022
YTSLIHSLIEESQNQQEKNEQELLELDKWASLWNWF
T20 (enfuvirtide)36FreeFreeLinearLNoneDerived from the natural sequence (aa 643–678) of the HIV-1 gp41 C-terminal heptad repeat (CHR) domainAntiviral (HIV fusion inhibitor)Blood samples were collected from the orbital sinus at 0, 0.5, 1.5, 3, 6, 9, 12, 24, 48, 72, 96 and 120 h after injection of the inhibitors tested1.26 mg/kg1.22 ± 0.2 Rats serum proteaseSandwich ELISARats serum In VivoNoneNoneIC50(nM)= 55.3 ± 2.4 against HIV-1 96USSN20 (X4/R5, A),IC50(nM) = 49.3 ± 4.9 against HIV-1 96USNG17 (X4, A), IC50(nM) = 50.1 ± 2.0 against HIV-1 90US_873 (R5, B), IC50(nM) =53.9 ± 4.3 against HIV-1 BZ167 (X4, B), IC50(nM) = 45.2 ± 3.2 against HIV-1 SE364 (R5, C), IC50(nM) = 46.9 ± 2.1 against HIV-1 PBL288 (R5, C), IC50(nM) = 77.1 ± 6.8 against HIV-1 92UG001 (X4/R5, D), IC50(nM) = 21.1 ± 1.1 against HIV-1 J32228M4 (R5, D), IC50(nM) = 55.6 ± 1.2 against HIV-1 DJ263 (R5, CRF02_AG), IC50(nM) = 61.2 ± 1.3 against HIV-1 CAM1475MV (R5, CRF02_AG) (infection on MT-4 cell) 
4620
354386952022
SFQ
SFQSeM3FreeSelenium methylated conjugation at C terminalLinearLNoneFrom soybeansEffective Se nutritional supplementN.A.N.A.81.60 ± 11.88N.A.N.A.N.A.N.A.NoneNoneN.A.
4621
354303362022
KPSSPPEE
A6 peptide8AcetylationAmidationLinearLNoneSyntheticAntitumorN.A.N.A.N.A.N.A.N.A.N.A.N.A.NoneNoneN.A.
4622
354148772022
MCFQYFHILWPFCGSGSDYKDDDDK
B_3.125C18 diacid-gGlu-2xOEGAmidation, FLAG tagCyclicLNoneSyntheticTargets GIP receptorAt selected time points samples were taken: 5, 15, 30, 60, 120, 210, 300 mins1 μMStableHuman plasma protease LC-MS80% pooled human Li-heparin plasma In VitroNoneNoneIC50(nM) = 347
4623
354148772022
MSFQYFHILWPFSGSGSDYKDDDDK
B_3.225AcetylationAmidation, FLAG tagLinearLNoneSyntheticTargets GIP receptorAt selected time points samples were taken: 5, 15, 30, 60, 120, 210, 300 mins1 μM~2Human plasma protease LC-MS80% pooled human Li-heparin plasma In VitroNoneNoneIC50(nM) = 7890
4624
354148772022
MCFTHFHMLWPFCGSGSDYKDDDDK
B_127525AcetylationAmidation, FLAG tagCyclicLNoneSyntheticTargets GIP receptorAt selected time points samples were taken: 5, 15, 30, 60, 120, 210, 300 mins1 μM~3.5Human plasma protease LC-MS80% pooled human Li-heparin plasma In VitroNoneNoneIC50(nM) = 2076
4625
354148772022
MCFTHFHMLWPFCGSGSDYKDDDDK
B_1275.125C18 diacid-gGlu-2xOEGAmidation, FLAG tagCyclicLNoneSyntheticTargets GIP receptorAt selected time points samples were taken: 5, 15, 30, 60, 120, 210, 300 mins1 μMStableHuman plasma protease LC-MS80% pooled human Li-heparin plasma In VitroNoneNoneIC50(nM) = 1209
4626
354148772022
MSFTHFHMLWPFSGSGSDYKDDDDK
B_1275.225AcetylationAmidation, FLAG tagLinearLNoneSyntheticTargets GIP receptorAt selected time points samples were taken: 5, 15, 30, 60, 120, 210, 300 mins1 μM~2Human plasma protease LC-MS80% pooled human Li-heparin plasma In VitroNoneNoneIC50(nM) = 8336
4627
354148772022
MCFTHFHMLWPFC
B_1275.314C18 diacid-gGlu-2xOEGAmidation, FLAG tagCyclicLNoneSyntheticTargets GIP receptorAt selected time points samples were taken: 5, 15, 30, 60, 120, 210, 300 mins1 μMStableHuman plasma protease LC-MS80% pooled human Li-heparin plasma In VitroNoneNoneIC50(nM) = 159
4628
354148772022
ACFTHFDLLWPFCGSGSDYKDDDDK
B_1275.425AcetylationAmidation, FLAG tagCyclicLNoneSyntheticTargets GIP receptorAt selected time points samples were taken: 5, 15, 30, 60, 120, 210, 300 mins1 μMStableHuman plasma protease LC-MS80% pooled human Li-heparin plasma In VitroNoneNoneIC50(nM) = 826
4629
354148772022
ACFTHFDLLWPFC
B_1275.514AcetylationFreeCyclicLNoneSyntheticTargets GIP receptorAt selected time points samples were taken: 5, 15, 30, 60, 120, 210, 300 mins1 μMStableHuman plasma protease LC-MS80% pooled human Li-heparin plasma In VitroNoneNoneIC50(nM) = 2300
4630
354148772022
ACFTHFDLLWPFC
B_1275.614C18 diacid-gGlu-2xOEGFreeCyclicLNoneSyntheticTargets GIP receptorAt selected time points samples were taken: 5, 15, 30, 60, 120, 210, 300 mins1 μMStableHuman plasma protease LC-MS80% pooled human Li-heparin plasma In VitroNoneNoneIC50(nM) = 860
4631
354148772022
MVATKTFALLLLSLFLAVGLGEKKEGHFSALPSLPVGSHAKVSSPQPRGPRYAEGTFISDYSIAMDKIHQQDFVNWLLAQKGKKNDWKHNITQREARALELASQANRKEEEAVEPQSSPAKNPSDEDLLRDLLIQELLACLLDQTNLCRLRSR
Native GIP153FreeFreeLinearLNoneGlucagonGlucose dependent insulinotropic At selected time points samples were taken: 5, 15, 30, 60, 120, 210, 300 mins1 μM45Human plasma protease LC-MS80% pooled human Li-heparin plasma In VitroNoneNoneN.A.
4632
354148772022
HAEGTFTSDVSSYLEGQAAKEFIAWLVKGRG
GLP-131FreeFreeLinearLNoneGlucagonAntidiabetesAt selected time points samples were taken: 5, 15, 30, 60, 120, 210, 300 mins1 μM35Human plasma protease LC-MS80% pooled human Li-heparin plasma In VitroPDB id: 5VAINoneN.A.
4633
354148772022
MCFQYFHILWPFCGSGSDYKDDDDK
B_3.125C18 diacid-gGlu-2xOEGAmidation, FLAG tagCyclicLNoneSyntheticTargets GIP receptorN.A.2 μM585 (Elimination Half Life)Rats plasma proteaseLC-MSRats plasmaIn VivoNoneNoneIC50(nM) = 347
4634
354148772022
MCFTHFHMLWPFCGSGSDYKDDDDK
B_1275.125C18 diacid-gGlu-2xOEGAmidation, FLAG tagCyclicLNoneSyntheticTargets GIP receptorN.A.2 μM643(Elimination Half Life)Rats plasma proteaseLC-MSRats plasmaIn VivoNoneNoneIC50(nM) = 1209
4635
354148772022
ACFTHFDLLWPFCGSGSDYKDDDDK
B_1275.425AcetylationAmidation, FLAG tagCyclicLNoneSyntheticTargets GIP receptorN.A.2 μM3.767 (Elimination half life)Rats plasma proteaseLC-MSRats plasmaIn VivoNoneNoneIC50(nM) = 826
4636
354148772022
ACFTHFDLLWPFC
B_1275.514AcetylationFreeCyclicLNoneSyntheticTargets GIP receptorN.A.2 μM2.367 (Elimination half life)Rats plasma proteaseLC-MSRats plasmaIn VivoNoneNoneIC50(nM) = 2300
4637
354148772022
ACFTHFDLLWPFC
B_1275.614C18 diacid-gGlu-2xOEGFreeCyclicLNoneSyntheticTargets GIP receptorN.A.2 μM250 (Elimination Half Life)Rats plasma proteaseLC-MSRats plasmaIn VivoNoneNoneIC50(nM) = 860
4638
353594942022
EMRLSKFFRDFILQRKK
CSP117FreeFreeLinearLNoneCompetence stimulating peptideModulates Quorum Sensing In Streptococcus PneumoniaeAliquots (100 μL) were taken at 0, 0.5, 1, 2, 3, 4, 5, 6, and 24 h time points1 mM30Trypsin RP-HPLCPBS solutionIn VitroNoneNoneEC50(nM) = 10 for CSP1 against ComD1 receptor, EC50(nM) = 530 for CSP1 against ComD2 receptor
4639
353594942022
EMRLSKFFRDFILQRKK
CSP117FreeFreeLinearLNoneCompetence stimulating peptideModulates Quorum Sensing In Streptococcus PneumoniaeAliquots (100 μL) were taken at 0, 0.5, 1, 2, 3, 4, 5, 6, and 24 h time points1 mM1ChymotrypsinRP-HPLCPBS solutionIn VitroNoneNoneEC50(nM) = 10 for CSP1 against ComD1 receptor, EC50(nM) = 530 for CSP1 against ComD2 receptor
4640
353594942022
AMRLSK-Cha-FRDFILQRKK
CSP1-E1A/F7Cha17FreeFreeLinearLintroduction of Cha = cyclohexylalanine residues at position 7,E1A substituitionsCSP1 analogModulates Quorum Sensing In Streptococcus PneumoniaeAliquots (100 μL) were taken at 0, 0.5, 1, 2, 3, 4, 5, 6, and 24 h time points1 mM4Trypsin RP-HPLCPBS solutionIn VitroNoneNoneIC50(nM) = 36 for CSP1-E1A/F7Cha against ComD1 receptor
4641
353594942022
AMRLSK-Cha-FRDFILQRKK
CSP1-E1A/F7Cha17FreeFreeLinearLintroduction of Cha = cyclohexylalanine residues at position 7CSP1 analogModulates Quorum Sensing In Streptococcus PneumoniaeAliquots (100 μL) were taken at 0, 0.5, 1, 2, 3, 4, 5, 6, and 24 h time points1 mM4ChymotrypsinRP-HPLCPBS solutionIn VitroNoneNoneIC50(nM) = 36 for CSP1-E1A/F7Cha against ComD1 receptor
4642
353594942022
EMRLSK-Cha-FRDF-Cha-LQRKK
CSP1-F7Cha/I12Cha17FreeFreeLinearLintroduction of Cha residues at positions 7 and 12CSP1 analogModulates Quorum Sensing In Streptococcus PneumoniaeAliquots (100 μL) were taken at 0, 0.5, 1, 2, 3, 4, 5, 6, and 24 h time points1 mM3Trypsin RP-HPLCPBS solutionIn VitroNoneNoneEC50(nM) = 0.97 for CSP1-F7Cha/I12Cha against ComD1 receptor, EC50(nM) = 70 for CSP1-F7Cha/I12Cha against ComD2 receptor
4643
353594942022
EMRLSK-Cha-FRDF-Cha-LQRKK
CSP1-F7Cha/I12Cha17FreeFreeLinearLintroduction of Cha residues at positions 7 and 12CSP1 analogModulates Quorum Sensing In Streptococcus PneumoniaeAliquots (100 μL) were taken at 0, 0.5, 1, 2, 3, 4, 5, 6, and 24 h time points1 mM6ChymotrypsinRP-HPLCPBS solutionIn VitroNoneNoneEC50(nM) = 0.97 for CSP1-F7Cha/I12Cha against ComD1 receptor, EC50(nM) = 70 for CSP1-F7Cha/I12Cha against ComD2 receptor
4644
351806462022
YPSKPDNPGEDAPAEDMARYYSALRHYINLITRQRY
NPY1–3636FreeAmidationLinearLNoneHuman derivedVasoconstrictor168 min for a study dayN.A.4.66 ± 0.70Human plasma proteaseLC-MS/MSHuman plasma after Heavy exerciseIn VivoPDB id: 7RTANoneN.A.
4645
351806462022
YPSKPDNPGEDAPAEDMARYYSALRHYINLITRQRY
NPY1–3636FreeAmidationLinearLNoneHuman derivedVasoconstrictor168 min for a study dayN.A.4.78 ± 1.07Human plasma proteaseLC-MS/MSHuman plasma with 5 mg saxagliptin after Heavy exerciseIn VivoPDB id: 7RTANoneN.A.
4646
351806462022
SKPDNPGEDAPAEDMARYYSALRHYINLITRQRY
NPY3–3634FreeAmidationLinearLNoneHuman derivedVasoconstrictor168 min for a study dayN.A.26.9 ± 6.2Human plasma proteaseLC-MS/MSHuman plasma after Heavy exerciseIn VivoPDB id: 7RTANoneN.A.
4647
351806462022
SKPDNPGEDAPAEDMARYYSALRHYINLITRQRY
NPY3–3634FreeAmidationLinearLNoneHuman derivedVasoconstrictor168 min for a study dayN.A.25.5 ± 6.2 Human plasma proteaseLC-MS/MSHuman plasma with 5 mg saxagliptin after Heavy exerciseIn VivoPDB id: 7RTANoneN.A.
4648
351746982022
MVSKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTLVTTLTYGVQCFSRYPDHMKQHDFFKSAMPEGYVQERTIFFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNYNSHNVYIMADKQKNGIKVNFKIRHNIEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSALSKDPNEKRDHMVLLEFVTAAGITLGMDELYK
eGFP239FreeFreeLinearLNoneEnhanced GFPTaggingN.A.N.A.565E. Coli Bl21(De3) cells lysate proteaseFluorescence assayE. coli BL21(DE3) cells lysate after 5 h removed the inducerIn VivoPDB id: 4EULNoneN.A.
4649
351746982022
MVSKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTLVTTLTYGVQCFSRYPDHMKQHDFFKSAMPEGYVQERTIFFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNYNSHNVYIMADKQKNGIKVNFKIRHNIEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSALSKDPNEKRDHMVLLEFVTAAGITLGMDELYK-AANDENYALAA
GFP-Ec250GFPEc (E.coli) SsrA tag sequences conjugationLinearLNoneeGFP derivativeIncreases Half LifeN.A.N.A.6E. Coli Bl21(De3) cells lysate proteaseFluorescence assayE. coli BL21(DE3) cells lysate after 5 h removed the inducerIn VivoPDB id: 4EULNoneN.A.
4650
351746982022
MVSKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTLVTTLTYGVQCFSRYPDHMKQHDFFKSAMPEGYVQERTIFFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNYNSHNVYIMADKQKNGIKVNFKIRHNIEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSALSKDPNEKRDHMVLLEFVTAAGITLGMDELYK-AANKNEENTNEVPTFMLNAGQANYAFA
GFP-Mf266GFPMf (M.fluorum) SsrA tag sequencesLinearLNoneeGFP derivativeIncreases Half LifeN.A.N.A.56E. Coli Bl21(De3) cells lysate proteaseFluorescence assayE. coli BL21(DE3) cells lysate after 5 h removed the inducerIn VivoPDB id: 4EULNoneN.A.
4651
351746982022
MVSKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTLVTTLTYGVQCFSRYPDHMKQHDFFKSAMPEGYVQERTIFFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNYNSHNVYIMADKQKNGIKVNFKIRHNIEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSALSKDPNEKRDHMVLLEFVTAAGITLGMDELYK
eGFP239FreeFreeLinearLNoneEnhanced GFPTaggingN.A.N.A.No DegradationE. Coli Bl21(De3) star strain lysate proteaseFluorescence assayE. coli BL21 (DE3) star strain lysate in which RNase E has been knocked out In VivoPDB id: 4EULNoneN.A.
4652
351746982022
MVSKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTLVTTLTYGVQCFSRYPDHMKQHDFFKSAMPEGYVQERTIFFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNYNSHNVYIMADKQKNGIKVNFKIRHNIEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSALSKDPNEKRDHMVLLEFVTAAGITLGMDELYK-AANDENYALAA
GFP-Ec250GFPEc (E.coli) SsrA tag sequencesLinearLNoneeGFP derivativeIncreases Half LifeN.A.N.A.14E. Coli Bl21(De3) star strain lysate proteaseFluorescence assayE. coli BL21 (DE3) star strain lysate in which RNase E has been knocked out In VivoPDB id: 4EULNoneN.A.
4653
351746982022
MVSKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTLVTTLTYGVQCFSRYPDHMKQHDFFKSAMPEGYVQERTIFFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNYNSHNVYIMADKQKNGIKVNFKIRHNIEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSALSKDPNEKRDHMVLLEFVTAAGITLGMDELYK-AANKNEENTNEVPTFMLNAGQANYAFA
GFP-Mf266GFPMf (M.fluorum) SsrA tag sequencesLinearLNoneeGFP derivativeIncreases Half LifeN.A.N.A.424E. Coli Bl21(De3) star strain lysate proteaseFluorescence assayE. coli BL21 (DE3) star strain lysate in which RNase E has been knocked out In VivoPDB id: 4EULNoneN.A.
4654
351508052022
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
Exenatide39FreeAmidationLinearLNoneGLP-1 analogsAntidiabetesBlood sampling was performed at 0.083, 0.5, 4, 24, 48 and 72 h after injection1200 nmol/kg0.137 (Terminal Half Life)Male CDR1 mice plasma proteaseELISAMale CDR1 mice plasmaIn VivoPDB id: 7MLLNoneEC50 = 0.42nM ( in the classical in vitro GLP1R cell based assay based on cAMP)
4655
351508052022
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPSIEGR
Exenatide-4aa-ABNF43FreeAlbumin binding Nanofitins (ABNF) linked at C terminus by 4 aaLinearLNoneGLP-1 analogsAntidiabetesBlood sampling was performed at 0.083, 0.5, 4, 24, 48 and 72 h after injection400 nmol/kg19.6 (Terminal Half Life)Male CDR1 mice plasma proteaseELISAMale CDR1 mice plasmaIn VivoPDB id: 7MLLNoneEC50 = 1.387 nM ( in the classical in vitro GLP1R cell based assay based on cAMP)
4656
351508052022
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPSASTKGPS
Exenatide-7aa'-ABNF46FreeAlbumin binding Nanofitins (ABNF) linked at C terminus by 7 aaLinearLNoneGLP-1 analogsAntidiabetesBlood sampling was performed at 0.083, 0.5, 4, 24, 48 and 72 h after injection400 nmol/kg20.8 (Terminal Half Life)Male CDR1 mice plasma proteaseELISAMale CDR1 mice plasmaIn VivoPDB id: 7MLLNoneEC50 = 0.5785 nM ( in the classical in vitro GLP1R cell based assay based on cAMP)
4657
351508052022
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPSGGGGSGG
Exenatide-7aa-ABNF46FreeAlbumin binding Nanofitins (ABNF) linked at C terminus by 7 aaLinearLNoneGLP-1 analogsAntidiabetesBlood sampling was performed at 0.083, 0.5, 4, 24, 48 and 72 h after injection400 nmol/kg19.3 (Terminal Half Life)Male CDR1 mice plasma proteaseELISAMale CDR1 mice plasmaIn VivoPDB id: 7MLLNoneEC50 = 0.7459 nM ( in the classical in vitro GLP1R cell based assay based on cAMP)
4658
351508052022
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS(GGGGS)2GG
Exenatide-12aa-ABNF51FreeAlbumin binding Nanofitins (ABNF) linked at C terminus by 12 aaLinearLNoneGLP-1 analogsAntidiabetesBlood sampling was performed at 0.083, 0.5, 4, 24, 48 and 72 h after injection400 nmol/kg21.9 (Terminal Half Life)Male CDR1 mice plasma proteaseELISAMale CDR1 mice plasmaIn VivoPDB id: 7MLLNoneEC50 = 0.8065 nM ( in the classical in vitro GLP1R cell based assay based on cAMP)
4659
351508052022
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPSGGS(GGGGS)4GG
Exenatide-25aa-ABNF64FreeAlbumin binding Nanofitins (ABNF) linked at C terminus by 25 aaLinearLNoneGLP-1 analogsAntidiabetesBlood sampling was performed at 0.083, 0.5, 4, 24, 48 and 72 h after injection370 nmol/kg18.7 (Terminal Half Life)Male CDR1 mice plasma proteaseELISAMale CDR1 mice plasmaIn VivoPDB id: 7MLLNoneEC50 = 0.4903 nM ( in the classical in vitro GLP1R cell based assay based on cAMP)
4660
351508052022
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPSHGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPSIEGR
Exenatide-Exenatide-4aa-ABNF82FreeAlbumin binding Nanofitins (ABNF) linked at C terminus by 4 aaLinearLNoneGLP-1 analogsAntidiabetesBlood sampling was performed at 0.083, 0.5, 4, 24, 48 and 72 h after injection300 nmol/kg20.5 (Terminal Half Life)Male CDR1 mice plasma proteaseELISAMale CDR1 mice plasmaIn VivoPDB id: 7MLLNoneEC50 = 0.3708 nM ( in the classical in vitro GLP1R cell based assay based on cAMP)
4661
351135752022
ETVTLLVALKVRYRERIT-Ahx-CKRGARSTC
TT1-IP peptide27FreeAmidationCyclic (C-C Disulfide Bond)LConjugation of TT1 and IP proteins which is linked by AhxTT1 and IP fusion proteinAntitumor (Effect on TPP-IPs on Cll xenograft models)periods of time (0, 1, 6, and 24 h)5 mg/kg40% of the peptide was recovered after 6 hours incubationHuman serum proteaseMS using MALDI-TOFHuman serumIn VitroNoneNoneThe average survival for TT1-IP and LinTT1-IP treated groups was 19 days (the survival range for TT1-IP group was 17-23 days and for LinTT1-IP group was 13-25 days) and for the control group 16 days (range of 14-20 days)
4662
351135752022
ETVTLLVALKVRYRERIT-Ahx-CKRGARSTC
TT1-IP peptide27FreeAmidationCyclic (C-C Disulfide Bond)LConjugation of TT1 and IP proteins which is linked by AhxTT1 and IP fusion proteinAntitumor (Effect on TPP-IPs on Cll xenograft models)plasma collected at 10, 20, 30, 45, 60, 120 and 360 min5 mg/kg28 (Terminal Half Life)BALB/c mice plasma proteaseHPLC-MSBalb/c mice plasmaIn VivoNoneNoneThe average survival for TT1-IP and LinTT1-IP treated groups was 19 days (the survival range for TT1-IP group was 17-23 days and for LinTT1-IP group was 13-25 days) and for the control group 16 days (range of 14-20 days)
4663
350534172022
WRWRWRWRWRWRWRWRWK-βA
(WR)8WK(Glutaryl-Dox)βA]19FreeβAlanine at C terminal conjugationCyclicLAn ester bond is utilized to attach Dox with a glutaryl linkerSyntheticTreat Breast, Leukemia, and Lymphoma Malignancies4 h at 37 °C5 µM∼6 Human Serum ProteaseHPLC25% Human serumIn VitroNoneNoneAt 10 μM: 65% reduction in cell viability after 72 hours for SK-OV-3 Cells (antiproliferative activity values for the [(WR)8WKβA]-Dox conjugate ), At 10 μM: 19% cell viability after 72 hours for MDA-MB-231 Cells (antiproliferative activity values for the [(WR)8WKβA]-Dox conjugate ), At 10 μM: 77% reduction in cell viability after 72 hours for MCF-7 Cells (antiproliferative activity values for the [(WR)8WKβA]-Dox conjugate ), At 10 μM: 64% reduction in cell viability after 24 hours for MES-SA/MX2 Cells (DOX-resistant) Cells (antiproliferative activity values for the [(WR)8WKβA]-Dox conjugate ) 
4664
350460192022
MSKGPG-(VPGGGVPGAGVPGYG)10-PGGGG-SKGEELFTGVVPILVELDGDVNGHKFSVRGEGEGDATNGKLTLKFICTTGKLPVPWPTLVTTLTYGVQCFSRYPDHMKRHDFFKSAMPEGYVQERTISFKDDGTYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNFNSHNVYITADKQKNGIKANFKIRHNVEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSVLSKDPNEKRDHMVLLEFVTAAGITHGMDELYKGS
ELP(0FA)GFP400FreeGFPLinearLNoneELP-GFP conjugateIncreases Half Life1 week10 μM1.6C57Bl/6J mice blood plasma proteaseGFP-specific ELISAC57BL/6J mice blood plasmaIn VivoNoneNoneKD MSA - Mouse serum albumin (μM) = n.d. (Binding affinity of ELP-GFP constructs for serum albumin), KD HSA - Human serum albumin (μM) = n.d
4665
350460192022
MSKGPG-(VPGGGVPGAGVPG(pAzF-FA)G)1(VPGGGVPGAGVPGYG)9-PGGGG-SKGEELFTGVVPILVELDGDVNGHKFSVRGEGEGDATNGKLTLKFICTTGKLPVPWPTLVTTLTYGVQCFSRYPDHMKRHDFFKSAMPEGYVQERTISFKDDGTYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNFNSHNVYITADKQKNGIKANFKIRHNVEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSVLSKDPNEKRDHMVLLEFVTAAGITHGMDELYKGS
ELP(1FA)GFP400FreeGFPLinearL1 Fatty acid conjugation through pAzF (para-azidophenylalanine)ELP-GFP conjugateIncreases Half Life1 week10 μM1.9C57Bl/6J mice blood plasma proteaseGFP-specific ELISAC57BL/6J mice blood plasmaIn VivoNoneNoneKD MSA (μM) = 126 ± 32.2, KD HSA - Human serum albumin (μM) = n.d
4666
350460192022
MSKGPG-(VPGGGVPGAGVPG(pAzF-FA)GVPGGGVPGAGVPGYG)5-PGGGG-SKGEELFTGVVPILVELDGDVNGHKFSVRGEGEGDATNGKLTLKFICTTGKLPVPWPTLVTTLTYGVQCFSRYPDHMKRHDFFKSAMPEGYVQERTISFKDDGTYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNFNSHNVYITADKQKNGIKANFKIRHNVEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSVLSKDPNEKRDHMVLLEFVTAAGITHGMDELYKGS
ELP(5FA)GFP400FreeGFPLinearL5 Fatty acid conjugation through pAzF (para-azidophenylalanine)ELP-GFP conjugateIncreases Half Life1 week10 μM19.6C57Bl/6J mice blood plasma proteaseGFP-specific ELISAC57BL/6J mice blood plasmaIn VivoNoneNoneKD MSA (μM) = 10.3 ± 4.0, KD HSA - Human serum albumin (μM) = n.d
4667
350460192022
MSKGPG-(VPGGGVPGAGVPG(pAzF)G)10-PGGGG–SKGEELFTGVVPILVELDGDVNGHKFSVRGEGEGDATNGKLTLKFICTTGKLPVPWPTLVTTLTYGVQCFSRYPDHMKRHDFFKSAMPEGYVQERTISFKDDGTYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNFNSHNVYITADKQKNGIKANFKIRHNVEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSVLSKDPNEKRDHMVLLEFVTAAGITHGMDELYKGS
ELP(10FA)GFP400FreeGFPLinearL10 Fatty acid conjugation through pAzF (para-azidophenylalanine)ELP-GFP conjugateIncreases Half Life1 week10 μM33.3C57Bl/6J mice blood plasma proteaseGFP-specific ELISAC57BL/6J mice blood plasmaIn VivoNoneNoneKD MSA (μM) =2.76 ± 0.19, KD HSA - Human serum albumin (μM) = n.d
4668
350460192022
MSKGPG-(VPGGGVPGAGVPG(pAzF-FA)G)1(VPGGGVPGAGVPGYG)9-PGGGG-SKGEELFTGVVPILVELDGDVNGHKFSVRGEGEGDATNGKLTLKFICTTGKLPVPWPTLVTTLTYGVQCFSRYPDHMKRHDFFKSAMPEGYVQERTISFKDDGTYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNFNSHNVYITADKQKNGIKANFKIRHNVEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSVLSKDPNEKRDHMVLLEFVTAAGITHGMDELYKGS
ELP(1FA)GFP400FreeGFPLinearL1 Fatty acid conjugation through pAzF (para-azidophenylalanine)ELP-GFP conjugateIncreases Half Life1 week10 μM18.5C57Bl/6J mice blood plasma proteaseGFP-specific ELISAC57BL/6J mice blood plasmaIn VivoNoneNoneKD MSA (μM) =25.9 ± 7.1, KD HSA - Human serum albumin (μM) = 19.3 ± 3.9
4669
350460192022
MSKGPG-(VPGGGVPGAGVPG(pAzF-FA)GVPGGGVPGAGVPGYG)5-PGGGG-SKGEELFTGVVPILVELDGDVNGHKFSVRGEGEGDATNGKLTLKFICTTGKLPVPWPTLVTTLTYGVQCFSRYPDHMKRHDFFKSAMPEGYVQERTISFKDDGTYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNFNSHNVYITADKQKNGIKANFKIRHNVEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSVLSKDPNEKRDHMVLLEFVTAAGITHGMDELYKGS
ELP(5FA)GFP400FreeGFPLinearL5 Fatty acid conjugation through pAzF (para-azidophenylalanine)ELP-GFP conjugateIncreases Half Life1 week10 μM31.7C57Bl/6J mice blood plasma proteaseGFP-specific ELISAC57BL/6J mice blood plasmaIn VivoNoneNoneKD MSA (μM) =4.0 ± 1.6, KD HSA - Human serum albumin (μM) = 3.16 ± 0.60
4670
350460192022
MSKGPG-(VPGGGVPGAGVPG(pAzF)G)10-PGGGG–SKGEELFTGVVPILVELDGDVNGHKFSVRGEGEGDATNGKLTLKFICTTGKLPVPWPTLVTTLTYGVQCFSRYPDHMKRHDFFKSAMPEGYVQERTISFKDDGTYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNFNSHNVYITADKQKNGIKANFKIRHNVEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSVLSKDPNEKRDHMVLLEFVTAAGITHGMDELYKGS
ELP(10FA)GFP400FreeGFPLinearL10 Fatty acid conjugation through pAzF (para-azidophenylalanine)ELP-GFP conjugateIncreases Half Life1 week10 μM27.9C57Bl/6J mice blood plasma proteaseGFP-specific ELISAC57BL/6J mice blood plasmaIn VivoNoneNoneKD MSA (μM) = 2.22 ± 0.03, KD HSA - Human serum albumin (μM) = 1.64 ± 0.17
4671
349540522022
KEIVSRNKRRYQEDGRKKRRQRRR
SY-00724FreeFreeLinearLNoneNeuropeptideTreatment of Ischemic StrokeBlood samples were collected for determinationsof SY-007 at pre-dose (within 0.5 h prior to dosing) and at 5, 10, 15, 20,30, 45 min, and 1, 1.5, 2, 3, 4, 5, 6 h after the beginning of the intravenous infusion1 mg0.25 ± 0.02Human plasma protease LC-MSHuman plasmaIn VivoNoneNoneN.A.
4672
349540522022
KEIVSRNKRRYQEDGRKKRRQRRR
SY-00724FreeFreeLinearLNoneNeuropeptideTreatment of Ischemic StrokeBlood samples were collected for determinationsof SY-007 at pre-dose (within 0.5 h prior to dosing) and at 5, 10, 15, 20,30, 45 min, and 1, 1.5, 2, 3, 4, 5, 6 h after the beginning of the intravenous infusion4 mg0.36 ± 0.04Human plasma protease LC-MSHuman plasmaIn VivoNoneNoneN.A.
4673
349540522022
KEIVSRNKRRYQEDGRKKRRQRRR
SY-00724FreeFreeLinearLNoneNeuropeptideTreatment of Ischemic StrokeBlood samples were collected for determinationsof SY-007 at pre-dose (within 0.5 h prior to dosing) and at 5, 10, 15, 20,30, 45 min, and 1, 1.5, 2, 3, 4, 5, 6 h after the beginning of the intravenous infusion10 mg0.45 ± 0.05Human plasma protease LC-MSHuman plasmaIn VivoNoneNoneN.A.
4674
349540522022
KEIVSRNKRRYQEDGRKKRRQRRR
SY-00724FreeFreeLinearLNoneNeuropeptideTreatment of Ischemic StrokeBlood samples were collected for determinationsof SY-007 at pre-dose (within 0.5 h prior to dosing) and at 5, 10, 15, 20,30, 45 min, and 1, 1.5, 2, 3, 4, 5, 6 h after the beginning of the intravenous infusion20 mg0.55 ± 0.07 Human plasma protease LC-MSHuman plasmaIn VivoNoneNoneN.A.
4675
349540522022
KEIVSRNKRRYQEDGRKKRRQRRR
SY-00724FreeFreeLinearLNoneNeuropeptideTreatment Of Ischemic Strokeblood samples were collected for determinationsof SY-007 at pre-dose (within 0.5 h prior to dosing) and at 5, 10, 15, 20,30, 45 min, and 1, 1.5, 2, 3, 4, 5, 6 h after the beginning of the intravenous infusion30 mg0.70 ± 0.08Human plasma protease LC-MSHuman plasmaIn VivoNoneNoneN.A.
4676
349540522022
KEIVSRNKRRYQEDGRKKRRQRRR
SY-00724FreeFreeLinearLNoneNeuropeptideTreatment Of Ischemic Strokeblood samples were collected for determinationsof SY-007 at pre-dose (within 0.5 h prior to dosing) and at 5, 10, 15, 20,30, 45 min, and 1, 1.5, 2, 3, 4, 5, 6 h after the beginning of the intravenous infusion45 mg0.73 ± 0.05Human plasma protease LC-MSHuman plasmaIn VivoNoneNoneN.A.
4677
349540522022
KEIVSRNKRRYQEDGRKKRRQRRR
SY-00724FreeFreeLinearLNoneNeuropeptideTreatment Of Ischemic Strokeblood samples were collected for determinationsof SY-007 at pre-dose (within 0.5 h prior to dosing) and at 5, 10, 15, 20,30, 45 min, and 1, 1.5, 2, 3, 4, 5, 6 h after the beginning of the intravenous infusion60 mg0.78 ± 0.06Human plasma protease LC-MSHuman plasmaIn VivoNoneNoneN.A.
4678
349104922022
SETSKSF
68Ga-DOTA-SETSKSF768Ga labelledFreeCyclicLNoneSyntheticUsed For Positron Emission Tomography imaging of PD-L1 expression in tumorsN.A.N.A.14.48 ± 3.26N.A.N.A.N.A.N.A.NoneNoneN.A.
4679
349104922022
SETSKSF
68Ga-DOTA-SETSKSF768Ga labelledFreeCyclicLNoneSyntheticUsed For Positron Emission Tomography imaging of PD-L1 expression in tumorsN.A.5.29 ± 0.21 (%ID/g)N.A.N.A.N.A.H1975 tumor modelIn VitroNoneNoneN.A.
4680
349104922022
SETSKSF
68Ga-DOTA-SETSKSF768Ga labelledFreeCyclicLNoneSyntheticUsed For Positron Emission Tomography imaging of PD-L1 expression in tumorsN.A.0.89 ± 0.10 (%ID/g)N.A.N.A.N.A.A549 tumor modelIn VitroNoneNoneN.A.
4681
348077602022
RRWVRRVRRVWRRVVRVVRRWVRR
PLG020624FreeFreeLinearLNoneSyntheticAntimicrobialBlood samples for PK assessment were collected at predose, at the midpoint of infusion, within 1 min of the end of infusion, and at 0.5, 1, 2, 4, 6, 8, 12, 20, 24, 36, and 48 h after the end of infusion0.05 mg/kg7.37 (Median Terminal Half Life)Human plasma protease HPLC-MSHuman plasmaIn VivoPubchem CID : 16152467NoneN.A.
4682
348077602022
RRWVRRVRRVWRRVVRVVRRWVRR
PLG020624FreeFreeLinearLNoneSyntheticAntimicrobialBlood samples for PK assessment were collected at predose, at the midpoint of infusion, within 1 min of the end of infusion, and at 0.5, 1, 2, 4, 6, 8, 12, 20, 24, 36, and 48 h after the end of infusion0.125 mg/kg10.5 (Median Terminal Half Life)Human plasma protease HPLC-MSHuman plasmaIn VivoPubchem CID : 16152467NoneN.A.
4683
348077602022
RRWVRRVRRVWRRVVRVVRRWVRR
PLG020624FreeFreeLinearLNoneSyntheticAntimicrobialBlood samples for PK assessment were collected at predose, at the midpoint of infusion, within 1 min of the end of infusion, and at 0.5, 1, 2, 4, 6, 8, 12, 20, 24, 36, and 48 h after the end of infusion0.25 mg/kg19.94 (Median Terminal Half Life)Human plasma protease HPLC-MSHuman plasmaIn VivoPubchem CID : 16152467NoneN.A.
4684
348077602022
RRWVRRVRRVWRRVVRVVRRWVRR
PLG020624FreeFreeLinearLNoneSyntheticAntimicrobialBlood samples for PK assessment were collected at predose, at the midpoint of infusion, within 1 min of the end of infusion, and at 0.5, 1, 2, 4, 6, 8, 12, 20, 24, 36, and 48 h after the end of infusion0.25 mg/kg13.16 (Median Terminal Half Life)Human plasma protease HPLC-MSHuman plasmaIn VivoPubchem CID : 16152467NoneN.A.
4685
348077602022
RRWVRRVRRVWRRVVRVVRRWVRR
PLG020624FreeFreeLinearLNoneSyntheticAntimicrobialBlood samples for PK assessment were collected at predose, at the midpoint of infusion, within 1 min of the end of infusion, and at 0.5, 1, 2, 4, 6, 8, 12, 20, 24, 36, and 48 h after the end of infusion0.5 mg/kg16.2 (Median Terminal Half Life)Human plasma protease HPLC-MSHuman plasmaIn VivoPubchem CID : 16152467NoneN.A.
4686
348077602022
RRWVRRVRRVWRRVVRVVRRWVRR
PLG020624FreeFreeLinearLNoneSyntheticAntimicrobialBlood samples for PK assessment were collected at predose, at the midpoint of infusion, within 1 min of the end of infusion, and at 0.5, 1, 2, 4, 6, 8, 12, 20, 24, 36, and 48 h after the end of infusion1 mg/kg 19.97 (Median Terminal Half Life)Human plasma protease HPLC-MSHuman plasmaIn VivoPubchem CID : 16152467NoneN.A.
4687
344310712022
PGQEHPNARKYKGANKKGLSKGCFGLKLDRIGSMSGLGC
vosoritide39FreeFreeCyclic (Cysteine (23->39)-Disulfide)LNoneAnalog of C-type natriuretic peptideTreatment of AchondroplasiaIn a phase II study, full PK sampling was performed at days 1, 10, 29, 85 and 183, during which plasma samples were collected predose and at 5 (± 2 min), 15 (± 2 min), 30 (± 5 min), 60 (± 5 min), 90 (± 5 min), 120 (± 5 min) and 180 (± 5 min) min postdose2.5 µg/kg N.A.Human plasma protease ELISAHuman plasmaIn Vivohttps://pubchem.ncbi.nlm.nih.gov/compound/119058036#section=2D-StructureNoneN.A.
4688
344310712022
PGQEHPNARKYKGANKKGLSKGCFGLKLDRIGSMSGLGC
vosoritide39FreeFreeCyclic (Cysteine (23->39)-Disulfide)LNoneAnalog of C-type natriuretic peptideTreatment of AchondroplasiaIn a phase II study, full PK sampling was performed at days 1, 10, 29, 85 and 183, during which plasma samples were collected predose and at 5 (± 2 min), 15 (± 2 min), 30 (± 5 min), 60 (± 5 min), 90 (± 5 min), 120 (± 5 min) and 180 (± 5 min) min postdose7.5 µg/kg N.A.Human plasma protease ELISAHuman plasmaIn Vivohttps://pubchem.ncbi.nlm.nih.gov/compound/119058036#section=2D-StructureNoneN.A.
4689
344310712022
PGQEHPNARKYKGANKKGLSKGCFGLKLDRIGSMSGLGC
vosoritide39FreeFreeCyclic (Cysteine (23->39)-Disulfide)LNoneAnalog of C-type natriuretic peptideTreatment of AchondroplasiaIn a phase II study, full PK sampling was performed at days 1, 10, 29, 85 and 183, during which plasma samples were collected predose and at 5 (± 2 min), 15 (± 2 min), 30 (± 5 min), 60 (± 5 min), 90 (± 5 min), 120 (± 5 min) and 180 (± 5 min) min postdose15 µg/kg 24.4Human plasma protease ELISAHuman plasmaIn Vivohttps://pubchem.ncbi.nlm.nih.gov/compound/119058036#section=2D-StructureNoneN.A.
4690
344310712022
PGQEHPNARKYKGANKKGLSKGCFGLKLDRIGSMSGLGC
vosoritide39FreeFreeCyclic (Cysteine (23->39)-Disulfide)LNoneAnalog of C-type natriuretic peptideTreatment of AchondroplasiaIn a phase II study, full PK sampling was performed at days 1, 10, 29, 85 and 183, during which plasma samples were collected predose and at 5 (± 2 min), 15 (± 2 min), 30 (± 5 min), 60 (± 5 min), 90 (± 5 min), 120 (± 5 min) and 180 (± 5 min) min postdose30 µg/kg 27Human plasma protease ELISAHuman plasmaIn Vivohttps://pubchem.ncbi.nlm.nih.gov/compound/119058036#section=2D-StructureNoneN.A.
4691
344310712022
PGQEHPNARKYKGANKKGLSKGCFGLKLDRIGSMSGLGC
vosoritide39FreeFreeCyclic (Cysteine (23->39)-Disulfide)LNoneAnalog of C-type natriuretic peptideTreatment of AchondroplasiaIn the phase III study, full PK sampling was performed at day 1 during which plasma samples were collected predose and at 5 (± 2 min), 15 (± 2 min), 30 (± 5 min), 45 (± 5 min), 60 (± 5 min), 90 (± 5 min) and 120 (± 5 min) min postdose15 µg/kg21Human plasma protease ELISAHuman plasmaIn Vivohttps://pubchem.ncbi.nlm.nih.gov/compound/119058036#section=2D-StructureNoneN.A.
4692
344310712022
PGQEHPNARKYKGANKKGLSKGCFGLKLDRIGSMSGLGC
vosoritide39FreeFreeCyclic (Cysteine (23->39)-Disulfide)LNoneAnalog of C-type natriuretic peptideTreatment of AchondroplasiaIn the phase III study, full PK sampling was performed at week 26 during which plasma samples were collected predose and at 5 (± 2 min), 15 (± 2 min), 30 (± 5 min), 45 (± 5 min), 60 (± 5 min), 90 (± 5 min) and 120 (± 5 min) min postdose15 µg/kg26.6Human plasma protease ELISAHuman plasmaIn Vivohttps://pubchem.ncbi.nlm.nih.gov/compound/119058036#section=2D-StructureNoneN.A.
4693
344310712022
PGQEHPNARKYKGANKKGLSKGCFGLKLDRIGSMSGLGC
vosoritide39FreeFreeCyclic (Cysteine (23->39)-Disulfide)LNoneAnalog of C-type natriuretic peptideTreatment of AchondroplasiaIn the phase III study, full PK sampling was performed at week 52, during which plasma samples were collected predose and at 5 (± 2 min), 15 (± 2 min), 30 (± 5 min), 45 (± 5 min), 60 (± 5 min), 90 (± 5 min) and 120 (± 5 min) min postdose15 µg/kg27.9Human plasma protease ELISAHuman plasmaIn Vivohttps://pubchem.ncbi.nlm.nih.gov/compound/119058036#section=2D-StructureNoneN.A.
4694
342177752022
VTHRLAGLLSRSGGVVKNNFVPTNVGSKAF
FE 99232630FreeAmidationLinearLNoneDerived from CGRPTreatment of Acute Episodic MigraineBlood sample was collected at 2, 6, 10, 15, 20, 30, 45, 60, 90, 120 min0.3 mg/kg6.5 ± 1.8Male SD rats plasma proteaseLC-MS/MSMale SD rats plasmaIn VivoNoneNoneRat (%Plasma Protein Binding) = 9 ± 3, Human(%Plasma Protein Binding) = 17 ± 2 for FE 205030
4695
342177752022
vYC-Agp-DVGPFC-3Pal
FE 99232510D-val at position 1Amidation, 3-Pal modification at C terminalCyclic (C3-C10 disulfide bond)MixAgpDerived from CGRPTreatment of Acute Episodic MigraineBlood sample was collected at 2, 6, 10, 15, 20, 30, 45, 60, 90, 120 min0.3 mg/kg21 ± 2Male SD rats plasma proteaseLC-MS/MSMale SD rats plasmaIn VivoNoneNoneRat (%Plasma Protein Binding) = 50 ± 5, Human(%Plasma Protein Binding) = 46 ± 4 for FE 992325
4696
342177752022
vFCODVGPFC-3Pal
FE 20503010Oxazole-2-carbonyl, D-val at position 1Amidation, 3-Pal modification at C terminalCyclic (C3-C10 disulfide bond)MixPhe linked with (2-Cbm),3Pal, Orn linked with iPrDerived from CGRPTreatment of Acute Episodic MigraineBlood sample was collected at 2, 6, 10, 15, 20, 40, 60, 90, 135, 180 min0.2 mg/kg25 ± 8Male SD rats plasma proteaseLC-MS/MSMale SD rats plasmaIn VivoNoneNoneRat (%Plasma Protein Binding) = 9 ± 3, Human(%Plasma Protein Binding) = 17 ± 2 for FE 205030
4697
342177752022
VTHRLAGLLSRSGGVVKNNFVPTNVGSKAF
FE 99232630FreeAmidationLinearLNoneDerived from CGRPTreatment of Acute Episodic MigraineBlood sample was collected at 5, 10, 20, 30, 45, 60, 90, 120, 180, 240, 300 min1 mg/kg11 ± 8.4Male SD rats plasma proteaseLC-MS/MSMale SD rats plasmaIn VivoNoneNoneRat (%Plasma Protein Binding) = 9 ± 3, Human(%Plasma Protein Binding) = 17 ± 2 for FE 205030
4698
342177752022
vYC-Agp-DVGPFC-3Pal
FE 99232510D-val at position 1Amidation, 3-Pal modification at C terminalCyclic (C3-C10 disulfide bond)MixAgpDerived from CGRPTreatment of Acute Episodic MigraineBlood sample was collected at 5, 10, 20, 30, 45, 60, 90, 120, 180, 240, 300 min1 mg/kg48 ± 11Male SD rats plasma proteaseLC-MS/MSMale SD rats plasmaIn VivoNoneNoneRat (%Plasma Protein Binding) = 50 ± 5, Human(%Plasma Protein Binding) = 46 ± 4 for FE 992325
4699
342177752022
vFCODVGPFC-3Pal
FE 20503010Oxazole-2-carbonyl, D-val at position 1AmidationCyclic (C3-C10 disulfide bond)MixPhe linked with (2-Cbm),3Pal, Orn linked with iPrDerived from CGRPTreatment of Acute Episodic MigraineBlood sample was collected at 5, 10, 20, 40, 60, 90, 120, 180, 240, 300 min0.6 mg/kg23 ± 2Male SD rats plasma proteaseLC-MS/MSMale SD rats plasmaIn VivoNoneNoneRat (%Plasma Protein Binding) = 9 ± 3, Human(%Plasma Protein Binding) = 17 ± 2 for FE 205030
4700
342177752022
vFCODVGPFC-3Pal
FE 20503010Oxazole-2-carbonyl, D-val at position 1AmidationCyclic (C3-C10 disulfide bond)MixPhe linked with (2-Cbm),3Pal, Orn linked with iPrDerived from CGRPTreatment of Acute Episodic MigraineBlood sample was collected at 2, 6, 10, 15, 20, 40, 60, 90, 135, 180 min0.1 mg/kg82 ± 9Male göttingen minipigs plasma proteaseLC-MS/MSMale göttingen minipigs plasma In VivoNoneNoneRat (%Plasma Protein Binding) = 9 ± 3, Human(%Plasma Protein Binding) = 17 ± 2 for FE 205030
4701
342177752022
vFCODVGPFC-3Pal
FE 20503010Oxazole-2-carbonyl, D-val at position 1Amidation, 3-Pal modification at C terminalCyclic (C3-C10 disulfide bond)MixPhe linked with (2-Cbm),3Pal, Orn linked with iPrDerived from CGRPTreatment of Acute Episodic MigraineBlood sample was collected at 5, 10, 20, 40, 60, 90, 120, 180, 240, 300 min0.25 mg/kg264 ± 80Male göttingen minipigs plasma proteaseLC-MS/MSMale göttingen minipigs plasma In VivoNoneNoneRat (%Plasma Protein Binding) = 9 ± 3, Human(%Plasma Protein Binding) = 17 ± 2 for FE 205030
4702
342177752022
vYC-Agp-DVGPFC-3Pal
FE 99232510D-val at position 1Amidation, 3-Pal modification at C terminalCyclic (C3-C10 disulfide bond)MixAgpDerived from CGRPTreatment of Acute Episodic MigraineBlood sample was collected at 2, 6, 10, 15, 20, 30, 45, 60, 90, 120 min0.2 mg/kg69 ± 7Male cynomolgus monkeys plasma proteaseLC-MS/MSMale cynomolgus monkeys plasma In VivoNoneNoneRat (%Plasma Protein Binding) = 50 ± 5, Human(%Plasma Protein Binding) = 46 ± 4 for FE 992325
4703
342177752022
vFCODVGPFC-3Pal
FE 20503010Oxazole-2-carbonyl, D-val at position 1Amidation, 3-Pal modification at C terminalCyclic (C3-C10 disulfide bond)MixPhe linked with (2-Cbm),3Pal, Orn linked with iPrDerived from CGRPTreatment of Acute Episodic MigraineBlood sample was collected at 2, 6, 10, 15, 20, 40, 60, 90, 135, 180 min0.1 mg/kg65 ± 5Male cynomolgus monkeys plasma proteaseLC-MS/MSMale cynomolgus monkeys plasma In VivoNoneNoneRat (%Plasma Protein Binding) = 9 ± 3, Human(%Plasma Protein Binding) = 17 ± 2 for FE 205030
4704
365887172022
GEPPPPGKPADDAGLV
BPC15715FreeFreeLinearLNoneIsolated from human gastric juiceTherapeutic Agent For Severe Trauma And Stress Damage And Can Promote The Healing Of Wounds, Ligament Injuries, Tendon Injuries, And FracturesBlood samples were collected from rats in groups one to four at the corresponding time points before (0 h) and within 6 h after BPC157 administration. Blood samples were collected from rats in group five before the last three doses and within 6 h after the last dose100 μg/kg18.5Rats plasma proteaseLC-MS/MSRats plasmaIn VivoNoneNoneN.A.
4705
365887172022
GEPPPPGKPADDAGLV
BPC15715FreeFreeLinearLNoneIsolated from human gastric juiceTherapeutic Agent For Severe Trauma And Stress Damage And Can Promote The Healing Of Wounds, Ligament Injuries, Tendon Injuries, And FracturesBlood samples were collected from rats in groups one to four at the corresponding time points before (0 h) and within 6 h after BPC157 administration. Blood samples were collected from rats in group five before the last three doses and within 6 h after the last dose20 μg/kg7.87Rats plasma proteaseLC-MS/MSRats plasmaIn VivoNoneNoneN.A.
4706
365887172022
GEPPPPGKPADDAGLV
BPC15715FreeFreeLinearLNoneIsolated from human gastric juiceTherapeutic Agent For Severe Trauma And Stress Damage And Can Promote The Healing Of Wounds, Ligament Injuries, Tendon Injuries, And FracturesBlood samples were collected from rats in groups one to four at the corresponding time points before (0 h) and within 6 h after BPC157 administration. Blood samples were collected from rats in group five before the last three doses and within 6 h after the last dose100 μg/kg17.1Rats plasma proteaseLC-MS/MSRats plasmaIn VivoNoneNoneN.A.
4707
365887172022
GEPPPPGKPADDAGLV
BPC15715FreeFreeLinearLNoneIsolated from human gastric juiceTherapeutic Agent For Severe Trauma And Stress Damage And Can Promote The Healing Of Wounds, Ligament Injuries, Tendon Injuries, And FracturesBlood samples were collected from rats in groups one to four at the corresponding time points before (0 h) and within 6 h after BPC157 administration. Blood samples were collected from rats in group five before the last three doses and within 6 h after the last dose500 μg/kg29.7Rats plasma proteaseLC-MS/MSRats plasmaIn VivoNoneNoneN.A.
4708
365887172022
GEPPPPGKPADDAGLV
BPC15715FreeFreeLinearLNoneIsolated from human gastric juiceTherapeutic Agent For Severe Trauma And Stress Damage And Can Promote The Healing Of Wounds, Ligament Injuries, Tendon Injuries, And FracturesBlood samples were collected at the corresponding time points before (0 h) and within 6 h of a single administration. Blood samples were collected from dogs administered multiple doses at corresponding time points before the first dosing (0 h), within 6 h after dosing, before the last three doses, and at corresponding time points after the last dosing6 μg/kg5.27 ± 2.25Beagle dogs plasma proteaseLC-MS/MSBeagle dogs plasmaIn VivoNoneNoneN.A.
4709
365887172022
GEPPPPGKPADDAGLV
BPC15715FreeFreeLinearLNoneIsolated from human gastric juiceTherapeutic Agent For Severe Trauma And Stress Damage And Can Promote The Healing Of Wounds, Ligament Injuries, Tendon Injuries, And FracturesBlood samples were collected at the corresponding time points before (0 h) and within 6 h of a single administration. Blood samples were collected from dogs administered multiple doses at corresponding time points before the first dosing (0 h), within 6 h after dosing, before the last three doses, and at corresponding time points after the last dosing30 μg/kg19.6 ± 3.72Beagle dogs plasma proteaseLC-MS/MSBeagle dogs plasmaIn VivoNoneNoneN.A.
4710
365887172022
GEPPPPGKPADDAGLV
BPC15715FreeFreeLinearLNoneIsolated from human gastric juiceTherapeutic Agent For Severe Trauma And Stress Damage And Can Promote The Healing Of Wounds, Ligament Injuries, Tendon Injuries, And FracturesBlood samples were collected at the corresponding time points before (0 h) and within 6 h of a single administration. Blood samples were collected from dogs administered multiple doses at corresponding time points before the first dosing (0 h), within 6 h after dosing, before the last three doses, and at corresponding time points after the last dosing6 μg/kg20.0 ± 5.53Beagle dogs plasma proteaseLC-MS/MSBeagle dogs plasmaIn VivoNoneNoneN.A.
4711
365887172022
GEPPPPGKPADDAGLV
BPC15715FreeFreeLinearLNoneIsolated from human gastric juiceTherapeutic Agent For Severe Trauma And Stress Damage And Can Promote The Healing Of Wounds, Ligament Injuries, Tendon Injuries, And FracturesBlood samples were collected at the corresponding time points before (0 h) and within 6 h of a single administration. Blood samples were collected from dogs administered multiple doses at corresponding time points before the first dosing (0 h), within 6 h after dosing, before the last three doses, and at corresponding time points after the last dosing30 μg/kg25.5 ± 7.08Beagle dogs plasma proteaseLC-MS/MSBeagle dogs plasmaIn VivoNoneNoneN.A.
4712
365887172022
GEPPPPGKPADDAGLV
BPC15715FreeFreeLinearLNoneIsolated from human gastric juiceTherapeutic Agent For Severe Trauma And Stress Damage And Can Promote The Healing Of Wounds, Ligament Injuries, Tendon Injuries, And FracturesBlood samples were collected at the corresponding time points before (0 h) and within 6 h of a single administration. Blood samples were collected from dogs administered multiple doses at corresponding time points before the first dosing (0 h), within 6 h after dosing, before the last three doses, and at corresponding time points after the last dosing150 μg/kg29.3 ± 5.06Beagle dogs plasma proteaseLC-MS/MSBeagle dogs plasmaIn VivoNoneNoneN.A.
4713
N.A.2022
eeeeeeeeeXPLGLAGrrrrrrrrrk
12kD-PEG-e9-XPLGLAG-r9-k(cy5)2512 KDa PEGCy5 linked with Lys side chain at C terminusLinearMixe=D-Glutamic acid, r=D-Aspartic acid, k=D-Lys, Cy5 = indocarbocyanine dye conjugated with Lys at C terminal, X=linkerSyntheticTransport moleculeBlood was collected in a heparinized capillary tube at 30 minutes and 1, 2 And 6 hour time points6 nmol20Mice blood plasma proteaseN.A.Mice blood plasmaIn VivoNoneUS 201916457763 AN.A.
4714
N.A.2022
eeeeeeeeeXPLGLAGrrrrrrrrrk 
Alb-e9-XPLGLAG-r9-k(cy5)25Alb=albuminCy5 linked with Lys side chain at C terminusLinearMixe=D-Glutamic acid, r=D-Aspartic acid, k=D-Lys, Alb=albumin, Cy5 = indocarbocyanine dye conjugated with Lys at C terminal, X=linkerSyntheticTransport moleculeBlood was collected in a heparinized capillary tube at 30 minutes and 1, 2 And 6 hour time points4.8 nmol3Mice blood plasma proteaseN.A.Mice blood plasmaIn VivoNoneUS 201916457763 AN.A.
4715
N.A.2022
eeeeeeeeeXPLGLAGrrrrrrrrrk 
Dex-e9-XPLGLAG-r9-k(cy5)25DextranCy5 linked with Lys side chain at C terminusLinearMixe=D-Glutamic acid, r=D-Aspartic acid, k=D-Lys, Dex=Dextran, Cy5 = indocarbocyanine dye conjugated with Lys at C terminal, X=linkerSyntheticTransport moleculeBlood was collected in a heparinized capillary tube at 30 minutes and 1, 2 And 6 hour time points5 nmol6Mice blood plasma proteaseN.A.Mice blood plasmaIn VivoNoneUS 201916457763 AN.A.
4716
N.A.2022
(eeeeeeeeeXPLGLAGrrrrrrrrrk)4 
Streptavidin-[e9-XPLGLAG-r9-k(cy5)]4100StreptavidinCy5 linked with Lys side chain at C terminusLinearMixe=D-Glutamic acid, r=D-Aspartic acid, k=D-Lys, Strep=Streptavidin, Cy5 = indocarbocyanine dye conjugated with Lys at C terminal, X=linkerSyntheticTransport moleculeBlood was collected in a heparinized capillary tube at 30 minutes and 1, 2 And 6 hour time points4 nmol4Mice blood plasma proteaseN.A.Mice blood plasmaIn VivoNoneUS 201916457763 AN.A.
4717
N.A.2022
(eeeeeeeeeXPLGLAXrrrrrrrrrk)2-(PEG)126 
G5-PAMAM4-[e9-XPLGLAX-r9-k(cy5)]2[PEG]12648G5-PAMAM4Cy5 linked with Lys side chain at C terminus, PEGylationLinearMixe=D-Glutamic acid, r=D-Aspartic acid, k=D-Lys, Strep=Streptavidin, Cy5 = indocarbocyanine dye conjugated with Lys at C terminal, X=linkerSyntheticTransport moleculeBlood was collected in a heparinized capillary tube at 30 minutes and 1, 2 And 6 hour time points3 nmol20Mice blood plasma proteaseN.A.Mice blood plasmaIn VivoNoneUS 201916457763 AN.A.
4718
N.A.2022
k-Sar-H-Aib-EGTFTSDVSSYLEGQAAKEFIAWLVRGRG
Chem.37 (reference compound)33k=D-Lysine,Sar=N-terminal glycine, N£-octadecanoylFreeLinearMixAib substituitions at position 2 of semaglutideSemaglutide Derivative AntidiabetesBlood samples (0.8 Ml) were taken via the second catheter at predetermined time points (0-3 weeks)10 nmol/kg78 (Terminal Half Life)Minipigs plasma proteaseLC-MSMinipigs plasmaIn VivoNoneEP 2021080747 WN.A.
4719
N.A.2022
N.A.
Test 1N.A.N.A.N.A.N.A.N.A.N.A.GLP-1 analogsAntidiabetesBlood samples (0.8 Ml) were taken via the second catheter at predetermined time points (0-3 weeks)10 nmol/kg100 (Terminal Half Life)Minipigs plasma proteaseLC-MSMinipigs plasmaIn VivoNoneEP 2021080747 WN.A.
4720
N.A.2022
N.A.
Test 2N.A.N.A.N.A.N.A.N.A.N.A.GLP-1 analogsAntidiabetesBlood samples (0.8 Ml) were taken via the second catheter at predetermined time points (0-3 weeks)10 nmol/kg101 (Terminal Half Life)Minipigs plasma proteaseLC-MSMinipigs plasmaIn VivoNoneEP 2021080747 WN.A.
4721
N.A.2022
N.A.
Test 3N.A.N.A.N.A.N.A.N.A.N.A.GLP-1 analogsAntidiabetesBlood samples (0.8 Ml) were taken via the second catheter at predetermined time points (0-3 weeks)10 nmol/kg105 (Terminal Half Life)Minipigs plasma proteaseLC-MSMinipigs plasmaIn VivoNoneEP 2021080747 WN.A.
4722
N.A.2022
N.A.
Test 4N.A.N.A.N.A.N.A.N.A.N.A.GLP-1 analogsAntidiabetesBlood samples (0.8 Ml) were taken via the second catheter at predetermined time points (0-3 weeks)10 nmol/kg109 (Terminal Half Life)Minipigs plasma proteaseLC-MSMinipigs plasmaIn VivoNoneEP 2021080747 WN.A.
4723
N.A.2022
H-Aib-EGTFTSDVSSYLEGQAAKEFIAWLVRGRG
Semaglutide31FreeFreeLinearLAib modification at position 2, Lys26 side chain conjugated with (ADO-linker-Glu-C18)GLP-1 analogsGLP-1 receptor agonistBlood samples (0.8 Ml) were taken via the second catheter at predetermined time points (0-3 weeks)10 nmol/kg69 (Terminal Half Life)Minipigs plasma proteaseLC-MSMinipigs plasmaIn VivoNoneEP 2021080747 WN.A.
4724
N.A.2022
QTVVTQEPSLTVSPGGTVTLTCRSSTGAVTTSNYANWVQQKPGQAPRGLIGGTNKRAPGTPARFSGSLLGGKAALTLSGVQPEDEAEYYCALWYSNLWVFGGGTKLTVLGGGGSGGGGSGGGGSEVQLVESGGGLVQPGGSLKLSCAASGFTFNTYAMNWVRQAPGKGLEWVARIRSKYNNYATYYADSVKDRFTISRDDSKNTAYLQMNNLKTEDTAVYYCVRHGNFGNSYVSWFAYWGQGTLVTVSSGGGGSQVQLQQSGSELKKPGASVKVSCKASGYTFTNYGMNWVKQAPGQGLKWMGWINTYTGEPTYTDDFKGRFAFSLDTSVSTAYLQISSLKADDTAVYFCARGGFGSSYWYFDVWGQGSLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSC-DIQLTQSPSSLSASVGDRVSITCKASQDVSIAVAWYQQKPGKAPKLLIYSASYRYTGVPDRFSGSGSGTDFTLTISSLQPEDFAVYYCQQHYITPLTFGAGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
TROP2 TCE (PC1)692FreeFab heavy chain linked to C terminus of ScFv light chainLinearLNoneSyntheticMediates tumor cytotoxicity and T cell activationN.A.3 ug/kg1.02Cynomolgus monkeys plasma proteaseELISACynomolgus monkeys plasmaIn VivoNoneUS 2021/0062261 WEC50(nM) = 0.1477 (TROP binding)
4725
N.A.2022
EVQLVESGGGLVQPGGSLRLSCAASGSTFYTAVMGWVRQAPGKGLEWVAAIRWTALTTSYADSVKGRFTISRDGAKTTLYLQMNSLRPEDTAVYYCAARGTLGLFTTADSYDYWGQGTLVTVSSGGGGSGGGSGGVYCGPEFDESVGCMGGGGSGGGLSGRSDAGSPLGLAGSGGGSEVQLVESGGGLVQPGGSLKLSCAASGFTFNKYAMNWVRQAPGKGLEWVARIRSKYNNYATYYADSVKDRFTISRDDSKNTAYLQMNNLKTEDTAVYYCVRHGNFGNSYISYWAYWGQGTLVTVSSGGGGSGGGGSGGGGSQTVVTQEPSLTVSPGGTVTLTCGSSTGAVTSGNYPNWVQQKPGQAPRGLIGGTKFLAPGTPARFSGSLLGGKAALTLSGVQPEDEAEYYCVLWYSNRWVFGGGTKLTVLGGGGSQVQLQQSGSELKKPGASVKVSCKASGYTFTNYGMNWVKQAPGQGLKWMGWINTYTGEPTYTDDFKGRFAFSLDTSVSTAYLQISSLKADDTAVYFCARGGFGSSYWYFDVWGQGSLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSC-GGVDFCKIYSWPVCHQGGGGSGGLSGRSDAGSPLGLAGSGGSDIQLTQSPSSLSASVGDRVSITCKASQDVSIAVAWYQQKPGKAPKLLIYSASYRYTGVPDRFSGSGSGTDFTLTISSLQPEDFAVYYCQQHYITPLTFGAGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
TROP2 TRACTr PC complex (PC5)911FreeFab heavy chain linked to C terminus of ScFv light chainLinearLNoneSyntheticMediates tumor cytotoxicity and T cell activationN.A.100 ug/kg90.16Cynomolgus monkeys plasma proteaseELISACynomolgus monkeys plasmaIn VivoNoneUS 2021/0062261 WEC50(nM) = 60.25 (TROP binding)
4726
N.A.2022
EVQLVESGGGLVQPGGSLRLSCAASGSTFYTAVMGWVRQAPGKGLEWVAAIRWTALTTSYADSVKGRFTISRDGAKTTLYLQMNSLRPEDTAVYYCAARGTLGLFTTADSYDYWGQGTLVTVSSGGGGSGGGSGGVYCGPEFDESVGCMGSSGGSAAGLLAPPGGLSGRSDAGGGGSEVQLVESGGGLVQPGGSLKLSCAASGFTFNKYAMNWVRQAPGKGLEWVARIRSKYNNYATYYADSVKDRFTISRDDSKNTAYLQMNNLKTEDTAVYYCVRHGNFGNSYISYWAYWGQGTLVTVSSGGGGSGGGGSGGGGSQTVVTQEPSLTVSPGGTVTLTCGSSTGAVTSGNYPNWVQQKPGQAPRGLIGGTKFLAPGTPARFSGSLLGGKAALTLSGVQPEDEAEYYCVLWYSNRWVFGGGTKLTVLGGGGSQVQLQQSGSELKKPGASVKVSCKASGYTFTNYGMNWVKQAPGQGLKWMGWINTYTGEPTYTDDFKGRFAFSLDTSVSTAYLQISSLKADDTAVYFCARGGFGSSYWYFDVWGQGSLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSC-GGIDFCMLYNWPICAGGGGGSSGGSAAGLLAPPGGLSGRSDAGGGGSDIQLTQSPSSLSASVGDRVSITCKASQDVSIAVAWYQQKPGKAPKLLIYSASYRYTGVPDRFSGSGSGTDFTLTISSLQPEDFAVYYCQQHYITPLTFGAGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
TROP2 TRACTr PC complex (PC18)916FreeFab heavy chain linked to C terminus of ScFv light chainLinearLNoneSyntheticMediates tumor cytotoxicity and T cell activationN.A.100 μg/kg 97.31Cynomolgus monkeys plasma proteaseELISACynomolgus monkeys plasmaIn VivoNoneUS 2021/0062261 WIC50(pM) = 3,253
4727
N.A.2022
EVQLVESGGGLVQPGGSLRLSCAASGSTFYTAVMGWVRQAPGKGLEWVAAIRWTALTTSYADSVKGRFTISRDGAKTTLYLQMNSLRPEDTAVYYCAARGTLGLFTTADSYDYWGQGTLVTVSSGGGGSGGGSGGVYCGPEFDESVGCMGSSGGSAAGLLAPPGGLSGRSDAGGGGSEVQLVESGGGLVQPGGSLKLSCAASGFTFNKYAMNWVRQAPGKGLEWVARIRSKYNNYATYYADSVKDRFTISRDDSKNTAYLQMNNLKTEDTAVYYCVRHGNFGNSYISYWAYWGQGTLVTVSSGGGGSGGGGSGGGGSQTVVTQEPSLTVSPGGTVTLTCGSSTGAVTSGNYPNWVQQKPGQAPRGLIGGTKFLAPGTPARFSGSLLGGKAALTLSGVQPEDEAEYYCVLWYSNRWVFGGGTKLTVLGGGGSQVQLQQSGSELKKPGASVKVSCKASGYTFTNYGMNWVKQAPGQGLKWMGWINTYTGEPTYTDDFKGRFAFSLDTSVSTAYLQISSLKADDTAVYFCARGGFGSSYWYFDVWGQGSLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSC-GGVDFCKIYSWPVCHQGGGGSSGGSAAGLLAPPGGLSGRSDAGGGGSDIQLTQSPSSLSASVGDRVSITCKASQDVSIAVAWYQQKPGKAPKLLIYSASYRYTGVPDRFSGSGSGTDFTLTISSLQPEDFAVYYCQQHYITPLTFGAGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGECGGIDFCMLYNWPICAGGGGGSSGGSAAGLLAPPGGLSGRSDAGGGGSDIQLTQSPSSLSASVGDRVSITCKASQDVSIAVAWYQQKPGKAPKLLIYSASYRYTGVPDRFSGSGSGTDFTLTISSLQPEDFAVYYCQQHYITPLTFGAGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
TROP2 TRACTr PC complex (PC21)1177FreeFab heavy chain linked to C terminus of ScFv light chainLinearLNoneSyntheticMediates tumor cytotoxicity and T cell activationN.A.100 μg/kg 100.73Cynomolgus monkeys plasma proteaseELISACynomolgus monkeys plasmaIn VivoNoneUS 2021/0062261 WN.A.
4728
N.A.2022
EVQLVESGGGLVQPGGSLRLSCAASGSTFYTAVMGWVRQAPGKGLEWVAAIRWTALTTSYADSVKGRFTISRDGAKTTLYLQMNSLRPEDTAVYYCAARGTLGLFTTADSYDYWGQGTLVTVSSGGGGSGGGSGGVYCGPEFDESVGCMGGGGSGGGLSGRSDAGSPLGLAGSGGGSEVQLVESGGGLVQPGGSLKLSCAASGFTFNKYAMNWVRQAPGKGLEWVARIRSKYNNYATYYADSVKDRFTISRDDSKNTAYLQMNNLKTEDTAVYYCVRHGNFGNSYISYWAYWGQGTLVTVSSGGGGSGGGGSGGGGSQTVVTQEPSLTVSPGGTVTLTCGSSTGAVTSGNYPNWVQQKPGQAPRGLIGGTKFLAPGTPARFSGSLLGGKAALTLSGVQPEDEAEYYCVLWYSNRWVFGGGTKLTVLGGGGSQVQLQQSGSELKKPGASVKVSCKASGYTFTNYGMNWVKQAPGQGLKWMGWINTYTGEPTYTDDFKGRFAFSLDTSVSTAYLQISSLKADDTAVYFCARGGFGSSYWYFDVWGQGSLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSC-GGIDFCMLYNWPICAGGGGGSGGLSGRSDAGSPLGLAGSGGSDIQLTQSPSSLSASVGDRVSITCKASQDVSIAVAWYQQKPGKAPKLLIYSASYRYTGVPDRFSGSGSGTDFTLTISSLQPEDFAVYYCQQHYITPLTFGAGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
PC-22 complex911FreeFab heavy chain linked to C terminus of ScFv light chainLinearLNoneSyntheticMediates tumor cytotoxicity and T cell activationN.A.100 μg/kg 68.97Cynomolgus monkeys plasma proteaseELISACynomolgus monkeys plasmaIn VivoNoneUS 2021/0062261 WN.A.
4729
N.A.2022
MTMRHNWTPDLSPLWVLLLCAHVVTLLVRATPVSQTTTAATASVRSTKDPCPSQPPVFPAAKQCPALEVTWPEVEVPLNGTLSLSCVACSRFPNFSILYWLGNGSFIEHLPGRLWEGSTSRERGSTGTQLCKALVLEQLTPALHSTNFSCVLVDPEQVVQRHVVLAQLWAGLRATLPPTQEALPSSHSSPQQQG
hIL-18BP194FreeFreeLinearLNoneSyntheticAntagonist of IL-18Single subcutaneous administration: 0, 0.33, 1, 1.5, 3, 5, 7, 12, 24, 48, 72, 120, And 168 Hours (13 Points In Total), Single Intravenous Administration: 0, 0.083, 0.25, 0.5, 1.25, 3, 5, 10, 24, 48, And 72 Hours (11 Points In Total)3 mg/kg + 1 mg/kg6.51Rats plasma proteaseELISARats plasmaIn VivoNoneIB 2021058964 WIC50 of IL-18BP-His was 0.0240 nM
4730
N.A.2022
MTMRHNWTPDLSPLWVLLLCAHVVTLLVRATPVSQTTTAATASVRSTKDPCPSQPPVFPAAKQCPALEVTWPEVEVPLNGTLSLSCVACSRFPNFSILYWLGNGSFIEHLPGRLWEGSTSRERGSTGTQLCKALVLEQLTPALHSTNFSCVLVDPEQVVQRHVVLAQLWAGLRATLPPTQEALPSSHSSPQQQG
hIL-18BP194FreeFreeLinearLNoneSyntheticAntagonist of IL-18Single intravenous administration: 0, 0.083, 0.25, 0.5, 1.25, 3, 5, 10, 24, 48, And 72 Hours (11 Points In Total)1 mg/kg6.51Rats plasma proteaseELISARats plasmaIn VivoNoneIB 2021058964 WIC50 of IL-18BP-His was 0.0240 nM
4731
N.A.2022
(GIVEQCCTSICSLYQLENYCNK*-OH)-(FVEQHLCGDHLVEALYLVCGERGFFETPR-OH)
Example 1251FreeB29R, desB30 modificationsCyclic (C7-C12 disulfide bond in A chain)LA22K(N(eps)tetradecanedioyl-4×gGlu), B3E, B26E modification, A and B chain linked with disulfide bondInsulin Derivative AntidiabetesBlood sample taken at the following time points: Predose (-10,0),3,6,9,12,15,20,30,45,60,90,120,150,180,240,300,360,420,480,540,600 And 720 Minutes1 nmol/kg46Lyd pig plasma proteaseELISALyd pig plasmaIn VivoNoneUS 201615754395 AhIGF1R 0.1% HSA (% rel to HI) Ex48 = 13
4732
N.A.2022
(GIVEQCCTSICSLYQLENYCNK*-OH)-(FVEQHLCGDHLVEALYLVCGERGFFYEER-OH)
Example 151FreeB29R, desB30 modificationsCyclic (C7-C12 disulfide bond in A chain)LA22K(N(eps)tetradecanedioyl-gGlu-2×OEG), B3E, B27E, B28E modifications, , A and B chain linked with disulfide bondInsulin Derivative AntidiabetesBlood sample taken at the following time points: Predose (-10,0),3,6,9,12,15,20,30,45,60,90,120,150,180,240,300,360,420,480,540,600 And 720 Minutes1 nmol/kg103Lyd pig plasma proteaseELISALyd pig plasmaIn VivoNoneUS 201615754395 AhIGF1R 0.1% HSA (% rel to HI) Ex48 = 66.3
4733
N.A.2022
(GIVEQCCTSICSLYQLENYCNK*-OH)-(FVEQHLCGDHLVEALYLVCGERGFFYTDR-OH)
Example 751FreeB29R, desB30 modificaitonCyclic (C7-C12 disulfide bond in A chain)LA22K(N(eps)tetradecanedioyl-gGlu-2×OEG), B3E, B28D modifications, A and B chain linked with disulfide bondInsulin Derivative AntidiabetesBlood sample taken at the following time points: Predose (-10,0),3,6,9,12,15,20,30,45,60,90,120,150,180,240,300,360,420,480,540,600 And 720 Minutes1 nmol/kg86Lyd pig plasma proteaseELISALyd pig plasmaIn VivoNoneUS 201615754395 AhIGF1R 0.1% HSA (% rel to HI) Ex48 = 124.4
4734
N.A.2022
(GIVEQCCTSICSLYQLENYCNK*-OH)-(FVEQHLCGDHLVEALYLVCGERGFFYTDR-OH)
Example 1051FreeB29R, desB30 modificationsCyclic (C7-C12 disulfide bond in A chain)LA22K(N(eps)tetradecanedioyl-4×gGlu), B3E, B28D modifications, A and B chain linked with disulfide bondInsulin Derivative AntidiabetesBlood sample taken at the following time points: Predose (-10,0),3,6,9,12,15,20,30,45,60,90,120,150,180,240,300,360,420,480,540,600 And 720 Minutes1 nmol/kg97Lyd pig plasma proteaseELISALyd pig plasmaIn VivoNoneUS 201615754395 AhIGF1R 0.1% HSA (% rel to HI) Ex48 = 77.3
4735
N.A.2022
(GIVEQCCTSICSLYQLENYCNK*-OH)-(FVEQHLCGSHLVEALYLVCGERGFFETPR-OH)
Example 4551FreeB29R, desB30 modificationsCyclic (C7-C12 disulfide bond in A chain)LA22K(N(eps)hexadecanedioyl-4×gGlu-2×OEG), B3E, B26E modificationsInsulin Derivative AntidiabetesBlood sample taken at the following time points: Predose (-10,0),3,6,9,12,15,20,30,45,60,90,120,150,180,240,300,360,420,480,540,600 And 720 Minutes1 nmol/kg987Lyd pig plasma proteaseELISALyd pig plasmaIn VivoNoneUS 201615754395 AN.A.
4736
N.A.2022
(GIVEQCCTSICSLYQLENYCNK*-OH)-(FVEQHLCGSHLVEALYLVCGERGFFETPR-OH)
Example 4551FreeB29R, desB30 modificationsCyclic (C7-C12 disulfide bond in A chain)LA22K(N(eps)hexadecanedioyl-4×gGlu-2×OEG), B3E, B26E modificationsInsulin Derivative AntidiabetesBlood sample taken at the following time points: Predose (-10,0),3,6,9,12,15,20,30,45,60,90,120,150,180,240,300,360,420,480,540,600 And 720 Minutes713 pmol/kg182Lyd pig plasma proteaseELISALyd pig plasmaIn VivoNoneUS 201615754395 AN.A.
4737
N.A.2022
(GIVEQCCTSICSLYQLENYCNK*-OH)-(FVEQHLCGSHLVEALYLVCGERGFFETPR-OH)
Example 4551FreeB29R, desB30 modificationsCyclic (C7-C12 disulfide bond in A chain)LA22K(N(eps)hexadecanedioyl-4×gGlu-2×OEG), B3E, B26E modificationsInsulin Derivative AntidiabetesBlood sample taken at the following time points: Predose (-10,0),3,6,9,12,15,20,30,45,60,90,120,150,180,240,300,360,420,480,540,600 And 720 Minutes1714 pmol/kg148Lyd pig plasma proteaseELISALyd pig plasmaIn VivoNoneUS 201615754395 AN.A.
4738
N.A.2022
(GIVEQCCTSICSLYQLENYCNK*-OH)-(FVEQHLCGSHLVEALYLVCGERGFFETPR-OH)
Example 4551FreeB29R, desB30 modificationsCyclic (C7-C12 disulfide bond in A chain)LA22K(N(eps)hexadecanedioyl-4×gGlu-2×OEG), B3E, B26E modificationsInsulin Derivative AntidiabetesBlood sample taken at the following time points: Predose (-10,0),3,6,9,12,15,20,30,45,60,90,120,150,180,240,300,360,420,480,540,600 And 720 Minutes720 pmol/kg153Lyd pig plasma proteaseELISALyd pig plasmaIn VivoNoneUS 201615754395 AN.A.
4739
N.A.2022
(GIVEQCCTSICSLYQLENYCNK*-OH)-(FVEQHLCGSHLVEALYLVCGERGFFETPR-OH)
Example 4551FreeB29R, desB30 modificationsCyclic (C7-C12 disulfide bond in A chain)LA22K(N(eps)hexadecanedioyl-4×gGlu-2×OEG), B3E, B26E modificationsInsulin Derivative AntidiabetesBlood sample taken at the following time points: Predose (-10,0),3,6,9,12,15,20,30,45,60,90,120,150,180,240,300,360,420,480,540,600 And 720 Minutes706 pmol/kg158Lyd pig plasma proteaseELISALyd pig plasmaIn VivoNoneUS 201615754395 AN.A.
4740
N.A.2022
(GIVEQCCTSICSLYQLENYCNK*-OH)-(FVEQHLCGSHLVEALYLVCGERGFFETPR-OH)
Example 4551FreeB29R, desB30 modificationsCyclic (C7-C12 disulfide bond in A chain)LA22K(N(eps)hexadecanedioyl-4×gGlu-2×OEG), B3E, B26E modificationsInsulin Derivative AntidiabetesBlood sample taken at the following time points: Predose (-10,0),3,6,9,12,15,20,30,45,60,90,120,150,180,240,300,360,420,480,540,600 And 720 Minutes1735 pmol/kg219Lyd pig plasma proteaseELISALyd pig plasmaIn VivoNoneUS 201615754395 AN.A.
4741
N.A.2022
(GIVEQCCTSICSLEQLENYCNK*-OH)-(FVEQHLCGDHLVEALYLVCGERGFFYEER-OH)
Example 451FreeB29R, desB30 modificationCyclic (C7-C12 disulfide bond in A chain)LA14E, A22K(N(eps)tetradecanedioyl-4×gGlu), B3E, B27E, B28E modifications, A and B chain linked with disulfide bondInsulin Derivative AntidiabetesPlasma collected at time points 0,3,7,15,30,60,120,180 Minutes After Dosing25 nmol/kg24SD rats plasma proteaseLC-MSSD rats plasmaIn VivoNoneUS 201615754395 AhIGF1R 0.1% HSA (% rel to HI) Ex48 = 28.6
4742
N.A.2022
(GIVEQCCTSICSLYQLENYCNK*-OH)-(FVEQHLCGDHLVEALYLVCGERGFFYTDR-OH)
Example 1051FreeB29R, desB30 modificationCyclic (C7-C12 disulfide bond in A chain)LA22K(N(eps)tetradecanedioyl-4×gGlu), B3E, B28D modification, A and B chain linked with disulfide bondInsulin Derivative AntidiabetesPlasma collected at time points 0,3,7,15,30,60,120,180 Minutes After Dosing25 nmol/kg28SD rats plasma proteaseLC-MSSD rats plasmaIn VivoNoneUS 201615754395 AhIGF1R 0.1% HSA (% rel to HI) Ex48 = 77.3
4743
N.A.2022
(GIVEQCCTSICSLYQLENYCNK*-OH)-(FVEQHLCGDHLVEALYLVCGERGFFETER-OH)
Example 1151FreeB29R, desB30 modificationCyclic (C7-C12 disulfide bond in A chain)LA22K(N(eps)tetradecanedioyl-4×gGlu), B3E, B26E, B28E modificatino, A and B chain linked with disulfide bondInsulin Derivative AntidiabetesPlasma collected at time points 0,3,7,15,30,60,120,180 Minutes After Dosing25 nmol/kg28SD rats plasma proteaseLC-MSSD rats plasmaIn VivoNoneUS 201615754395 AhIGF1R 0.1% HSA (% rel to HI) Ex48 = 13.6
4744
N.A.2022
(GIVEQCCTSICSLYQLENYCNK*-OH)-(FVEQHLCGDHLVEALYLVCGERGFFETPR-OH)
Example 1251FreeB29R, desB30 modificationCyclic (C7-C12 disulfide bond in A chain)LA22K(N(eps)tetradecanedioyl-4×gGlu), B3E, B26E modifications, A and B chain linked with disulfide bondInsulin Derivative AntidiabetesPlasma collected at time points 0,3,7,15,30,60,120,180 Minutes After Dosing25 nmol/kg25SD rats plasma proteaseLC-MSSD rats plasmaIn VivoNoneUS 201615754395 AhIGF1R 0.1% HSA (% rel to HI) Ex48 = 13
4745
N.A.2022
(GIVEQCCTSICSLYQLENYCNK*-OH)-(FVNQHLCGSHLVEALYLVCGERGFFYTPR-OH)
PA251FreeB29R, desB30 modificationCyclic (C7-C12 disulfide bond in A chain)LA22K(N(eps)tetradecanedioyl-gGlu-2×OEG) modificationsInsulin Derivative AntidiabetesPlasma collected at time points 0,3,7,15,30,60,120,180 Minutes After Dosing25 nmol/kg24SD rats plasma proteaseLC-MSSD rats plasma with 3 Zn/Hexamer Of Insulin DerivativeIn VivoNoneUS 201615754395 AN.A.
4746
N.A.2022
(GIVEQCCTSICSLYQLENYCNK*-OH)-(FVNQHLCGSHLVEALYLVCGERGFFYTDR-OH)
PA351FreeB29R, desB30 modificationCyclic (C7-C12 disulfide bond in A chain)LA22K(N(eps)tetradecanedioyl-4×gGlu), B28D modificationsInsulin Derivative AntidiabetesPlasma collected at time points 0,3,7,15,30,60,120,180 Minutes After Dosing25 nmol/kg26SD rats plasma proteaseLC-MSSD rats plasma with 3 Zn/Hexamer Of Insulin DerivativeIn VivoNoneUS 201615754395 AN.A.
4747
N.A.2022
(GIVEQCCTSICSLYQLENYCNK*-OH)-(FVEQHLCGDHLVEALYLVCGERGFFYTDR-OH)
Example 3351FreeB29R, desB30 modificationCyclic (C7-C12 disulfide bond in A chain)LA22K(N(eps)hexadecanedioyl-gGlu-2×OEG), B3E, B28D modifications, A and B chain linked with disulfide bondInsulin Derivative AntidiabetesPlasma collected at time points 0,3,7,15,30,60,120,180 Minutes After Dosing25 nmol/kg58SD rats plasma proteaseLC-MSSD rats plasma with 3 Zn/Hexamer Of Insulin DerivativeIn VivoNoneUS 201615754395 AhIGF1R 0.1% HSA (% rel to HI) Ex48 = 85.1
4748
N.A.2022
(GIVEQCCTSICSLYQLENYCNK*-OH)-(FVEQHLCGDHLVEALYLVCGERGFFYEER-OH)
Example 3151FreeB29R, desB30 modificationCyclic (C7-C12 disulfide bond in A chain)LA22K(N(eps)hexadecanedioyl-gGlu-2×OEG), B3E, B27E, B28E modifications, A and B chain linked with disulfide bondInsulin Derivative AntidiabetesPlasma collected at time points 0,3,7,15,30,60,120,180 Minutes After Dosing25 nmol/kg79SD rats plasma proteaseLC-MSSD rats plasma with 3 Zn/Hexamer Of Insulin DerivativeIn VivoNoneUS 201615754395 AhIGF1R 0.1% HSA (% rel to HI) Ex48 = 55
4749
N.A.2022
(GIVEQCCTSICSLYQLENYCNK*-OH)-(FVEQHLCGDHLVEALYLVCGERGFFETPR-OH)
Example 4151FreeB29R, desB30 modificationCyclic (C7-C12 disulfide bond in A chain)LA22K(N(eps)hexadecanedioyl-4×gGlu), B3E, B26E modifications, A and B chain linked with disulfide bondInsulin Derivative AntidiabetesPlasma collected at time points 0,3,7,15,30,60,120,180 Minutes After Dosing25 nmol/kg57SD rats plasma proteaseLC-MSSD rats plasma with 3 Zn/Hexamer Of Insulin DerivativeIn VivoNoneUS 201615754395 AN.A.
4750
N.A.2022
(GIVEQCCTSICSLYQLENYCNK*-OH)-(FVEQHLCGDHLVEALYLVCGERGFFETPR-OH)
Example 4251FreeB29R, desB30 modificationCyclic (C7-C12 disulfide bond in A chain)LA22K(N(eps)hexadecanedioyl-gGlu-2×OEG), B3E, B26E modifications, A and B chain linked with disulfide bondInsulin Derivative AntidiabetesPlasma collected at time points 0,3,7,15,30,60,120,180 Minutes After Dosing25 nmol/kg41SD rats plasma proteaseLC-MSSD rats plasma with 3 Zn/Hexamer Of Insulin DerivativeIn VivoNoneUS 201615754395 AN.A.
4751
N.A.2022
(GIVEQCCTSICSLYQLENYCNK*-OH)-(FVNQHLCGSHLVEALYLVCGERGFFYTPR-OH)
PA151FreeB29R, desB30 modificationCyclic (C7-C12 disulfide bond in A chain)LA22K(N(eps)hexadecanedioyl-gGlu-2×OEG) modificationInsulin Derivative AntidiabetesPlasma collected at time points 0,3,7,15,30,60,120,180 Minutes After Dosing25 nmol/kg41SD rats plasma proteaseLC-MSSD rats plasma with 3 Zn/Hexamer Of Insulin DerivativeIn VivoNoneUS 201615754395 AN.A.
4752
359102762022
MRKSIVRYFVMAFILLFALSTFLTGVQATSVPDKKSPELEKAEIYGDIDVTSDKQTTVIVELKEKSLAEAKADGEKQTKASLKTARSKAKSKALKTLKKAKVNREYDRVFSGFSMKLPASEIPKLLAVKEVKAVYPNATYKPDSVKGKDVTLAADAIYPQMDKSAPFIGADQAWKSGYTGKGIKVAVIDTGVDYTHPDLKNNFGPYKGYDFVDNDYDPQETPTGDPRGGATDHGTHVAGTIAANGQIKGVAPEATLLAYRVLGPGGSGTTENVIAGIEKAVADGAKVMNLSLGNSLNSPDYATSIALDWAMAEGVVAVTSNGNSGPENWTVGSPGTSRVAISVGASQLPYNEYSVTLPSYSSAKVMGYQEEKDLEALNGQEVELVEAGLGQADDFSGKDVKGKVAVIQRGVIPFVDKAENAKNAGAIGAVIYNNATGEIEANVMGMAVPTVKLSKEEGEKLVQQIKEGKHSVVFSFKLDKKLGETIASFSSRGPVMDTWMIKPDVSAPGVNIVSTIPTHDPKNPYGYGSKQGTSMASPHVAGTAAILKQAKPDWTPEQIKGVLMNTAEKLTDENGKPLPHNTQGAGSIRIMEALKASSIVTPGSHSYGTFLKDKGKQTKKQAFTIENLSSHRKAYQLEYSFKGTGITVSGTERVVVPANQTGKAAAKVTVNSAKTKAGTYEGTVYIREDGRKVAEIPLLLIVKEPDYPRVTSVTVEPGAKQGAYTIEAYLPGGAEELAFLVYDENLNLLGQAGVYKNQGKGYQSYQWNGKINDAASLKSGKYYMLAYASAKGKSSYVLTEDPFIVE
KB-SP 806FreeFreeLinearLNoneDerived from Bacillus sp. KB111 strainHaloprotease50°CN.A.90 (Enzyme Activity)N.A.ZymographyEDTA + Tris-HCl + 0.5 M NaCl+ azocaseinIn VitroGenBank id: KUL11341.1NoneKB-SP exhibited more than 50% of the highest activity at pH=6.5–10
4753
359102762022
MRKSIVRYFVMAFILLFALSTFLTGVQATSVPDKKSPELEKAEIYGDIDVTSDKQTTVIVELKEKSLAEAKADGEKQTKASLKTARSKAKSKALKTLKKAKVNREYDRVFSGFSMKLPASEIPKLLAVKEVKAVYPNATYKPDSVKGKDVTLAADAIYPQMDKSAPFIGADQAWKSGYTGKGIKVAVIDTGVDYTHPDLKNNFGPYKGYDFVDNDYDPQETPTGDPRGGATDHGTHVAGTIAANGQIKGVAPEATLLAYRVLGPGGSGTTENVIAGIEKAVADGAKVMNLSLGNSLNSPDYATSIALDWAMAEGVVAVTSNGNSGPENWTVGSPGTSRVAISVGASQLPYNEYSVTLPSYSSAKVMGYQEEKDLEALNGQEVELVEAGLGQADDFSGKDVKGKVAVIQRGVIPFVDKAENAKNAGAIGAVIYNNATGEIEANVMGMAVPTVKLSKEEGEKLVQQIKEGKHSVVFSFKLDKKLGETIASFSSRGPVMDTWMIKPDVSAPGVNIVSTIPTHDPKNPYGYGSKQGTSMASPHVAGTAAILKQAKPDWTPEQIKGVLMNTAEKLTDENGKPLPHNTQGAGSIRIMEALKASSIVTPGSHSYGTFLKDKGKQTKKQAFTIENLSSHRKAYQLEYSFKGTGITVSGTERVVVPANQTGKAAAKVTVNSAKTKAGTYEGTVYIREDGRKVAEIPLLLIVKEPDYPRVTSVTVEPGAKQGAYTIEAYLPGGAEELAFLVYDENLNLLGQAGVYKNQGKGYQSYQWNGKINDAASLKSGKYYMLAYASAKGKSSYVLTEDPFIVE
KB-SP 806FreeFreeLinearLNoneDerived from Bacillus sp. KB111 strainHaloprotease60 °CN.A.10 (Enzyme Activity)N.A.ZymographyEDTA + Tris-HCl + 0.5 M NaCl+ azocaseinIn VitroGenBank id: KUL11341.1NoneKB-SP exhibited more than 50% of the highest activity at pH=6.5–10
4754
359102762022
MRKSIVRYFVMAFILLFALSTFLTGVQATSVPDKKSPELEKAEIYGDIDVTSDKQTTVIVELKEKSLAEAKADGEKQTKASLKTARSKAKSKALKTLKKAKVNREYDRVFSGFSMKLPASEIPKLLAVKEVKAVYPNATYKPDSVKGKDVTLAADAIYPQMDKSAPFIGADQAWKSGYTGKGIKVAVIDTGVDYTHPDLKNNFGPYKGYDFVDNDYDPQETPTGDPRGGATDHGTHVAGTIAANGQIKGVAPEATLLAYRVLGPGGSGTTENVIAGIEKAVADGAKVMNLSLGNSLNSPDYATSIALDWAMAEGVVAVTSNGNSGPENWTVGSPGTSRVAISVGASQLPYNEYSVTLPSYSSAKVMGYQEEKDLEALNGQEVELVEAGLGQADDFSGKDVKGKVAVIQRGVIPFVDKAENAKNAGAIGAVIYNNATGEIEANVMGMAVPTVKLSKEEGEKLVQQIKEGKHSVVFSFKLDKKLGETIASFSSRGPVMDTWMIKPDVSAPGVNIVSTIPTHDPKNPYGYGSKQGTSMASPHVAGTAAILKQAKPDWTPEQIKGVLMNTAEKLTDENGKPLPHNTQGAGSIRIMEALKASSIVTPGSHSYGTFLKDKGKQTKKQAFTIENLSSHRKAYQLEYSFKGTGITVSGTERVVVPANQTGKAAAKVTVNSAKTKAGTYEGTVYIREDGRKVAEIPLLLIVKEPDYPRVTSVTVEPGAKQGAYTIEAYLPGGAEELAFLVYDENLNLLGQAGVYKNQGKGYQSYQWNGKINDAASLKSGKYYMLAYASAKGKSSYVLTEDPFIVE
KB-SP 806FreeFreeLinearLNoneDerived from Bacillus sp. KB111 strainHaloprotease50°CN.A.5 (Enzyme Activity)N.A.ZymographyEDTA + Tris-HCl + 0.5 M NaCl+ azocasein In VitroGenBank id: KUL11341.1NoneKB-SP exhibited more than 50% of the highest activity at pH=6.5–10
4755
359102762022
N.A.
BA17N.A.FreeFreeLinearLNoneIsolated from B. licheniformisSerine protease50°CN.A.90 (Enzyme Activity)N.A.ZymographyN.A.In VitroNoneNoneN.A.
4756
359102762022
N.A.
BA17N.A.FreeFreeLinearLNoneIsolated from B. licheniformisSerine protease60 °CN.A.12 (Enzyme Activity)N.A.ZymographyN.A.In VitroNoneNoneN.A.
4757
358584232022
LQEHPQARKYKGAQKKGLSKGCFGLKLDRIGSMSGLGC
MS-[Gln6,14]CNP-38 (4A)38FreeFreeLinearN.A.Mod = (CH3)2CHSO2-MS-BCN microsphere conjugationSyntheticTreatment of achondroplasiapH 9.4, 37 °CN.A.6 (Release Half Life)N.A.N.A.N.A.N.A.NoneNoneN.A.
4758
358584232022
LQEHPQARKYKGAQKKGLSKGCFGLKLDRIGSMSGLGC
MS-[Gln6,14]CNP-38(4B)38FreeFreeLinearN.A.Mod = (CH3)2NSO2-MS-BCN microsphere conjugationSyntheticTreatment of achondroplasiapH 9.4, 37 °CN.A.15.8 (Release Half Life)N.A.N.A.N.A.N.A.NoneNoneN.A.
4759
358584232022
LQEHPQARKYKGAQKKGLSKGCFGLKLDRIGSMSGLGC
MS-[Gln6,14]CNP-38 (4A)38FreeFreeLinearN.A.Mod = (CH3)2CHSO2-MS-BCN microsphere conjugationSyntheticTreatment of achondroplasiapH 7.4, 37 °C,N.A.600 (Release Half Life)N.A.N.A.N.A.N.A.NoneNoneN.A.
4760
358584232022
LQEHPQARKYKGAQKKGLSKGCFGLKLDRIGSMSGLGC
MS-[Gln6,14]CNP-38(4B)38FreeFreeLinearN.A.Mod = (CH3)2NSO2-MS-BCN microsphere conjugationSyntheticTreatment of achondroplasiapH 7.4, 37 °C,N.A.1580 (Release Half Life)N.A.N.A.N.A.N.A.NoneNoneN.A.
4761
357117552022
N.A.
R13 Fae393N.A.N.A.N.A.N.A.N.A.SyntheticXylanasepH 6.0 25 CelsiusN.A.23 (Half Life Activty)N.A.N.A.Phosphate bufferIn VitroNoneNoneN.A.
4762
357117552022
N.A.
R13 Fae393N.A.N.A.N.A.N.A.N.A.SyntheticXylanasepH 6.0 ,35°CN.A.16 (Half Life Activity)N.A.N.A.Phosphate bufferIn VitroNoneNoneN.A.
4763
354883382022
N.A.
FRAP-smTGN.A.Frap (A Fusion Tag)FreeLinearLNoneTGm1 variant Used to generate protein crosslinking or attachment of small molecules60 ℃0.4 mg/mL < 2 (Activity Half Life)N.A.N.A.N.A.N.A.NoneNoneN.A.
4764
354883382022
N.A.
FRAP-TGm1N.A.Frap (A Fusion Tag)FreeLinearLNoneTGm1 variant Used to generate protein crosslinking or attachment of small molecules60 ℃0.4 mg/mL 11.31 (Activity Half Life)N.A.N.A.N.A.N.A.NoneNoneN.A.
4765
354883382022
N.A.
FRAPD-TGm1N.A.Frap (A Fusion Tag)FreeLinearLadditional modification (Asp residue)TGm1 variant Used to generate protein crosslinking or attachment of small molecules60 ℃0.4 mg/mL 21.97 (Activity Half Life)N.A.N.A.N.A.N.A.NoneNoneN.A.
4766
351338602022
NDRAAAIIRADDLASTGYTGEGQIVGVADSGLDTGDLDRIHPDFEGRVKELYAIGRKGDASDPDGHGTHVAGSIVGTGKASDGOYKGMAPDAKLVFHSMLDEYGYLAGDVSDILEEAYADGARIHSDSWGVDDDGEYGLDSFLFDQFLWEHPDMTALVAAGNAGIYGYETIGTPATAKNVIAVGASENDRPELDEDEADDPDEVAAFSSRGTTADGRLKPDLVAPGSYILSTRSSLAPDENFHGLFNAFYAYLSGTSMATPVLAGGVAQVRQFLQENGVDNPSGALIKAMLISGADDLNEDMRVQGFGRANLRRAIETGFVDEKKGLKTGDVATYRLNVTDDSQPLAITLAWTDYPASLAAERTLVNNLNLRVVTPSGETLNGNDFFHYPYDDEVDNLNNVEQVWIKHPEEGVYTVTVEGYNVPMGPQPYALAANG
mTSS436FreeFreeLinearLNoneDerived from preTSSCollagenolytic protease 75°CN.A.1.5 (Activity Half Life)N.A.N.A.10 mM CaCl2 at pH 9.0In Viro Study NoneNoneIn the presence of 10 mM CaCl2 at pH 9.0, mTSS retained more than 80% or 70% of the original activity after 8 h of incubation at 60°C or 70°C
4767
351338602022
NDRAAAIIRADDLASTGYTGEGQIVGVADSGLDTGDLDRIHPDFEGRVKELYAIGRKGDASDPDGHGTHVAGSIVGTGKASDGOYKGMAPDAKLVFHSMLDEYGYLAGDVSDILEEAYADGARIHSDSWGVDDDGEYGLDSFLFDQFLWEHPDMTALVAAGNAGIYGYETIGTPATAKNVIAVGASENDRPELDEDEADDPDEVAAFSSRGTTADGRLKPDLVAPGSYILSTRSSLAPDENFHGLFNAFYAYLSGTSMATPVLAGGVAQVRQFLQENGVDNPSGALIKAMLISGADDLNEDMRVQGFGRANLRRAIETGFVDEKKGLKTGDVATYRLNVTDDSQPLAITLAWTDYPASLAAERTLVNNLNLRVVTPSGETLNGNDFFHYPYDDEVDNLNNVEQVWIKHPEEGVYTVTVEGYNVPMGPQPYALAANG
mTSS436FreeFreeLinearLNoneDerived from preTSSCollagenolytic protease 60°CN.A.2 (Activity Half Life)N.A.N.A.10 mM CaCl2 at pH 11.0 In Viro Study NoneNoneIn the presence of 10 mM CaCl2 at pH 9.0, mTSS retained more than 80% or 70% of the original activity after 8 h of incubation at 60°C or 70°C
4768
351338602022
NDRAAAIIRADDLASTGYTGEGQIVGVADSGLDTGDLDRIHPDFEGRVKELYAIGRKGDASDPDGHGTHVAGSIVGTGKASDGOYKGMAPDAKLVFHSMLDEYGYLAGDVSDILEEAYADGARIHSDSWGVDDDGEYGLDSFLFDQFLWEHPDMTALVAAGNAGIYGYETIGTPATAKNVIAVGASENDRPELDEDEADDPDEVAAFSSRGTTADGRLKPDLVAPGSYILSTRSSLAPDENFHGLFNAFYAYLSGTSMATPVLAGGVAQVRQFLQENGVDNPSGALIKAMLISGADDLNEDMRVQGFGRANLRRAIETGFVDEKKGLKTGDVATYRLNVTDDSQPLAITLAWTDYPASLAAERTLVNNLNLRVVTPSGETLNGNDFFHYPYDDEVDNLNNVEQVWIKHPEEGVYTVTVEGYNVPMGPQPYALAANG
mTSS436FreeFreeLinearLNoneDerived from preTSSCollagenolytic protease N.A.N.A.>12 (Activity Half Life)N.A.N.A.10 mM CaCl2 at pH 7.5In Viro Study NoneNoneIn the presence of 10 mM CaCl2 at pH 9.0, mTSS retained more than 80% or 70% of the original activity after 8 h of incubation at 60°C or 70°C
4769
351338602022
NDRAAAIIRADDLASTGYTGEGQIVGVADSGLDTGDLDRIHPDFEGRVKELYAIGRKGDASDPDGHGTHVAGSIVGTGKASDGOYKGMAPDAKLVFHSMLDEYGYLAGDVSDILEEAYADGARIHSDSWGVDDDGEYGLDSFLFDQFLWEHPDMTALVAAGNAGIYGYETIGTPATAKNVIAVGASENDRPELDEDEADDPDEVAAFSSRGTTADGRLKPDLVAPGSYILSTRSSLAPDENFHGLFNAFYAYLSGTSMATPVLAGGVAQVRQFLQENGVDNPSGALIKAMLISGADDLNEDMRVQGFGRANLRRAIETGFVDEKKGLKTGDVATYRLNVTDDSQPLAITLAWTDYPASLAAERTLVNNLNLRVVTPSGETLNGNDFFHYPYDDEVDNLNNVEQVWIKHPEEGVYTVTVEGYNVPMGPQPYALAANG
mTSS436FreeFreeLinearLNoneDerived from preTSSCollagenolytic protease 70°CN.A.6 (Activity Half Life)N.A.N.A.pH 9In Viro Study NoneNoneIn the presence of 10 mM CaCl2 at pH 9.0, mTSS retained more than 80% or 70% of the original activity after 8 h of incubation at 60°C or 70°C
4770
351338602022
N.A.
E187A N.A.FreeFreeLinearLResidue Glu187 of the Ca1 site in the catalytic domain was replaced by AlaDerived from preTSSCollagenolytic protease 70°CN.A.N.A.N.A.N.A.N.A.In Viro Study NoneNoneWhen the residue Glu187 of the Ca1 site in the catalytic domain was replaced by Ala, the resulting variant E187A was completely inactivated after incubation at 70°C for 3 h
4771
351779452022
RPRLSHKGPMPF
pE13F13pGlu = PyroglutamateFreeLinearLNoneApelin AnalogDiuretic and Cardiovascular effectsIncubated at 37°C for various times, from T0 to T4 h5 μM7.2Mouse plasma proteaseLC-MSMouse plasmaIn Vitrohttps://pubmed.ncbi.nlm.nih.gov/29412822/, https://pubmed.ncbi.nlm.nih.gov/27815337/NoneKi(nM) = 0.56 ± 0.07
4772
351779452022
QRPRlS-Aib-Ka-P-Nle-P
P2612N-Acetylated Arg2FreeLinearMixD-Leu, D-ala = l and a, Proline side chain linked with (4Br-Phe) at C terminusApelin AnalogDiuretic and Cardiovascular effectsIncubated at 37°C for various times, from T0 to T4 h5 μM86Mouse plasma proteaseLC-MSMouse plasmaIn Vitrohttps://pubmed.ncbi.nlm.nih.gov/29412822/, https://pubmed.ncbi.nlm.nih.gov/27815337/NoneKi(nM) = 2.11 ± 0.40
4773
351779452022
KFRRQRPRLSHKGPMPF
K17F17FreeFreeLinearLNoneApelin AnalogDiuretic and Cardiovascular effectsIncubated at 37°C for various times, from T0 to T4 h5 μM4.6Mouse plasma proteaseLC-MSMouse plasmaIn Vitrohttps://pubmed.ncbi.nlm.nih.gov/29412822/, https://pubmed.ncbi.nlm.nih.gov/27815337/NoneKi(nM) = 0.06 ± 0.01
4774
351779452022
KFrRqRPRlS-Aib-kaP-Nle-P
P9216Lys1 acetylationFreeLinearMixD-Arg = r, D-Gln = q, D-Leu = l, D-ala = a, Proline side chain linked with (4Br-Phe) at C terminusApelin AnalogDiuretic and Cardiovascular effectsIncubated at 37°C for various times, from T0 to T4 h5 μM24Mouse plasma proteaseLC-MSMouse plasmaIn Vitrohttps://pubmed.ncbi.nlm.nih.gov/29412822/, https://pubmed.ncbi.nlm.nih.gov/27815337/NoneKi(nM) = 0.09 ± 0.02
4775
351779452022
KFRRQRPRLSHKGPMPF
LIT01-19617FC [CF3(CF2)7(CH2)2C(O)] conjugation at N terminalFreeLinearLNoneApelin AnalogDiuretic and Cardiovascular effectsIncubated at 37°C for various times, from T0 to T4 h5 μM1440Mouse plasma proteaseLC-MSMouse plasmaIn Vitrohttps://pubmed.ncbi.nlm.nih.gov/29412822/, https://pubmed.ncbi.nlm.nih.gov/27815337/NoneKi(nM) = 0.08 ± 0.01
4776
351779452022
QRPRLSHKGPMPF
Apelin-1313FreeFreeLinearLNoneSecreted by White Adipose Tissue (Wat) in both humans and animalsAntidiabetes, Anorexic EffectsN.A.N.A.2.1Mouse plasma proteaseRP-HPLCMouse plasmaIn Vitrohttps://pubmed.ncbi.nlm.nih.gov/29412822/, https://pubmed.ncbi.nlm.nih.gov/27815337/NoneEC50 = 7.4 x 10⁻⁹ M
4777
351779452022
QRPRLSHKGPMPF
(Lys8GluPAL)apelin-13-amide13FreeAmidationLinearLNoneApelin-13 AnalogueAntidiabetes, Anorexic EffectsN.A.N.A.>24Mouse plasma proteaseRP-HPLCMouse plasmaIn Vitrohttps://pubmed.ncbi.nlm.nih.gov/29412822/, https://pubmed.ncbi.nlm.nih.gov/27815337/NoneEC50 = 1.2 x 10⁻¹⁰ M
4778
351779452022
QRPRLSHKGPMPY
Lys8GluPAL(Tyr13)apelin-1313FreeTyr13 modifcation, carboxylationLinearLNoneApelin-13 AnalogueAntidiabetes, Anorexic EffectsN.A.N.A.>24Mouse plasma proteaseRP-HPLCMouse plasmaIn Vitrohttps://pubmed.ncbi.nlm.nih.gov/29412822/, https://pubmed.ncbi.nlm.nih.gov/27815337/NoneEC50 = 1.1 x 10⁻⁹ M
4779
351779452022
QRPRLSHKGPMPV
Lys8GluPAL(Val13)apelin-1313FreeVal13 modifcation, carboxylationLinearLNoneApelin-13 AnalogueAntidiabetes, Anorexic EffectsN.A.N.A.>24Mouse plasma proteaseRP-HPLCMouse plasmaIn Vitrohttps://pubmed.ncbi.nlm.nih.gov/29412822/, https://pubmed.ncbi.nlm.nih.gov/27815337/NoneEC50 = 2.2 x 10⁻¹⁰M
4780
351779452022
pGlu-RPRLSHKGPMPF
pGlu(Lys8GluPAL)apelin-13-amide13pGlu = PyroglutamateAmidationLinearLNoneApelin-13 AnalogueAntidiabetes, Anorexic EffectsN.A.N.A.>24Mouse plasma proteaseRP-HPLCMouse plasmaIn Vitrohttps://pubmed.ncbi.nlm.nih.gov/29412822/, https://pubmed.ncbi.nlm.nih.gov/27815337/NoneEC50 = 3.1 x 10⁻¹⁰M
4781
351779452022
QRPRLSHKGPMPY
Lys8GluPAL(Tyr13)apelin-1313FreeTyr13 modifcation, carboxylationLinearLI125 radioactive labeledApelin-13 AnalogueAntidiabetes, Anorexic EffectsBlood (20 microliter) collected at 0, 15, 30, 45, 60, 90, 120, 240, 480, 960 and 1440 min after injection4.1 nmol/kg2.5 - 3NIH swiss mice plasma proteaseRP-HPLCNIH swiss mice plasmaIn Vivohttps://pubmed.ncbi.nlm.nih.gov/29412822/, https://pubmed.ncbi.nlm.nih.gov/27815337/NoneEC50 = 1.1 x 10⁻⁹ M
4782
351779452022
QRPRLSHKGPMPA
(Ala13)apelin-1313FreeAla13 modifcation, carboxylationLinearLNoneApelin-13 AnalogueInsulinotrophic activity0, 2, 4, 8, 24 h20 μg 10.3Mouse plasma proteaseRP-HPLCMouse plasma in the presence of 50 Mmol/L TEA-HCl Buffer In Vitrohttps://pubmed.ncbi.nlm.nih.gov/29412822/, https://pubmed.ncbi.nlm.nih.gov/27815337/NoneEC50(M) = 1.74e-009 (In vitro insulin secretion)
4783
351779452022
pGlu-RPRLSHKGPMPF
(pGlu)apelin-1313pGlu = PyroglutamateAmidationLinearLNoneApelin-13 AnalogueInsulinotrophic activity0, 2, 4, 8, 24 h20 μg 3.8Mouse plasma proteaseRP-HPLCMouse plasma in the presence of 50 Mmol/L TEA-HCl Buffer In Vitrohttps://pubmed.ncbi.nlm.nih.gov/29412822/, https://pubmed.ncbi.nlm.nih.gov/27815337/NoneEC50(M) = 1.10e-008 (In vitro insulin secretion)
4784
351779452022
pGlu-RPRLSHKGPMPA
pGlu(Ala13)apelin-1313pGlu = PyroglutamateAla13 modifcation, carboxylationLinearLNoneApelin-13 AnalogueInsulinotrophic activity0, 2, 4, 8, 24 h20 μg 11.1Mouse plasma proteaseRP-HPLCMouse plasma in the presence of 50 Mmol/L TEA-HCl Buffer In Vitrohttps://pubmed.ncbi.nlm.nih.gov/29412822/, https://pubmed.ncbi.nlm.nih.gov/27815337/NoneEC50(M) = 7.68e-009 (In vitro insulin secretion)
4785
351779452022
pGlu-RPRLSHKGPMPV
pGlu(Val13)apelin-1313pGlu = PyroglutamateVal13 modifcation, carboxylationLinearLNoneApelin-13 AnalogueInsulinotrophic Activity0, 2, 4, 8, 24 h20 microgram9.8Mouse plasma proteaseRP-HPLCMouse plasma in the presence of 50 Mmol/L TEA-HCl Buffer In Vitrohttps://pubmed.ncbi.nlm.nih.gov/29412822/, https://pubmed.ncbi.nlm.nih.gov/27815337/NoneEC50(M) = 1.59e-008 (In vitro insulin secretion)
4786
351779452022
pGlu-RPRLSHKGPMPY
pGlu(Tyr13)apelin-1313pGlu = PyroglutamateTyr13 modifcation, carboxylationLinearLNoneApelin-13 AnalogueInsulinotrophic Activity0, 2, 4, 8, 24 h20 microgram12.2Mouse plasma proteaseRP-HPLCMouse plasma in the presence of 50 Mmol/L TEA-HCl Buffer In Vitrohttps://pubmed.ncbi.nlm.nih.gov/29412822/, https://pubmed.ncbi.nlm.nih.gov/27815337/NoneEC50(M) = 1.48e-008 (In vitro insulin secretion)
4787
352591492022
(CH-Mal-C3-GIVEQCCTSICSLYQLENYCN)-FVNQHLCGSHLVEALYLVCGERGFFYTPK
CH-/HPN-Conjugated Insulins (GlyA1)50Gly1(A) Maleimide modified linked using linker C3 (N-[β-maleimidopropyloxy] succinimide ester, BMPS) with chondroitin [CH]FreeCyclic (C6-C11 disulfide bond in A chain)LC7-C7 and C20-C19 disulfide bond between A and B chainHuman insulin analogAntidiabetesBlood samples were collected immediately before injection and at various time points up to 48 h after injection340 nmol/kg5.6Mice serum proteaseSandwich ELISAMice serumIn Vivohttps://pubs.acs.org/doi/10.1021/acsomega.9b00059, https://pubmed.ncbi.nlm.nih.gov/28365509/NoneEC50(nM) = 4.84
4788
352591492022
(CH-Mal-C3-GIVEQCCTSICSLYQLENYCN)-FVNQHLCGSHLVEALYLVCGERGFFYTPK
CH-/HPN-Conjugated Insulins (GlyA1)50Gly1(A) Maleimide modified linked using linker C3 (N-[β-maleimidopropyloxy] succinimide ester, BMPS) with chondroitin [CH]FreeCyclic (C6-C11 disulfide bond in A chain)LC7-C7 and C20-C19 disulfide bond between A and B chainHuman insulin analogAntidiabetesBlood samples were collected immediately before injection and at various time points up to 48 h after injection340 nmol/kg5.5Mice serum proteaseSandwich ELISAMice serumIn Vivohttps://pubs.acs.org/doi/10.1021/acsomega.9b00059, https://pubmed.ncbi.nlm.nih.gov/28365509/NoneEC50(nM) = 4.84
4789
352591492022
GIVEQCCTSICSLYQLENYCN-(FVNQHLCGSHLVEALYLVCGERGFFYTPK-C3-Mal-CH)
CH-/HPN-Conjugated Insulins (LysB29)50FreeK29(B) Maleimide modified linked using linker C3 (N-[β-maleimidopropyloxy] succinimide ester, BMPS) with chondroitin [CH]Cyclic (C6-C11 disulfide bond in A chain)LC7-C7 and C20-C19 disulfide bond between A and B chainHuman insulin analogAntidiabetesBlood samples were collected immediately before injection and at various time points up to 48 h after injection340 nmol/kg3.4Mice serum proteaseSandwich ELISAMice serumIn Vivohttps://pubs.acs.org/doi/10.1021/acsomega.9b00059, https://pubmed.ncbi.nlm.nih.gov/28365509/NoneEC50(nM) = 2.48
4790
352591492022
GIVEQCCTSICSLYQLENYCN-(FVNQHLCGSHLVEALYLVCGERGFFYTPK-C3-Mal-CH)
CH-/HPN-Conjugated Insulins (LysB29)50FreeK29(B) Maleimide modified linked using linker C3 (N-[β-maleimidopropyloxy] succinimide ester, BMPS) with chondroitin [CH]Cyclic (C6-C11 disulfide bond in A chain)LC7-C7 and C20-C19 disulfide bond between A and B chainHuman insulin analogAntidiabetesBlood samples were collected immediately before injection and at various time points up to 48 h after injection340 nmol/kg4.4Mice serum proteaseSandwich ELISAMice serumIn Vivohttps://pubs.acs.org/doi/10.1021/acsomega.9b00059, https://pubmed.ncbi.nlm.nih.gov/28365509/NoneEC50(nM) = 2.48
4791
352591492022
(CH-Mal-C3-GIVEQCCTSICSLYQLENYCN)-(FVNQHLCGSHLVEALYLVCGERGFFYTPK-C3-Mal-CH)
CH-/HPN-Conjugated Insulins (GlyA1/LysB29)50Gly1(A) Maleimide modified linked using linker C3 (N-[β-maleimidopropyloxy] succinimide ester, BMPS) with chondroitin [CH]K29(B) Maleimide modified linked using linker C3 (N-[β-maleimidopropyloxy] succinimide ester, BMPS) with chondroitin [CH]Cyclic (C6-C11 disulfide bond in A chain)LC7-C7 and C20-C19 disulfide bond between A and B chainHuman insulin analogAntidiabetesBlood samples were collected immediately before injection and at various time points up to 48 h after injection340 nmol/kg7.5Mice serum proteaseSandwich ELISAMice serumIn Vivohttps://pubs.acs.org/doi/10.1021/acsomega.9b00059, https://pubmed.ncbi.nlm.nih.gov/28365509/NoneEC50(nM) = 6.32
4792
352591492022
(CH-Mal-C3-GIVEQCCTSICSLYQLENYCN)-(FVNQHLCGSHLVEALYLVCGERGFFYTPK-C3-Mal-CH)
CH-/HPN-Conjugated Insulins (GlyA1/LysB29)50Gly1(A) Maleimide modified linked using linker C3 (N-[β-maleimidopropyloxy] succinimide ester, BMPS) with chondroitin [CH]K29(B) Maleimide modified linked using linker C3 (N-[β-maleimidopropyloxy] succinimide ester, BMPS) with chondroitin [CH]Cyclic (C6-C11 disulfide bond in A chain)LC7-C7 and C20-C19 disulfide bond between A and B chainHuman insulin analogAntidiabetesBlood samples were collected immediately before injection and at various time points up to 48 h after injection340 nmol/kg7.1Mice serum proteaseSandwich ELISAMice serumIn Vivohttps://pubs.acs.org/doi/10.1021/acsomega.9b00059, https://pubmed.ncbi.nlm.nih.gov/28365509/NoneEC50(nM) = 6.32
4793
352591492022
(CH-Mal-C6-GIVEQCCTSICSLYQLENYCN)-FVNQHLCGSHLVEALYLVCGERGFFYTPK
CH-/HPN-Conjugated Insulins (GlyA1)50Gly1(A) Maleimide modified linked using linker C6 (N-[ε-maleimidocaproyloxy] sulfosuccinimide ester, EMCS) with chondroitin [CH]FreeCyclic (C6-C11 disulfide bond in A chain)LC7-C7 and C20-C19 disulfide bond between A and B chainHuman insulin analogAntidiabetesBlood samples were collected immediately before injection and at various time points up to 48 h after injection340 nmol/kg5.6Mice serum proteaseSandwich ELISAMice serumIn Vivohttps://pubs.acs.org/doi/10.1021/acsomega.9b00059, https://pubmed.ncbi.nlm.nih.gov/28365509/NoneEC50(nM) = 9.76
4794
352591492022
(CH-Mal-C6-GIVEQCCTSICSLYQLENYCN)-FVNQHLCGSHLVEALYLVCGERGFFYTPK
CH-/HPN-Conjugated Insulins (GlyA1)50Gly1(A) Maleimide modified linked using linker C6 (N-[ε-maleimidocaproyloxy] sulfosuccinimide ester, EMCS) with chondroitin [CH]FreeCyclic (C6-C11 disulfide bond in A chain)LC7-C7 and C20-C19 disulfide bond between A and B chainHuman insulin analogAntidiabetesBlood samples were collected immediately before injection and at various time points up to 48 h after injection340 nmol/kg6.9Mice serum proteaseSandwich ELISAMice serumIn Vivohttps://pubs.acs.org/doi/10.1021/acsomega.9b00059, https://pubmed.ncbi.nlm.nih.gov/28365509/NoneEC50(nM) = 9.76
4795
352591492022
GIVEQCCTSICSLYQLENYCN-(FVNQHLCGSHLVEALYLVCGERGFFYTPK-C6-Mal-CH)
CH-/HPN-Conjugated Insulins (LysB29)50FreeK29(B) Maleimide modified linked using linker C6 (N-[ε-maleimidocaproyloxy] sulfosuccinimide ester, EMCS) with chondroitin [CH]Cyclic (C6-C11 disulfide bond in A chain)LC7-C7 and C20-C19 disulfide bond between A and B chainHuman insulin analogAntidiabetesBlood samples were collected immediately before injection and at various time points up to 48 h after injection340 nmol/kg2.2Mice serum proteaseSandwich ELISAMice serumIn Vivohttps://pubs.acs.org/doi/10.1021/acsomega.9b00059, https://pubmed.ncbi.nlm.nih.gov/28365509/NoneEC50(nM) = 1.52
4796
352591492022
GIVEQCCTSICSLYQLENYCN-(FVNQHLCGSHLVEALYLVCGERGFFYTPK-C6-Mal-CH)
CH-/HPN-Conjugated Insulins (LysB29)50FreeK29(B) Maleimide modified linked using linker C6 (N-[ε-maleimidocaproyloxy] sulfosuccinimide ester, EMCS) with chondroitin [CH]Cyclic (C6-C11 disulfide bond in A chain)LC7-C7 and C20-C19 disulfide bond between A and B chainHuman insulin analogAntidiabetesBlood samples were collected immediately before injection and at various time points up to 48 h after injection340 nmol/kg2.8Mice serum proteaseSandwich ELISAMice serumIn Vivohttps://pubs.acs.org/doi/10.1021/acsomega.9b00059, https://pubmed.ncbi.nlm.nih.gov/28365509/NoneEC50(nM) = 1.52
4797
352591492022
(CH-Mal-C6-GIVEQCCTSICSLYQLENYCN)-(FVNQHLCGSHLVEALYLVCGERGFFYTPK-C6-Mal-CH)
CH-/HPN-Conjugated Insulins (GlyA1/LysB29)50Gly1(A) Maleimide modified linked using linker C6 (N-[ε-maleimidocaproyloxy] sulfosuccinimide ester, EMCS) with chondroitin [CH]K29(B) Maleimide modified linked using linker C6 (N-[ε-maleimidocaproyloxy] sulfosuccinimide ester, EMCS) with chondroitin [CH]Cyclic (C6-C11 disulfide bond in A chain)LC7-C7 and C20-C19 disulfide bond between A and B chainHuman insulin analogAntidiabetesBlood samples were collected immediately before injection and at various time points up to 48 h after injection340 nmol/kg9.4Mice serum proteaseSandwich ELISAMice serumIn Vivohttps://pubs.acs.org/doi/10.1021/acsomega.9b00059, https://pubmed.ncbi.nlm.nih.gov/28365509/NoneEC50(nM) = 32.87
4798
352591492022
(CH-Mal-C6-GIVEQCCTSICSLYQLENYCN)-(FVNQHLCGSHLVEALYLVCGERGFFYTPK-C6-Mal-CH)
CH-/HPN-Conjugated Insulins (GlyA1/LysB29)50Gly1(A) Maleimide modified linked using linker C6 (N-[ε-maleimidocaproyloxy] sulfosuccinimide ester, EMCS) with chondroitin [CH]K29(B) Maleimide modified linked using linker C6 (N-[ε-maleimidocaproyloxy] sulfosuccinimide ester, EMCS) with chondroitin [CH]Cyclic (C6-C11 disulfide bond in A chain)LC7-C7 and C20-C19 disulfide bond between A and B chainHuman insulin analogAntidiabetesBlood samples were collected immediately before injection and at various time points up to 48 h after injection340 nmol/kg11.8Mice serum proteaseSandwich ELISAMice serumIn Vivohttps://pubs.acs.org/doi/10.1021/acsomega.9b00059, https://pubmed.ncbi.nlm.nih.gov/28365509/NoneEC50(nM) = 32.87
4799
352591492022
(CH-Mal-C11-GIVEQCCTSICSLYQLENYCN)-FVNQHLCGSHLVEALYLVCGERGFFYTPK
CH-/HPN-Conjugated Insulins (GlyA1)50Gly1(A) Maleimide modified linked using linker C11 (N-[κ-maleimidoundecanoyloxy]- sulfosuccinimide ester, KMUS) with chondroitin [CH]FreeCyclic (C6-C11 disulfide bond in A chain)LC7-C7 and C20-C19 disulfide bond between A and B chainHuman insulin analogAntidiabetesBlood samples were collected immediately before injection and at various time points up to 48 h after injection340 nmol/kg4.8Mice serum proteaseSandwich ELISAMice serumIn Vivohttps://pubs.acs.org/doi/10.1021/acsomega.9b00059, https://pubmed.ncbi.nlm.nih.gov/28365509/NoneEC50(nM) = 11.01
4800
352591492022
(CH-Mal-C11-GIVEQCCTSICSLYQLENYCN)-FVNQHLCGSHLVEALYLVCGERGFFYTPK
CH-/HPN-Conjugated Insulins (GlyA1)50Gly1(A) Maleimide modified linked using linker C11 (N-[κ-maleimidoundecanoyloxy]- sulfosuccinimide ester, KMUS) with chondroitin [CH]FreeCyclic (C6-C11 disulfide bond in A chain)LC7-C7 and C20-C19 disulfide bond between A and B chainHuman insulin analogAntidiabetesBlood samples were collected immediately before injection and at various time points up to 48 h after injection340 nmol/kg5.8Mice serum proteaseSandwich ELISAMice serumIn Vivohttps://pubs.acs.org/doi/10.1021/acsomega.9b00059, https://pubmed.ncbi.nlm.nih.gov/28365509/NoneEC50(nM) = 11.01
4801
352591492022
GIVEQCCTSICSLYQLENYCN-(FVNQHLCGSHLVEALYLVCGERGFFYTPK-C11-Mal-CH)
CH-/HPN-Conjugated Insulins (LysB29)50FreeK29(B) Maleimide modified linked using linker C11 (N-[κ-maleimidoundecanoyloxy]- sulfosuccinimide ester, KMUS) with chondroitin [CH]Cyclic (C6-C11 disulfide bond in A chain)LC7-C7 and C20-C19 disulfide bond between A and B chainHuman insulin analogAntidiabetesBlood samples were collected immediately before injection and at various time points up to 48 h after injection340 nmol/kg4.9Mice serum proteaseSandwich ELISAMice serumIn Vivohttps://pubs.acs.org/doi/10.1021/acsomega.9b00059, https://pubmed.ncbi.nlm.nih.gov/28365509/NoneEC50(nM) = 1.29
4802
352591492022
GIVEQCCTSICSLYQLENYCN-(FVNQHLCGSHLVEALYLVCGERGFFYTPK-C11-Mal-CH)
CH-/HPN-Conjugated Insulins (LysB29)50FreeK29(B) Maleimide modified linked using linker C11 (N-[κ-maleimidoundecanoyloxy]- sulfosuccinimide ester, KMUS) with chondroitin [CH]Cyclic (C6-C11 disulfide bond in A chain)LC7-C7 and C20-C19 disulfide bond between A and B chainHuman insulin analogAntidiabetesBlood samples were collected immediately before injection and at various time points up to 48 h after injection340 nmol/kg4.4Mice serum proteaseSandwich ELISAMice serumIn Vivohttps://pubs.acs.org/doi/10.1021/acsomega.9b00059, https://pubmed.ncbi.nlm.nih.gov/28365509/NoneEC50(nM) = 1.29
4803
352591492022
(CH-Mal-C11-GIVEQCCTSICSLYQLENYCN)-(FVNQHLCGSHLVEALYLVCGERGFFYTPK-C11-Mal-CH)
CH-/HPN-Conjugated Insulins (GlyA1/LysB29)50Gly1(A) Maleimide modified linked using linker C11 (N-[κ-maleimidoundecanoyloxy]- sulfosuccinimide ester, KMUS) with chondroitin [CH]K29(B) Maleimide modified linked using linker C11 (N-[κ-maleimidoundecanoyloxy]- sulfosuccinimide ester, KMUS) with chondroitin [CH]Cyclic (C6-C11 disulfide bond in A chain)LC7-C7 and C20-C19 disulfide bond between A and B chainHuman insulin analogAntidiabetesBlood samples were collected immediately before injection and at various time points up to 48 h after injection340 nmol/kg14Mice serum proteaseSandwich ELISAMice serumIn Vivohttps://pubs.acs.org/doi/10.1021/acsomega.9b00059, https://pubmed.ncbi.nlm.nih.gov/28365509/NoneEC50(nM) = 86.25
4804
352591492022
(CH-Mal-C11-GIVEQCCTSICSLYQLENYCN)-(FVNQHLCGSHLVEALYLVCGERGFFYTPK-C11-Mal-CH)
CH-/HPN-Conjugated Insulins (GlyA1/LysB29)50Gly1(A) Maleimide modified linked using linker C11 (N-[κ-maleimidoundecanoyloxy]- sulfosuccinimide ester, KMUS) with chondroitin [CH]K29(B) Maleimide modified linked using linker C11 (N-[κ-maleimidoundecanoyloxy]- sulfosuccinimide ester, KMUS) with chondroitin [CH]Cyclic (C6-C11 disulfide bond in A chain)LC7-C7 and C20-C19 disulfide bond between A and B chainHuman insulin analogAntidiabetesBlood samples were collected immediately before injection and at various time points up to 48 h after injection340 nmol/kg12.1Mice serum proteaseSandwich ELISAMice serumIn Vivohttps://pubs.acs.org/doi/10.1021/acsomega.9b00059, https://pubmed.ncbi.nlm.nih.gov/28365509/NoneEC50(nM) = 86.25
4805
352591492022
(HPN-Mal-C3-GIVEQCCTSICSLYQLENYCN)-FVNQHLCGSHLVEALYLVCGERGFFYTPK
CH-/HPN-Conjugated Insulins (GlyA1)50Gly1(A) Maleimide modified linked using linker C3 (N-[β-maleimidopropyloxy] succinimide ester, BMPS) with heparosan [HPN]FreeCyclic (C6-C11 disulfide bond in A chain)LC7-C7 and C20-C19 disulfide bond between A and B chainHuman insulin analogAntidiabetesBlood samples were collected immediately before injection and at various time points up to 48 h after injection100 nmol/kg7.3Mice serum proteaseSandwich ELISAMice serumIn Vivohttps://pubs.acs.org/doi/10.1021/acsomega.9b00059, https://pubmed.ncbi.nlm.nih.gov/28365509/NoneEC50(nM) = 6.54
4806
352591492022
GIVEQCCTSICSLYQLENYCN-(FVNQHLCGSHLVEALYLVCGERGFFYTPK-C3-Mal-HPN)
CH-/HPN-Conjugated Insulins (LysB29)50FreeK29(B) Maleimide modified linked using linker C3 (N-[β-maleimidopropyloxy] succinimide ester, BMPS) with heparosan [HPN]Cyclic (C6-C11 disulfide bond in A chain)LC7-C7 and C20-C19 disulfide bond between A and B chainHuman insulin analogAntidiabetesBlood samples were collected immediately before injection and at various time points up to 48 h after injection100 nmol/kg6.1Mice serum proteaseSandwich ELISAMice serumIn Vivohttps://pubs.acs.org/doi/10.1021/acsomega.9b00059, https://pubmed.ncbi.nlm.nih.gov/28365509/NoneEC50(nM) = 0.93
4807
352591492022
(HPN-Mal-C11-GIVEQCCTSICSLYQLENYCN)-(FVNQHLCGSHLVEALYLVCGERGFFYTPK-C3-Mal-HPN)
CH-/HPN-Conjugated Insulins (GlyA1/LysB29)50Gly1(A) Maleimide modified linked using linker C3 (N-[β-maleimidopropyloxy] succinimide ester, BMPS) with heparosan [HPN]K29(B) Maleimide modified linked using linker C3 (N-[β-maleimidopropyloxy] succinimide ester, BMPS) with heparosan [HPN]Cyclic (C6-C11 disulfide bond in A chain)LC7-C7 and C20-C19 disulfide bond between A and B chainHuman insulin analogAntidiabetesBlood samples were collected immediately before injection and at various time points up to 48 h after injection100 nmol/kg16.9Mice serum proteaseSandwich ELISAMice serumIn Vivohttps://pubs.acs.org/doi/10.1021/acsomega.9b00059, https://pubmed.ncbi.nlm.nih.gov/28365509/NoneEC50(nM) = 24.16
4808
352591492022
(HPN-Mal-C11-GIVEQCCTSICSLYQLENYCN)-FVNQHLCGSHLVEALYLVCGERGFFYTPK
CH-/HPN-Conjugated Insulins (GlyA1)50Gly1(A) Maleimide modified linked using linker C11 (N-[κ-maleimidoundecanoyloxy]- sulfosuccinimide ester, KMUS) withheparosan [HPN]FreeCyclic (C6-C11 disulfide bond in A chain)LC7-C7 and C20-C19 disulfide bond between A and B chainHuman insulin analogAntidiabetesBlood samples were collected immediately before injection and at various time points up to 48 h after injection100 nmol/kg5.6Mice serum proteaseSandwich ELISAMice serumIn Vivohttps://pubs.acs.org/doi/10.1021/acsomega.9b00059, https://pubmed.ncbi.nlm.nih.gov/28365509/NoneEC50(nM) = 8.68
4809
352591492022
GIVEQCCTSICSLYQLENYCN-(FVNQHLCGSHLVEALYLVCGERGFFYTPK-C11-Mal-HPN)
CH-/HPN-Conjugated Insulins (LysB29)50FreeK29(B) Maleimide modified linked using linker C11 (N-[κ-maleimidoundecanoyloxy]- sulfosuccinimide ester, KMUS) with heparosan [HPN]Cyclic (C6-C11 disulfide bond in A chain)LC7-C7 and C20-C19 disulfide bond between A and B chainHuman insulin analogAntidiabetesBlood samples were collected immediately before injection and at various time points up to 48 h after injection100 nmol/kg6.9Mice serum proteaseSandwich ELISAMice serumIn Vivohttps://pubs.acs.org/doi/10.1021/acsomega.9b00059, https://pubmed.ncbi.nlm.nih.gov/28365509/NoneEC50(nM) = 1.25
4810
352591492022
(HPN-Mal-C11-GIVEQCCTSICSLYQLENYCN)-(FVNQHLCGSHLVEALYLVCGERGFFYTPK-C11-Mal-HPN)
CH-/HPN-Conjugated Insulins (GlyA1/LysB29)50Gly1(A) Maleimide modified linked using linker C11 (N-[κ-maleimidoundecanoyloxy]- sulfosuccinimide ester, KMUS) withheparosan [HPN]K29(B) Maleimide modified linked using linker C11 (N-[κ-maleimidoundecanoyloxy]- sulfosuccinimide ester, KMUS) with heparosan [HPN]Cyclic (C6-C11 disulfide bond in A chain)LC7-C7 and C20-C19 disulfide bond between A and B chainHuman insulin analogAntidiabetesBlood samples were collected immediately before injection and at various time points up to 48 h after injection100 nmol/kg12.9Mice serum proteaseSandwich ELISAMice serumIn Vivohttps://pubs.acs.org/doi/10.1021/acsomega.9b00059, https://pubmed.ncbi.nlm.nih.gov/28365509/NoneEC50(nM) = 88.23
4811
352591492022
(CH-Mal-C3-GIVEQCCTSICSLYQLENYCN)-FVNQHLCGSHLVEALYLVCGERGFFYTPK
CH-/HPN-Conjugated Insulins (GlyA1)50Gly1(A) Maleimide modified linked using linker C3 (N-[β-maleimidopropyloxy] succinimide ester, BMPS) with chondroitin [CH]FreeCyclic (C6-C11 disulfide bond in A chain)LC7-C7 and C20-C19 disulfide bond between A and B chainHuman insulin analogAntidiabetesBlood samples were collected immediately before injection and at various time points up to 48 h after injection340 nmol/kg5.7Mice serum proteaseSandwich ELISAMice serumIn Vivohttps://pubs.acs.org/doi/10.1021/acsomega.9b00059, https://pubmed.ncbi.nlm.nih.gov/28365509/NoneEC50(nM) = 4.84
4812
352591492022
(CH-Mal-C3-GIVEQCCTSICSLYQLENYCN)-FVNQHLCGSHLVEALYLVCGERGFFYTPK
CH-/HPN-Conjugated Insulins (GlyA1)50Gly1(A) Maleimide modified linked using linker C3 (N-[β-maleimidopropyloxy] succinimide ester, BMPS) with chondroitin [CH]FreeCyclic (C6-C11 disulfide bond in A chain)LC7-C7 and C20-C19 disulfide bond between A and B chainHuman insulin analogAntidiabetesBlood samples were collected immediately before injection and at various time points up to 48 h after injection340 nmol/kg9.5Mice serum proteaseSandwich ELISAMice serumIn Vivohttps://pubs.acs.org/doi/10.1021/acsomega.9b00059, https://pubmed.ncbi.nlm.nih.gov/28365509/NoneEC50(nM) = 4.84
4813
352591492022
(HPN-Mal-C3-GIVEQCCTSICSLYQLENYCN)-FVNQHLCGSHLVEALYLVCGERGFFYTPK
CH-/HPN-Conjugated Insulins (GlyA1)50Gly1(A) Maleimide modified linked using linker C3 (N-[β-maleimidopropyloxy] succinimide ester, BMPS) with heparosan [HPN]FreeCyclic (C6-C11 disulfide bond in A chain)LC7-C7 and C20-C19 disulfide bond between A and B chainHuman insulin analogAntidiabetesBlood samples were collected immediately before injection and at various time points up to 48 h after injection100 nmol/kg8Mice serum proteaseSandwich ELISAMice serumIn Vivohttps://pubs.acs.org/doi/10.1021/acsomega.9b00059, https://pubmed.ncbi.nlm.nih.gov/28365509/NoneEC50(nM) = 6.54
4814
352591492022
(HPN-Mal-C3-GIVEQCCTSICSLYQLENYCN)-FVNQHLCGSHLVEALYLVCGERGFFYTPK
CH-/HPN-Conjugated Insulins (GlyA1)50Gly1(A) Maleimide modified linked using linker C3 (N-[β-maleimidopropyloxy] succinimide ester, BMPS) with heparosan [HPN]FreeCyclic (C6-C11 disulfide bond in A chain)LC7-C7 and C20-C19 disulfide bond between A and B chainHuman insulin analogAntidiabetesBlood samples were collected immediately before injection and at various time points up to 48 h after injection100 nmol/kg11.7Mice serum proteaseSandwich ELISAMice serumIn Vivohttps://pubs.acs.org/doi/10.1021/acsomega.9b00059, https://pubmed.ncbi.nlm.nih.gov/28365509/NoneEC50(nM) = 6.54
4815
352591492022
HGEGTFTSDVSSYLEGQAAKEFIAWLVKGRC
Conjugate 231FreeEthylene Diamine-modified chondroitin90 (CH) linked with C terminus of GLP-1C using linker C12 , (N-[λ-maleimidododecanoyloxy]-sulfosuccinimide ester (sulfo-LMDS, C12 derived from LMDS)LinearLNoneCH-Conjugated Glp-1C PeptideAntidiabetesBlood samples were collected from the tail vein at 0, 12, 24, 48, 72, 96, 120, and 144 h postadministration300 nmol/kg25.3 (T1/2 Elimination Half Life)ICR mice plasma proteaseELISAICR mice plasma In Vivohttps://pubs.acs.org/doi/10.1021/acsomega.9b00059, https://pubmed.ncbi.nlm.nih.gov/28365509/NoneEC50 = 9.9 nM
4816
352591492022
HGEGTFTSDVSSYLEGQAAKEFIAWLVKGRC
Conjugate 231FreeEthylene Diamine-modified chondroitin90 (CH) linked with C terminus of GLP-1C using linker C12 , (N-[λ-maleimidododecanoyloxy]-sulfosuccinimide ester (sulfo-LMDS, C12 derived from LMDS)LinearLNoneCH-Conjugated Glp-1C PeptideAntidiabetesBlood samples were collected from the tail vein at 0, 12, 24, 48, 72, 96, 120, and 144 h postadministration100 nmol/kg30.3 (T1/2 Elimination Half Life)ICR mice plasma proteaseELISAICR mice plasma In Vivohttps://pubs.acs.org/doi/10.1021/acsomega.9b00059, https://pubmed.ncbi.nlm.nih.gov/28365509/NoneEC50 = 9.9 nM
4817
352591492022
HGEGTFTSDVSSYLEGQAAKEFIAWLVKGRC
Conjugate 331FreeEthylene Diamine-modified heparosan (HPN) linked with C terminus of GLP-1C using linker C12 , (N-[λ-maleimidododecanoyloxy]-sulfosuccinimide ester (sulfo-LMDS, C12 derived from LMDS)LinearLNoneHpn-Conjugated Glp-1C PeptideAntidiabetesBlood samples were collected from the tail vein at 0, 12, 24, 48, 72, 96, 120, and 144 h postadministration300 nmol/kg33.6 (T1/2 Elimination Half Life)ICR mice plasma proteaseELISAICR mice plasma In Vivohttps://pubs.acs.org/doi/10.1021/acsomega.9b00059, https://pubmed.ncbi.nlm.nih.gov/28365509/NoneEC50 = 7.0 nM
4818
352591492022
HGEGTFTSDVSSYLEGQAAKEFIAWLVKGRC
Conjugate 331FreeEthylene Diamine-modified heparosan (HPN) linked with C terminus of GLP-1C using linker C12 , (N-[λ-maleimidododecanoyloxy]-sulfosuccinimide ester (sulfo-LMDS, C12 derived from LMDS)LinearLNoneHpn-Conjugated Glp-1C PeptideAntidiabetesBlood samples were collected from the tail vein at 0, 12, 24, 48, 72, 96, 120, and 144 h postadministration100 nmol/kg25.8 (T1/2 Elimination Half Life)ICR mice plasma proteaseELISAICR mice plasma In Vivohttps://pubs.acs.org/doi/10.1021/acsomega.9b00059, https://pubmed.ncbi.nlm.nih.gov/28365509/NoneEC50 = 7.0 nM
4819
352591492022
RKDVY
TP5-MA5FreeFreeLinearLConjugating a myristic acid-acylated lysine to a permissive site of TP5, Radiolabeling C14 at Lys2Myristic Acid-Modified Tp5Treatment Of Patients With Immunodeficiency Diseases, Such As Rheumatoid Arthritis, Cancers, Hepatitis B Virus Infection, And Acquired Immunodeficiency Syndrome (Aids)One hundred microliter plasma samples were collected at the following time intervals: 0.5, 5, 10, 20, 30, and 45 min and 1, 2, 3, 4, 6, 8,and 10 h after peptide administration.1 mg/kg1.75 ± 0.72Wistar rats plasma proteaseLC-MS/MSWistar rats plasmaIn Vivohttps://pubs.acs.org/doi/10.1021/acsomega.9b00059, https://pubmed.ncbi.nlm.nih.gov/28365509/NoneThe cytotoxicity of TP5-MA was evaluated in mice spleen lymphocytes. Cytotoxicity was not detected after treatment with different concentrations of TP5-MA and TP5 
4820
352591492022
RKDVY
TP55FreeFreeLinearLNoneSyntheticTreatment Of Patients With Immunodeficiency Diseases, Such As Rheumatoid Arthritis, Cancers, Hepatitis B Virus Infection, And Acquired Immunodeficiency Syndrome (Aids)One hundred microliter plasma samples were collected at the following time intervals: 0.5, 5, 10, 20, 30, and 45 min and 1, 2, 3, 4, 6, 8,and 10 h after peptide administration.1 mg/kg0.022 ± 0.004Wistar rats plasma proteaseLC-MS/MSWistar rats plasmaIn Vivohttps://pubs.acs.org/doi/10.1021/acsomega.9b00059, https://pubmed.ncbi.nlm.nih.gov/28365509/NoneThe cytotoxicity of TP5-MA was evaluated in mice spleen lymphocytes. Cytotoxicity was not detected after treatment with different concentrations of TP5-MA and TP5 
4821
352591492022
RKDVY
TP5-MA5FreeFreeLinearLConjugating a myristic acid-acylated lysine to a permissive site of TP5, Radiolabeling C14 at Lys2Myristic Acid-Modified Tp5Treatment Of Patients With Immunodeficiency Diseases, Such As Rheumatoid Arthritis, Cancers, Hepatitis B Virus Infection, And Acquired Immunodeficiency Syndrome (Aids)37 °CN.A.4.42Human plasma proteaseLC-MS/MS1 mg/mL human plasmaIn Vitrohttps://pubs.acs.org/doi/10.1021/acsomega.9b00059, https://pubmed.ncbi.nlm.nih.gov/28365509/NoneThe cytotoxicity of TP5-MA was evaluated in mice spleen lymphocytes. Cytotoxicity was not detected after treatment with different concentrations of TP5-MA and TP5 
4822
356514772022
Y-Aib-EGTFTSDYSI-Aib-LDKIAQKAFVQWLIAGGPSSGAPPPS
LY329817639FreeAmidationLinearLConjugated to a C20 fatty diacid moiety via a linker connected to the lysine residue at position 20 (C20 diacid-yGlu-(AEEA)2), two non-coded amino acid residues at positions 2 and 13 (Aib, α-amino isobutyric acid)Fatty Acid Modified PeptideAntidiabetesBlood samples for PK assessment of LY3298176 in the SAD part were collected at predose, 8, 24, 48, 72, 96, 120, 168, and 336 hours postdose0.25 mg116Human plasma proteaseHRAM LC/MSHuman plasmaIn Vivohttps://pubmed.ncbi.nlm.nih.gov/30473097/NoneGIPR, EC50 nM (cAMP potency) = 0.0224 
4823
356514772022
Y-Aib-EGTFTSDYSI-Aib-LDKIAQKAFVQWLIAGGPSSGAPPPS
LY329817639FreeAmidationLinearLConjugated to a C20 fatty diacid moiety via a linker connected to the lysine residue at position 20 (C20 diacid-yGlu-(AEEA)2), two non-coded amino acid residues at positions 2 and 13 (Aib, α-amino isobutyric acid)Fatty Acid Modified PeptideAntidiabetesBlood samples for PK assessment of LY3298176 in the SAD part were collected at predose, 8, 24, 48, 72, 96, 120, 168, and 336 hours postdose0.5 mg124Human plasma proteaseHRAM LC/MSHuman plasmaIn Vivohttps://pubmed.ncbi.nlm.nih.gov/30473097/NoneGIPR, EC50 nM (cAMP potency) = 0.0224 
4824
356514772022
Y-Aib-EGTFTSDYSI-Aib-LDKIAQKAFVQWLIAGGPSSGAPPPS
LY329817639FreeAmidationLinearLConjugated to a C20 fatty diacid moiety via a linker connected to the lysine residue at position 20 (C20 diacid-yGlu-(AEEA)2), two non-coded amino acid residues at positions 2 and 13 (Aib, α-amino isobutyric acid)Fatty Acid Modified PeptideAntidiabetesBlood samples for PK assessment of LY3298176 in the SAD part were collected at predose, 8, 24, 48, 72, 96, 120, 168, and 336 hours postdose1 mg106Human plasma proteaseHRAM LC/MSHuman plasmaIn Vivohttps://pubmed.ncbi.nlm.nih.gov/30473097/NoneGIPR, EC50 nM (cAMP potency) = 0.0224 
4825
356514772022
Y-Aib-EGTFTSDYSI-Aib-LDKIAQKAFVQWLIAGGPSSGAPPPS
LY329817639FreeAmidationLinearLConjugated to a C20 fatty diacid moiety via a linker connected to the lysine residue at position 20 (C20 diacid-yGlu-(AEEA)2), two non-coded amino acid residues at positions 2 and 13 (Aib, α-amino isobutyric acid)Fatty Acid Modified PeptideAntidiabetesBlood samples for PK assessment of LY3298176 in the SAD part were collected at predose, 8, 24, 48, 72, 96, 120, 168, and 336 hours postdose2.5 mg120Human plasma proteaseHRAM LC/MSHuman plasmaIn Vivohttps://pubmed.ncbi.nlm.nih.gov/30473097/NoneGIPR, EC50 nM (cAMP potency) = 0.0224 
4826
356514772022
Y-Aib-EGTFTSDYSI-Aib-LDKIAQKAFVQWLIAGGPSSGAPPPS
LY329817639FreeAmidationLinearLConjugated to a C20 fatty diacid moiety via a linker connected to the lysine residue at position 20 (C20 diacid-yGlu-(AEEA)2), two non-coded amino acid residues at positions 2 and 13 (Aib, α-amino isobutyric acid)Fatty Acid Modified PeptideAntidiabetesBlood samples for PK assessment of LY3298176 in the SAD part were collected at predose, 8, 24, 48, 72, 96, 120, 168, and 336 hours postdose5 mg123Human plasma proteaseHRAM LC/MSHuman plasmaIn Vivohttps://pubmed.ncbi.nlm.nih.gov/30473097/NoneGIPR, EC50 nM (cAMP potency) = 0.0224 
4827
356514772022
Y-Aib-EGTFTSDYSI-Aib-LDKIAQKAFVQWLIAGGPSSGAPPPS
LY329817639FreeAmidationLinearLConjugated to a C20 fatty diacid moiety via a linker connected to the lysine residue at position 20 (C20 diacid-yGlu-(AEEA)2), two non-coded amino acid residues at positions 2 and 13 (Aib, α-amino isobutyric acid)Fatty Acid Modified PeptideAntidiabetesBlood samples for PK assessment of LY3298176 in the SAD part were collected at predose, 8, 24, 48, 72, 96, 120, 168, and 336 hours postdose8 mg111Human plasma proteaseHRAM LC/MSHuman plasmaIn Vivohttps://pubmed.ncbi.nlm.nih.gov/30473097/NoneGIPR, EC50 nM (cAMP potency) = 0.0224 
4828
358075582022
Y-Aib-EGTFTSDYSI-Aib-LDKIAQKAFVQWLIAGGPSSGAPPPS
Tirzepatide39FreeAmidationLinearLC20 fatty diacid moiety at Lys20SyntheticInsulinotrophicN.A.5 mg127Human plasma proteaseN.A.Human plasma With Multiple Dose (Participants Received 5‐Mg Tirzepatide Weeks 1‐8)(Japanese Participant With Type 2 Diabetes) In Vivohttps://pubmed.ncbi.nlm.nih.gov/34647404/, https://pubmed.ncbi.nlm.nih.gov/30399314/NoneN.A.
4829
358075582022
Y-Aib-EGTFTSDYSI-Aib-LDKIAQKAFVQWLIAGGPSSGAPPPS
Tirzepatide39FreeAmidationLinearLC20 fatty diacid moiety at Lys20SyntheticInsulinotrophicN.A.10 mg135Human plasma proteaseN.A.Human plasma With Multiple Dose (Participants Received 2.5‐Mg Tirzepatide, Weeks 1‐2; 5 Mg, Weeks 3‐4; 10 Mg, Weeks 5‐8) (Japanese Participant With Type 2 Diabetes) In Vivohttps://pubmed.ncbi.nlm.nih.gov/34647404/, https://pubmed.ncbi.nlm.nih.gov/30399314/NoneN.A.
4830
358075582022
Y-Aib-EGTFTSDYSI-Aib-LDKIAQKAFVQWLIAGGPSSGAPPPS
Tirzepatide39FreeAmidationLinearLC20 fatty diacid moiety at Lys20SyntheticInsulinotrophicN.A.15 mg121Human plasma proteaseN.A.Human plasma With Multiple Dose(Participants Received 5‐Mg Tirzepatide, Weeks 1‐2; 10 Mg, Weeks 3‐6; 15 Mg, Weeks 7‐8) (Japanese Participant With Type 2 Diabetes) In Vivohttps://pubmed.ncbi.nlm.nih.gov/34647404/, https://pubmed.ncbi.nlm.nih.gov/30399314/NoneN.A.
4831
358075582022
IKPEAPGEDASPEELNRYYASLRHYLNLVTRQRY
PYY3-3634FreeFreeLinearLNoneNeuropeptide YAntidiabetes, AntiobesityThe reaction was stopped at selected time points (5, 15, 30, 60, 90, 120, 150, 180, 210, 240, 270, and 300 min)1 μM200Minipigs plasma proteaseLC-MSMinipigs plasmaIn Vitrohttps://pubmed.ncbi.nlm.nih.gov/34647404/, https://pubmed.ncbi.nlm.nih.gov/30399314/NoneKi(nM) = 40 (In Vitro Binding of Peptide Analogues against Human Y1 receptor)
4832
358075582022
IKPEAPGEDASPEELNRYYASLRHYLNLVTRQRY
PYY3−36 (methylamide)34FreeMethyl amide addition at C terminusLinearLNonePYY analogueAntidiabetes, AntiobesityThe reaction was stopped at selected time points (5, 15, 30, 60, 90, 120, 150, 180, 210, 240, 270, and 300 min)1 μM200Minipigs plasma proteaseLC-MSMinipigs plasmaIn Vitrohttps://pubmed.ncbi.nlm.nih.gov/34647404/, https://pubmed.ncbi.nlm.nih.gov/30399314/NoneKi(nM) = >10,000 (In Vitro Binding of Peptide Analogues against Human Y1 receptor)
4833
358075582022
IKPEAPGEDASPEELNRYYASLRHYLNLVTRQR-MeTyr
[MeTyr36]PYY3−3634FreeMethylated Tyr36 at C terminusLinearLNonePYY analogueAntidiabetes, AntiobesityThe reaction was stopped at selected time points (5, 15, 30, 60, 90, 120, 150, 180, 210, 240, 270, and 300 min)1 μM370Minipigs plasma proteaseLC-MSMinipigs plasmaIn Vitrohttps://pubmed.ncbi.nlm.nih.gov/34647404/, https://pubmed.ncbi.nlm.nih.gov/30399314/NoneKi(nM) = 4000 (In Vitro Binding of Peptide Analogues against Human Y1 receptor)
4834
358075582022
IKPEAPGEDASPEELNRYYASLRHYLNLVTR-MeArg-Y
[MeArg35]PYY3−3634FreeMethylated Arg35 at C terminusLinearLNonePYY analogueAntidiabetes, AntiobesityThe reaction was stopped at selected time points (5, 15, 30, 60, 90, 120, 150, 180, 210, 240, 270, and 300 min)1 μM620Minipigs plasma proteaseLC-MSMinipigs plasmaIn Vitrohttps://pubmed.ncbi.nlm.nih.gov/34647404/, https://pubmed.ncbi.nlm.nih.gov/30399314/NoneKi(nM) = 500 (In Vitro Binding of Peptide Analogues against Human Y1 receptor)
4835
358075582022
IKPEAPGEDASPEELNRYYASLRHYLNLVTR-MeGln-RY
[MeGln34]PYY3−3634FreeMethylated Gln34 at C terminusLinearLMethylated Gln34PYY analogueAntidiabetes, AntiobesityThe reaction was stopped at selected time points (5, 15, 30, 60, 90, 120, 150, 180, 210, 240, 270, and 300 min)1 μM890Minipigs plasma proteaseLC-MSMinipigs plasmaIn Vitrohttps://pubmed.ncbi.nlm.nih.gov/34647404/, https://pubmed.ncbi.nlm.nih.gov/30399314/NoneKi(nM) = 0.40 (In Vitro Binding of Peptide Analogues against Human Y1 receptor)
4836
358075582022
IKPEAPGEDASPEELNRYYASLRHYLNLVT-MeArg-QRY
[MeArg33]PYY3−3634FreeMethylated Arg33 at C terminusLinearLMethylated Arg33PYY analogueAntidiabetes, AntiobesityThe reaction was stopped at selected time points (5, 15, 30, 60, 90, 120, 150, 180, 210, 240, 270, and 300 min)1 μM200Minipigs plasma proteaseLC-MSMinipigs plasmaIn Vitrohttps://pubmed.ncbi.nlm.nih.gov/34647404/, https://pubmed.ncbi.nlm.nih.gov/30399314/NoneKi(nM) = 2500 (In Vitro Binding of Peptide Analogues against Human Y1 receptor)
4837
358075582022
IKPEAPGEDASPEELNRYYASLRHYLNLVTRQR-βhTyr
[β-homoTyr36]PYY3−3634Freeβ-homoTyr36 at C terminusLinearLNonePYY analogueAntidiabetes, AntiobesityThe reaction was stopped at selected time points (5, 15, 30, 60, 90, 120, 150, 180, 210, 240, 270, and 300 min)1 μM430Minipigs plasma proteaseLC-MSMinipigs plasmaIn Vitrohttps://pubmed.ncbi.nlm.nih.gov/34647404/, https://pubmed.ncbi.nlm.nih.gov/30399314/NoneKi(nM) = 4000 (In Vitro Binding of Peptide Analogues against Human Y1 receptor)
4838
358075582022
IKPEAPGEDASPEELNRYYASLRHYLNLVTRQ-βArg-Y
[β-homoArg35]PYY3−3634Freeβ-homoArg35 at C terminusLinearLNonePYY analogueAntidiabetes, AntiobesityThe reaction was stopped at selected time points (5, 15, 30, 60, 90, 120, 150, 180, 210, 240, 270, and 300 min)1 μM680Minipigs plasma proteaseLC-MSMinipigs plasmaIn Vitrohttps://pubmed.ncbi.nlm.nih.gov/34647404/, https://pubmed.ncbi.nlm.nih.gov/30399314/NoneKi(nM) = 6300 (In Vitro Binding of Peptide Analogues against Human Y1 receptor)
4839
358075582022
IKPEAPGEDASPEELNRYYASLRHYLNLVTR-βhGln-RY
[β-homoGln34]PYY3−3634Freeβ-homoGln34 at C terminusLinearLβ-homoGln34 modificationPYY analogueAntidiabetes, AntiobesityThe reaction was stopped at selected time points (5, 15, 30, 60, 90, 120, 150, 180, 210, 240, 270, and 300 min)1 μM1200Minipigs plasma proteaseLC-MSMinipigs plasmaIn Vitrohttps://pubmed.ncbi.nlm.nih.gov/34647404/, https://pubmed.ncbi.nlm.nih.gov/30399314/NoneKi(nM) = 160 (In Vitro Binding of Peptide Analogues against Human Y1 receptor)
4840
358075582022
IKPEAPGEDASPEELNRYYASLRHYLNLVT-βhArg-QRY
[β-homoArg33]PYY3−3634Freeβ-homoArg33 at C terminusLinearLβ-homoArg33 modificationPYY analogueAntidiabetes, AntiobesityThe reaction was stopped at selected time points (5, 15, 30, 60, 90, 120, 150, 180, 210, 240, 270, and 300 min)1 μM230Minipigs plasma proteaseLC-MSMinipigs plasmaIn Vitrohttps://pubmed.ncbi.nlm.nih.gov/34647404/, https://pubmed.ncbi.nlm.nih.gov/30399314/NoneKi(nM) = 200 (In Vitro Binding of Peptide Analogues against Human Y1 receptor)
4841
358075582022
IKPEAPGEDASPEELNRYYASLRHYLNWVTRQ-MeArg-RY
[Trp30, MeArg35]PYY3−3634FreeMeArg35 at C terminusLinearLTrp30 modification, Methylated Arg35 PYY analogueAntidiabetes, AntiobesityThe reaction was stopped at selected time points (5, 15, 30, 60, 90, 120, 150, 180, 210, 240, 270, and 300 min)1 μM980Minipigs plasma proteaseLC-MSMinipigs plasmaIn Vitrohttps://pubmed.ncbi.nlm.nih.gov/34647404/, https://pubmed.ncbi.nlm.nih.gov/30399314/NoneKi(nM) = 2500 (In Vitro Binding of Peptide Analogues against Human Y1 receptor)
4842
358075582022
IKPEAPGEDASPEELNRYYASLRHYLNWVTRQ-βhArg-Y
[Trp30,β-homoArg35]PYY3−3634Freeβ-homoArg35 at C terminusLinearLTrp30 modificationPYY analogueAntidiabetes, AntiobesityThe reaction was stopped at selected time points (5, 15, 30, 60, 90, 120, 150, 180, 210, 240, 270, and 300 min)1 μM570Minipigs plasma proteaseLC-MSMinipigs plasmaIn Vitrohttps://pubmed.ncbi.nlm.nih.gov/34647404/, https://pubmed.ncbi.nlm.nih.gov/30399314/NoneKi(nM) = 10,000 (In Vitro Binding of Peptide Analogues against Human Y1 receptor)
4843
358075582022
HAEGTFTSDVSSYLEGQAAKEFIAWLVKGRG
GLP-131FreeFreeLinearLNoneGlucagonTreatment Of Type 2 DiabetesThe reaction was stopped at selected time points (5, 15, 30, 60, 90, 120, 150, 180, 210, 240, 270, and 300 min)1 μM46Minipigs plasma proteaseLC-MSMinipigs plasmaIn Vitrohttps://pubmed.ncbi.nlm.nih.gov/34647404/, https://pubmed.ncbi.nlm.nih.gov/30399314/, PDB id: 5VAINoneN.A.
4844
350595682021
Hoo-FOP-hle-Pff-F
JPE-13757Hoo = L-hydroorotic acidAmidationLinearMixhle5 = D-homoleucine, Pff6 = Phe(4-F), Orn = Ornithine,Replaces the C-terminal Arg of PMX53 with a hydrophobic amino acidPeptidomimetic C5a receptor antagonistsC5Ar1 AntagonistsSerial blood samples were collected at 10, 15, 30, 45, and 60 min, and at 2, 4, 6, and 24 h via a tail vein 1 mg/kg0.13 (Elimination Half Life)Mice plasma proteaseLC-MSMice plasmaIn VivoNoneNoneThe inhibition of TNF levels also presented a similar median effective concentration (EC50) for PMX53 (5.9 μM) 
4845
350595682021
FOP-Cha-WR
PMX536AcetylationFreeCyclic(Orn-Arg N-C bond)Mixcha4 = D-cyclohexylalanine, O2 = OrnithinePeptidomimetic C5a receptor antagonistsC5Ar1 AntagonistsSerial blood samples were collected at 10, 15, 30, 45, and 60 min, and at 2, 4, 6, and 24 h via a tail vein 1 mg/kg1.3 (Elimination Half Life)Mice plasma proteaseLC-MSMice plasmaIn VivoNoneNoneThe inhibition of TNF levels also presented a similar median effective concentration (EC50) for JPE-1375 (4.5 μM) 
4846
350569792021
FRRG
Al-ProD4MaleimideDOXLinearLNoneAlbumin-binding maleimide and cathepsin B-cleavable peptide conjugateAntitumorblood samples were collected from mice at pre-determined times (0, 3 h, 6 h, 9 h, 12 h, 24 h, 48 h, 72 h, 96 h, 120 h, and 144 h)3 mg/kg3.1BALB/C nude mice plasma proteaseFluorescence assayBALB/c nude mice plasmaIn VivoNoneNoneThe IC50 value of HSA-bound Al-ProD in MDA-MB231 breast cancer cells is 7.33 µM, On day 20, the tumor volume in the Al-ProD-treated group was 347.42 ± 25.9 mm³, significantly smaller than the free DOX group (580.25 ± 139.92 mm³) and saline group (1810.98 ± 544.56 mm³)
4847
350367032021
CWRLRWHSPLKGM
[64Cu]CM-11364Cu labeling FreeLinearLNoneSyntheticPET Radiotracer For Cd1331 hour∼100 μCi22.4 Of Intact [64Cu]Cm-1 RemainedMouse serum proteaseradio-HPLC mouse serumIn VitroNoneNoneCM1 shows high binding affinity for CD133 (KD = 7.37 nM), 64Cu]CM-2 showed a binding affinity (IC50) of 44.95 nM, which is similar to that of [64Cu]CM-1 (IC50 = 52.55 nM)
4848
350367032021
CWRLRWHSPLKGM
[64Cu]CM-11364Cu labeling FreeLinearLNoneSyntheticPET Radiotracer For Cd1332 hour∼100 μCi20.1% Of Intact [64Cu]Cm-1 RemainedMouse serum proteaseradio-HPLC mouse serumIn VitroNoneNoneCM1 shows high binding affinity for CD133 (KD = 7.37 nM), 64Cu]CM-2 showed a binding affinity (IC50) of 44.95 nM, which is similar to that of [64Cu]CM-1 (IC50 = 52.55 nM)
4849
350367032021
CWRLRWHSPLKGM
[64Cu]CM-2146-aminohexanoic acid (Ahx) linker is anchored between the N terminus of the peptide and the (DOTA) 1,4,7,10-tetraazacyclododecane-1,4,7,10-tetraacetic acid , 64Cu labeling FreeLinearLNoneSyntheticPET Radiotracer For Cd1331 hour∼100 μCi94.9 of intact tracers remainedMouse serum proteaseradio-HPLC mouse serumIn VitroNoneNone64Cu]CM-2 showed a binding affinity (IC50) of 44.95 nM, which is similar to that of [64Cu]CM-1 (IC50 = 52.55 nM)
4850
350367032021
CWRLRWHSPLKGM
[64Cu]CM-2146-aminohexanoic acid (Ahx) linker is anchored between the N terminus of the peptide and the (DOTA) 1,4,7,10-tetraazacyclododecane-1,4,7,10-tetraacetic acid , 64Cu labeling FreeLinearLNoneSyntheticPET Radiotracer For Cd1332 hour∼100 μCi91.9% of intact tracers remainedMouse serum proteaseradio-HPLC mouse serumIn VitroNoneNone64Cu]CM-2 showed a binding affinity (IC50) of 44.95 nM, which is similar to that of [64Cu]CM-1 (IC50 = 52.55 nM)
4851
350113242021
SAVGRHGRRFGLRKHRKH
AWRK618FreeFreeLinearLNoneBased on the natural occurring peptide dybowskin-2CDYaAntimicrobialBlood samples were collected from orbital venous plexus at 0.083, 0.167, 0.25, 0.5, 1, 1.5, 2, 3, 4, 6, 8, and 10 h2.35 mg/kg2.946 ± 2.048SPF-grade male SD rats plasma proteaseLC-MS/MSSPF-grade male SD rats plasmaIn VivoNoneNoneN.A.
4852
350113242021
SAVGRHGRRFGLRKHRKH
AWRK618FreeFreeLinearLNoneBased on the natural occurring peptide dybowskin-2CDYaAntimicrobialBlood samples were collected from orbital venous plexus at 0.083, 0.167, 0.25, 0.5, 1, 1.5, 2, 3, 4, 6, 8, and 10 h4.7 mg/kg2.941 ± 1.399SPF-grade male SD rats plasma proteaseLC-MS/MSSPF-grade male SD rats plasmaIn VivoNoneNoneN.A.
4853
350113242021
SAVGRHGRRFGLRKHRKH
AWRK618FreeFreeLinearLNoneBased on the natural occurring peptide dybowskin-2CDYaAntimicrobialBlood samples were collected from orbital venous plexus at 0.083, 0.167, 0.25, 0.5, 1, 1.5, 2, 3, 4, 6, 8, and 10 h9.4 mg/kg2.781 ± 1.021SPF-grade male SD rats plasma proteaseLC-MS/MSSPF-grade male SD rats plasmaIn VivoNoneNoneN.A.
4854
350113242021
SAVGRHGRRFGLRKHRKH
AWRK618FreeFreeLinearLNoneBased on the natural occurring peptide dybowskin-2CDYaAntimicrobialBlood samples were collected from orbital venous plexus at 0.083, 0.167, 0.25, 0.5, 1, 1.5, 2, 3, 4, 6, 8, and 10 h4.7 mg/kg1.983 ± 0.583SPF-grade male SD rats plasma proteaseLC-MS/MSSPF-grade male SD rats plasmaIn VivoNoneNoneN.A.
4855
348593812021
pGlu-WNLNAAGYLLATHACG
M89b17pGlu = Pyroglutamate at position 1FreeLinearLNonegalanin analogInteracts With Different G Protein-Coupled Receptors>23 hours10 µM 40% Of M89B Had Been DegradedRats serum proteaseHPLCRats serumIn VitroNoneNoneEC50 ratios to Gal-(1-15)(n) = NA(3) (in GAL1R) (B-Arrestin), EC50 ratios to Gal-(1-15)(n) = NA(3) (in GAL1R) (Ca-efflux)
4856
348593812021
GWTLNSAGYLLGPHL
GAL-(1–15)15FreeFreeLinearLNoneisolated from the porcine intestineInteracts With Different G Protein-Coupled Receptors>30 minutes10 µM 80% Of Gal-(1–15) Was DegradedRats serum proteaseHPLCRats serumIn VitroNoneNoneEC50 ratios to Gal-(1-15)(n) = 1.7(3) (in GAL2R) (B-Arrestin), EC50 ratios to Gal-(1-15)(n) = 1.4(3) (in GAL2R) (Ca-efflux)
4857
347071782021
IKPEAPGEDASPEELNRYYASLRHYLNLVTRQRY
PYY3-36 analogues 134FreeAmidationLinearLNoneDerived from PYYAntiobesityBlood samples (0.8 ml) were taken either from the jugular vein using vacutainer or from the IV catheter not used for dosing according to one of the following schedules: Predose, and 5, 15, 30, 45 min, 1 h, 1.5 h, 2 h, 3 h, 4 h, 6 h, 8 h, 10 h, 24 h, 48 h, 72 h,96 h, 120 h, 168 h, 192 h, 216 h, 240 h, 264 h and 288 h post dosing; or Predose, and 5, 30 min, 1 h, 2 h, 4 h, 7 h, 11 h, 24 h, 48 h, 72 h,96 h, 120 h, 168 h, 216 h, 264 h post dosing15 nmol/kg17Male göttingen minipigs plasma proteaseLC-MSMale göttingen minipigs plasma In VivoNoneNoneEC50(nM) = 0.6 for Y2 receptor
4858
347071782021
IKPEAPGEDASPEELNRYYASLRHYLNLVTRQRY
PYY3-36 analogues 234FreeAmidationLinearLFatty acid conjugation at position 4 (C18 diacid-γGlu-2xAdo)Derived from PYYAntiobesityBlood samples (0.8 ml) were taken either from the jugular vein using vacutainer or from the IV catheter not used for dosing according to one of the following schedules: Predose, and 5, 15, 30, 45 min, 1 h, 1.5 h, 2 h, 3 h, 4 h, 6 h, 8 h, 10 h, 24 h, 48 h, 72 h,96 h, 120 h, 168 h, 192 h, 216 h, 240 h, 264 h and 288 h post dosing; or Predose, and 5, 30 min, 1 h, 2 h, 4 h, 7 h, 11 h, 24 h, 48 h, 72 h,96 h, 120 h, 168 h, 216 h, 264 h post dosing15 nmol/kg14Male göttingen minipigs plasma proteaseLC-MSMale göttingen minipigs plasma In VivoNoneNoneEC50(nM) = 10 for Y2 receptor
4859
347071782021
IKPEAPGEDASPEELNRYYASLRHYLNLVTRQRY
PYY3-36 analogues 334FreeAmidationLinearLFatty acid conjugation at position 5Derived from PYYAntiobesityN.A.15 nmol/kg8.8Male göttingen minipigs plasma proteaseLC-MSMale göttingen minipigs plasma In VivoNoneNoneEC50(nM) = 25 for Y2 receptor
4860
347071782021
IKPEAPGEDASPEELNRYYASLRHYLNLVTRQRY
PYY3-36 analogues 734FreeAmidationLinearLFatty acid conjugation at position 9Derived from PYYAntiobesityN.A.15 nmol/kg12Male göttingen minipigs plasma proteaseLC-MSMale göttingen minipigs plasma In VivoNoneNoneEC50(nM) = 40 for Y2 receptor
4861
347071782021
IKPEAPGEDASPEELNRYYASLRHYLNLVTRQRY
PYY3-36 analogues 834FreeAmidationLinearLFatty acid conjugation at position 10Derived from PYYAntiobesityN.A.15 nmol/kg8.4Male göttingen minipigs plasma proteaseLC-MSMale göttingen minipigs plasma In VivoNoneNoneEC50(nM) = 13 for Y2 receptor
4862
347071782021
IKPEAPGEDASPEELNRYYASLRHYLNLVTRQRY
PYY3-36 analogues 934FreeAmidationLinearLFatty acid conjugation at position 11Derived from PYYAntiobesityN.A.15 nmol/kg11Male göttingen minipigs plasma proteaseLC-MSMale göttingen minipigs plasma In VivoNoneNoneEC50(nM) = 1.3 for Y2 receptor
4863
347071782021
IKPEAPGEDASPEELNRYYASLRHYLNLVTRQRY
PYY3-36 analogues 1134FreeAmidationLinearLFatty acid conjugation at position 13Derived from PYYAntiobesityN.A.15 nmol/kg13Male göttingen minipigs plasma proteaseLC-MSMale göttingen minipigs plasma In VivoNoneNoneEC50(nM) = 16 for Y2 receptor
4864
347071782021
IKPEAPGEDASPEELNRYYASLRHYLNLVTRQRY
PYY3-36 analogues 2034FreeAmidationLinearLFatty acid conjugation at position 22Derived from PYYAntiobesityN.A.15 nmol/kg36Male göttingen minipigs plasma proteaseLC-MSMale göttingen minipigs plasma In VivoNoneNoneEC50(nM) = 4 for Y2 receptor
4865
347071782021
IKPEAPGEDASPEELNRYYASLRHYLNLVTRQRY
PYY3-36 analogues 2134FreeAmidationLinearLFatty acid conjugation at position 23Derived from PYYAntiobesityN.A.15 nmol/kg19Male göttingen minipigs plasma proteaseLC-MSMale göttingen minipigs plasma In VivoNoneNoneEC50(nM) = 2 for Y2 receptor
4866
347071782021
IKPEAPGEDASPEELNRYYASLRHYLNLVTRQRY
PYY3-36 analogues 2734FreeAmidationLinearLFatty acid conjugation at position 29Derived from PYYAntiobesityN.A.15 nmol/kg39Male göttingen minipigs plasma proteaseLC-MSMale göttingen minipigs plasma In VivoNoneNoneEC50(nM) = 32 for Y2 receptor
4867
347071782021
IKPEAPGEDASPEELNRYYASLRHYLNLVTRQRY
PYY3-36 analogues 2834FreeAmidationLinearLFatty acid conjugation at position 30Derived from PYYAntiobesityN.A.15 nmol/kg76Male göttingen minipigs plasma proteaseLC-MSMale göttingen minipigs plasma In VivoNoneNoneEC50(nM) = 500 for Y2 receptor
4868
347071782021
IKPEAPGEDASPEELNRYYASLRHYLNLVTRQRY
PYY3-36 analogues 3134FreeAmidationLinearLFatty acid conjugation at position 33Derived from PYYAntiobesityN.A.15 nmol/kg56Male göttingen minipigs plasma proteaseLC-MSMale göttingen minipigs plasma In VivoNoneNoneEC50(nM) = 50 for Y2 receptor
4869
347071782021
IKPEAPGEDASPEELNRYYASLRHYLNLVTRQRY
PYY3-36 analogues 3334FreeAmidationLinearLFatty acid conjugation at position 35Derived from PYYAntiobesityN.A.15 nmol/kg67Male göttingen minipigs plasma proteaseLC-MSMale göttingen minipigs plasma In VivoNoneNoneN.A.
4870
347071782021
IKPEAPGEDASPEELNRYYASLRHYLNLVTRQRY
PYY3-36 analogues 3434FreeAmidationLinearLFatty acid conjugation at position 30Derived from PYYAntiobesityN.A.15 nmol/kg4Male göttingen minipigs plasma proteaseLC-MSMale göttingen minipigs plasma In VivoNoneNoneN.A.
4871
347071782021
IKPEAPGEDASPEELNRYYASLRHYLNLVTRQRY
PYY3-36 analogues 3534FreeAmidationLinearLFatty acid conjugation at position 30Derived from PYYAntiobesityN.A.15 nmol/kg28Male göttingen minipigs plasma proteaseLC-MSMale göttingen minipigs plasma In VivoNoneNoneN.A.
4872
347071782021
IKPEAPGEDASPEELNRYYASLRHYLNLVTRQRY
PYY3-36 analogues 3634FreeAmidationLinearLFatty acid conjugation at position 30Derived from PYYAntiobesityN.A.15 nmol/kg99Male göttingen minipigs plasma proteaseLC-MSMale göttingen minipigs plasma In VivoNoneNoneN.A.
4873
347071782021
IKPEAPGEDASPEELNRYYASLRHYLNLVTRQRY
PYY3-36 analogues 3734FreeAmidationLinearLFatty acid conjugation at position 30Derived from PYYAntiobesityN.A.15 nmol/kg2Male göttingen minipigs plasma proteaseLC-MSMale göttingen minipigs plasma In VivoNoneNoneN.A.
4874
347071782021
IKPEAPGEDASPEELNRYYASLRHYLNLVTRQRY
PYY3-36 analogues 3834FreeAmidationLinearLFatty acid conjugation at position 30Derived from PYYAntiobesityN.A.15 nmol/kg4Male göttingen minipigs plasma proteaseLC-MSMale göttingen minipigs plasma In VivoNoneNoneN.A.
4875
347071782021
IKPEAPGEDASPEELNRYYASLRHYLNLVTRQRY
PYY3-36 analogues 3934FreeAmidationLinearLFatty acid conjugation at position 30Derived from PYYAntiobesityN.A.15 nmol/kg13Male göttingen minipigs plasma proteaseLC-MSMale göttingen minipigs plasma In VivoNoneNoneN.A.
4876
347071782021
IKPEAPGEDASPEELNRYYASLRHYLNLVTRQRY
PYY3-36 analogues 4034FreeAmidationLinearLFatty acid conjugation at position 30Derived from PYYAntiobesityN.A.15 nmol/kg20Male göttingen minipigs plasma proteaseLC-MSMale göttingen minipigs plasma In VivoNoneNoneN.A.
4877
347071782021
IKPEAPGEDASPEELNRYYASLRHYLNLVTRQRY
PYY3-36 analogues 4134FreeAmidationLinearLFatty acid conjugation at position 30Derived from PYYAntiobesityN.A.15 nmol/kg97Male göttingen minipigs plasma proteaseLC-MSMale göttingen minipigs plasma In VivoNoneNoneN.A.
4878
347071782021
IKPEAPGEDASPEELNRYYASLRHYLNLVTRQRY
PYY3-36 analogues 4234FreeAmidationLinearLFatty acid conjugation at position 30Derived from PYYAntiobesityN.A.15 nmol/kg75Male göttingen minipigs plasma proteaseLC-MSMale göttingen minipigs plasma In VivoNoneNoneN.A.
4879
347071782021
IKPEAPGEDASPEELNRYYASLRHYLNLVTRQRY
PYY3-36 analogues 4334FreeAmidationLinearLFatty acid conjugation at position 30Derived from PYYAntiobesityN.A.15 nmol/kg78Male göttingen minipigs plasma proteaseLC-MSMale göttingen minipigs plasma In VivoNoneNoneN.A.
4880
347071782021
IKPEAPGEDASPEELNRYYASLRHYLNLVTRQRY
PYY3-36 analogues 4434FreeAmidationLinearLFatty acid conjugation at position 30Derived from PYYAntiobesityN.A.15 nmol/kg0.5Male göttingen minipigs plasma proteaseLC-MSMale göttingen minipigs plasma In VivoNoneNoneN.A.
4881
347071782021
I-MeArg-PEAPGEDASPEELNRYYASLRHYLNLVTRQRY
PYY3-36 analogues 4534FreeAmidationLinearLFatty acid conjugation at position 4, MeArg4Derived from PYYAntiobesityN.A.15 nmol/kg83Male göttingen minipigs plasma proteaseLC-MSMale göttingen minipigs plasma In VivoNoneNoneN.A.
4882
347071782021
IKPEAPGEDASPEELNRYYASLRHYLNAKVTRQRY
PYY3-36 analogues 4635FreeAmidationLinearLFatty acid conjugation at position 30Derived from PYYAntiobesityN.A.15 nmol/kg84Male göttingen minipigs plasma proteaseLC-MSMale göttingen minipigs plasma In VivoNoneNoneN.A.
4883
347071782021
IKPEAPGEDASPEELNRYYASLRHYLNAKVTRQRY
PYY3-36 analogues 4735FreeAmidationLinearLFatty acid conjugation at position 30Derived from PYYAntiobesityN.A.15 nmol/kg62Male göttingen minipigs plasma proteaseLC-MSMale göttingen minipigs plasma In VivoNoneNoneN.A.
4884
347071782021
IKPEAPGEDASPEELNRYYASLRHYLNNKVTRQRY
PYY3-36 analogues 4835FreeAmidationLinearLFatty acid conjugation at position 30Derived from PYYAntiobesityN.A.15 nmol/kg104Male göttingen minipigs plasma proteaseLC-MSMale göttingen minipigs plasma In VivoNoneNoneN.A.
4885
347071782021
IKPEAPGEDASPEELNRYYASLRHYLNAKVTRQRY
PYY3-36 analogues 4935FreeAmidationLinearLFatty acid conjugation at position 30, Acetylation at Asn28Derived from PYYAntiobesityN.A.15 nmol/kg113Male göttingen minipigs plasma proteaseLC-MSMale göttingen minipigs plasma In VivoNoneNoneN.A.
4886
347071782021
IKPEAPGEDASPEELNRYYASLRHYLNRKVTRQRY
PYY3-36 analogues 5035FreeAmidationLinearLFatty acid conjugation at position 30, Acetylation at Asn28Derived from PYYAntiobesityN.A.15 nmol/kg120Male göttingen minipigs plasma proteaseLC-MSMale göttingen minipigs plasma In VivoNoneNoneN.A.
4887
347071782021
IKPEAPGEDASPEELNRYYASLRHYLNANKVTRQRY
PYY3-36 analogues 5136FreeAmidationLinearLFatty acid conjugation at position 30, Acetylation at Asn28Derived from PYYAntiobesityN.A.15 nmol/kg114Male göttingen minipigs plasma proteaseLC-MSMale göttingen minipigs plasma In VivoNoneNoneN.A.
4888
347071782021
IKPEAPGEDASPEELNRYYASLRHYLNRQKVTRQRY
PYY3-36 analogues 5236FreeAmidationLinearLFatty acid conjugation at position 30, Acetylation at Asn28Derived from PYYAntiobesityN.A.15 nmol/kg79Male göttingen minipigs plasma proteaseLC-MSMale göttingen minipigs plasma In VivoNoneNoneEC50(nM) = 30 for Y2 receptor
4889
346613902021
VVGSPSAQDEASPLS
VVGS peptide15FreeFreeLinearLNoneSyntheticTargets tropoelastinAliquots (6 μL) taken after 0, 35, and 120 min 0.6 mM which is diluted in water at a final concentration of 0.06 mM when aliquoting45Pooled serum protease from human male AB plasmaRP-HPLC50% pooled serum from human male AB plasmaIn VitroNoneNoneKD (μM) = 41 ± 12 ( Interaction between Immobilized Human Recombinant Tropoelastin and Gd4TESMA)
4890
346613902021
KKK-Mal-CVVGSPSAQDEASPLS
Gd4-TESMA19Gd4FreeLinearLMal links KKK and other peptideSyntheticFor imaging Atherosclerotic Plaque vulnerability2 hours0.6 mM which is diluted in water at a final concentration of 0.06 mM when aliquotingNo DegradationPooled serum protease from human male AB plasmaRP-HPLC50% pooled serum from human male AB plasmaIn VitroNoneNoneKD (μM) = 41 ± 12 ( Interaction between Immobilized Human Recombinant Tropoelastin and Gd4TESMA)
4891
346303782021
LAEAKVLANRELDKYGVSDYYKNLINNAKTVEGVKALIDEILAALPGPVEDAITAAIGRVADTVGTGPTNSEAIPALTAAETGHTSQVVPGDTMQTRHVKNYHSRSESTIENFLCRSACVYFTEYENSGAKRYAEWVLTPRQAAQLRRKLEFFTYVRFDLELTFVITSTQQPSTTQNQDAQILTHQIMYVPPGGPVPDKVDSYVWQTSTNPSVFWTEGNAPPRMSIPFLSIGNAYSNFYDGWSEFSRNGVYGINTLNNMGTLYARHVNAGSTGPIKSTIRIYFKPKHVKAWIPRPPRLCQYEKAKNVNFQPSGVTTTRQSITTMTNTGAF
ABD-VP1330ABDFreeLinearLNoneSyntheticTreatment of Coxsackievirus B3 (Cvb3)-Induced Viral Myocarditis 1h at RT0.25 μg/μL280Murine serum proteaseELISAMurine serumIn VivoNoneNoneABD-VP1 increased the 28-day survival rate from about 40% (VP1) to 73%
4892
346303782021
GPVEDAITAAIGRVADTVGTGPTNSEAIPALTAAETGHTSQVVPGDTMQTRHVKNYHSRSESTIENFLCRSACVYFTEYENSGAKRYAEWVLTPRQAAQLRRKLEFFTYVRFDLELTFVITSTQQPSTTQNQDAQILTHQIMYVPPGGPVPDKVDSYVWQTSTNPSVFWTEGNAPPRMSIPFLSIGNAYSNFYDGWSEFSRNGVYGINTLNNMGTLYARHVNAGSTGPIKSTIRIYFKPKHVKAWIPRPPRLCQYEKAKNVNFQPSGVTTTRQSITTMTNTGAF
VP1 vaccine284FreeFreeLinearLNoneSyntheticTreatment of Coxsackievirus B3 (Cvb3)-Induced Viral Myocarditis 1h at RT0.25 μg/μL<15Murine serum proteaseELISAMurine serumIn VivoNoneNoneABD-VP1 increased the 28-day survival rate from about 40% (VP1) to 73%
4893
345755812021
OP-(d-Cha)-WR
C5a receptor 1 antagonist (PMX205)5HC = Hydrocinnamate, O1: ornithineFreeCyclicMixD-Cha3: cyclohexylalanineLipophilic analogue of PMX53Treatment of Inflammatory Bowel Disease, Amyotrophic Lateral Sclerosis, Allergic Asthma, And Spinal Cord InjuryBlood samples were collected at 0.04, 0.25, 0.5, 0.75, 1, 1.5, 1, 4, 6, and 24 h for both groups and then 48, 72, 96, and 120 h1 mg/kg0.84 (Terminal Elmination Half Life)Mice plasma proteaseLC-MS/MS Mice plasmaIn VivoNoneNoneIC50 = 31 nM for PMX205
4894
345755812021
OP-(d-Cha)-WR
C5a receptor 1 antagonist (PMX205)5HC = Hydrocinnamate, O1: ornithineFreeCyclicMixD-Cha3: cyclohexylalanineLipophilic analogue of PMX53Treatment of Inflammatory Bowel Disease, Amyotrophic Lateral Sclerosis, Allergic Asthma, And Spinal Cord InjurySamples (n = 4) were quenched at regular intervals of 5 min, 10 min, 15 min, 30 min and 60 min 1 µg/ml0.17 (Elimination Half Life)Mice plasma proteaseLC-MS/MS Mice plasmaIn VivoNoneNoneIC50 = 31 nM for PMX205
4895
345755812021
OP-(d-Cha)-WR
C5a receptor 1 antagonist (PMX205)5HC = Hydrocinnamate, O1: ornithineFreeCyclicMixD-Cha3: cyclohexylalanineLipophilic analogue of PMX53Treatment of Inflammatory Bowel Disease, Amyotrophic Lateral Sclerosis, Allergic Asthma, And Spinal Cord InjuryBlood sample was collected at 2.5, 5, 10, 15, 30, 45, 60, and 90 min1 μg/mL0.33 (Elimination Half Life)Mice spinal cord homogenate proteaseLC-MS/MS Mice spinal cord homogenateIn VivoNoneNoneIC50 = 31 nM for PMX205
4896
345061382021
H-Aib-QGTFTSDYSKYLDSRRAQDFVQWL-X1-T
α/sulfono-γ-AApeptide hybrid analogue 1535FreeAmidationLinearLSubstitution of L-serine at position 2 with α-aminoisobutyric acid (Aib), X1 = Structure given in paperα/Sulfono-γ-AApeptide Hybrid Analogues of Glucagon Regulating glucose homeostasis blood samples were obtained at 15 min, 30 min, 1 h, 2 h, 4 h, 8 h, and 24 h after injection5 mg/kg~4C57Bl/6J female mice plasma proteaseLC-MS/MSC57BL/6J female mice plasmaIn VivoNoneNoneEC50 (nM) = 0.86 (Bioactivity of α/Sulfono-γ-AApeptide Hybrid Analogues in Cre Luc Production Functional Assay)
4897
344590352021
PFSTQDTDLDLEMLAPYIPMDDDFQLRSFDQLSP
FLAGHIF1α 34FreeFreeLinearLFLAG tagHypoxia-Inducible Factor 1-alphaRole in survival, metabolism, and angiogenesisN.A.N.A.~50% IncreaseCells lysate proteaseCHX assay, Western blottingHEK293 Flp‐In T‐REx cell lysate after pevonedistat treatmentIn VitroPDB id: 1LQBNoneN.A.
4898
344590352021
EFKLELVEKLFAEDTEAKNPFSTQDTDLDLEMLAPYIPMDDDFQLRSFDQLSPLESSSASPESASPQSTVTVFQQTQIQEPTANATTTTATTDELKTVTKDRMEDIKILIASPSPTHIHKETT
CODD120FreeFreeLinearLFLAG tagC-Terminal oxygen-dependent degradation domainRegulates gene expressionN.A.N.A.5.8‐Fold Increase Cells lysate proteaseCHX assay, Western blottingHEK293 Flp‐In T‐REx cells lysate after neddylation inhibitionIn VitroNoneNoneN.A.
4899
344550102021
pGlu-RPVNLTMRRKLRKHNCLQRRCMPLHSRVPFP
ELA-3232pGlu = PyroglutamateFreeCyclic (Cys-Cys Disulfide Bond)LNoneDerived from ZebrafishAnticancer, Treatment of Cardiovascular DiseaseBlood sample were withdrawn at time points: 0, 2, 5, 10, 15, 30, 60, 120, 240 min5 μg/mL47.2 ± 5.7Human plasma proteaseLC–MS/MS Human plasmaIn VitroNoneNoneN.A.
4900
344550102021
pGlu-RPVNLTMRRKLRKHNCLQRRCMPLHSRVPFP
ELA-3232pGlu = PyroglutamateFreeCyclic (Cys-Cys Disulfide Bond)LNoneDerived from ZebrafishAnticancer, Treatment of Cardiovascular DiseaseBlood sample were withdrawn at time points: 0, 2, 5, 10, 15, 30, 60, 120 min5 μg/mL44.2 ± 3Human kidney homogenate proteaseLC–MS/MS Human kidney homogenate In VitroNoneNoneN.A.
4901
344502232021
HGEGTFTSNVSSYLEGQAAKEFIAWLVKGRG
GLP-2DARPin31Genetic fusion of modified GLP-1 to the N-terminal of DARPins through a flexible linke (GGGGS)3 further DARPin linked with another DARPin using PT-linkerFreeLinearLFITC labeledGLP-1 analogsAntidiabetesAt 0.5, 2, 4, 7, 10, 24, 36, 48 and 72 h after injection, 20 μL of blood was collected 2 mg/mL52.3 ± 4.6Mice plasma proteaseFluorescence assayMice plasmaIn VivoNoneNoneGlucose-lowering effect of GLP-DARPin was more potent than that of GLP-2DARPin, EC50 of GLP-2DARPin was 0.51 ± 0.04 nM
4902
344502232021
HGEGTFTSNVSSYLEGQAAKEFIAWLVKGRG
GLP-DARPin31Genetic fusion of modified GLP-1 to the N-terminal of DARPins through a flexible linke (GGGGS)3FreeLinearLFITC labeledGLP-1 analogsAntidiabetesAt 0.5, 2, 4, 7, 10, 24, 36, 48 and 72 h after injection, 20 μL of blood was collected 2 mg/mL18.0 ± 2.8Mice plasma proteaseFluorescence assayMice plasmaIn VivoNoneNoneGlucose-lowering effect of GLP-DARPin was more potent than that of GLP-2DARPin, EC50 of GLP-2DARPin was 9.06 ± 0.15 nM
4903
344021972021
HGDGSFSDEMNTILDNLAARDFINWLIQTKITD
Teduglutide33FreeFreeLinearLNoneGLP-2 analogueTreatment of Short Bowel Syndrome N.A.0.05 mg/kg1.1Human plasma protease N.A.Human adult plasma (in Japanese patients with SBS)In VivoDB id: DB08900NoneN.A.
4904
344021972021
HGDGSFSDEMNTILDNLAARDFINWLIQTKITD
Teduglutide33FreeFreeLinearLNoneGLP-2 analogueTreatment of Short Bowel Syndrome N.A.0.05 mg/kg1.24Human plasma protease N.A.Human adult plasma (in Non-Japanese patients with SBS)In VivoDB id: DB08900NoneN.A.
4905
344021972021
HGDGSFSDEMNTILDNLAARDFINWLIQTKITD
Teduglutide33FreeFreeLinearLNoneGLP-2 analogueTreatment of Short Bowel Syndrome N.A.0.05 mg/kg0.89Human plasma protease N.A.Human pediatrics plasma (in Japanese patients with SBS)In VivoDB id: DB08900NoneN.A.
4906
344021972021
HGDGSFSDEMNTILDNLAARDFINWLIQTKITD
Teduglutide33FreeFreeLinearLNoneGLP-2 analogueTreatment of Short Bowel Syndrome N.A.0.05 mg/kg1Human plasma protease N.A.Human pediatrics plasma (in non - Japanese patients with SBS)In VivoDB id: DB08900NoneN.A.
4907
343937942021
KFRRQRPRLSHLGPMPF
LIT01-19617Fluorocarbon chain (CF3(CF2)7(CH2)2C(O)) attached to the N-terminal part of K17FFreeLinearLNoneApelin-17 AnalogTreatment of HypertensionN.A.15 nmol/kg156Rats plasma proteaseRIARats plasma In VivoPubchem CID Apelin: 56841713NoneIC50 = 0.56 ± 0.04 nmol/l for LIT01-196
4908
343937942021
KFRRQRPRLSHLGPMPF
K17F17FreeFreeLinearLNoneApelin-17 AnalogTreatment of HypertensionN.A.250 nmol/kg50Rats plasma proteaseRIARats plasma In VivoPubchem CID Apelin: 56841713NoneIC50: 0.11 ± 0.01 nmol/l for K17F
4909
343937942021
KFRRQRPRLSHLGPMPF
LIT01-19617Fluorocarbon chain (CF3(CF2)7(CH2)2C(O)) to the N-terminal part of K17FFreeLinearLNoneApelin-17 AnalogTreatment of HypertensionN.A.900 nmol/kg28Rats plasma proteaseRIARats plasma In VivoPubchem CID Apelin: 56841713NoneIC50 = 0.56 ± 0.04 nmol/l for LIT01-196
4910
343581222021
GGGGDRVYIHPF
AT1-HSA-MRN-NPs12FreeHSA linked through PEG4LinearLNoneSyntheticTreatment of Cardiovascular Disease Blood was collected from the jugular vein at the following timepoints: 0, 5, 15, 30, 45, 60, 120, and 360 min50 μg/kg101.3Rats plasma proteaseHPLCRats plasma In VivoNoneNoneN.A.
4911
342541012021
GG
Glycylglycine model dipeptide2FreeFreeLinearLNoneSyntheticN.A.60 °C and pD 7.4Equimolar amounts of Hf-NU-1000 and GG231N.A.1H-NMREquimolar amounts of Hf-NU-1000 (Metal-organic Framework)(Hf6O8-based NU-1000) and GGIn VitroNoneNoneA glycylglycine model dipeptide was hydrolysed with a rate constant of kobs = 8.33 × 10−7 s−1
4912
342066312021
YGGFL
Leu-ENK5FreeFreeLinearLNoneOpioid peptideAnalgesicAliquot (95 µL) was taken at 0, 5, 15, 60, and 300 min315 µmol/L25Mice plasma proteaseUPLCMice dipotassium ethylenediaminetetraacetic acid containing pooled plasmaIn VitroNoneNoneN.A.
4913
342066312021
YGGFL
KK 1036N terminal of Tyr linked with NH bond with R1 = Structure given in paper FreeLinearLNoneSyntheticAnalgesicAliquot (95 µL) was taken at 0, 5, 15, 60, and 300 min315 µmol/L37Mice plasma proteaseUPLCMice dipotassium ethylenediaminetetraacetic acid containing pooled plasmaIn VitroNoneNoneN.A.
4914
342066312021
YGGFL
KK 1036N terminal of Tyr linked with NH bond with R1 = Structure given in paper FreeLinearLNoneSyntheticAnalgesicAliquot (95 µL) was taken at 0, 5, 15, 60, and 300 min315 µmol/L>95% RemainedCSF ProteaseUPLCPooled human cerebrospinal fluidIn VitroNoneNoneN.A.
4915
342066312021
YGGFL
Leu-ENK5FreeFreeLinearLNoneOpioid peptideAnalgesicAliquot (95 µL) was taken at 0, 5, 15, 60, and 300 min315 µmol/L>80% RemainedCSF ProteaseUPLCPooled human cerebrospinal fluidIn VitroNoneNoneN.A.
4916
342013982021
KRRVRWIIW
optP79FreeFreeLinearLNoneSyntheticAntimicrobialFor 0, 0.5, 1, 3, 6, and 24 h at 37 °C100 μM13Human serum proteaseUPLC-MS Human serumIn VitroNoneNoneMIC(µM) = 3 for Pseudomonas aeruginosa in growth media MH,MIC(µM) = 0.8 for E.coli in growth media MH,MIC(µM) = 1.5 for K. pneumoniae in growth media MH,MIC(µM) = 1.5 for A. baumannii in growth media MH,MIC(µM) = 0.8 for VRE in growth media MH,MIC(µM) = 6 for MRSA in growth media MH
4917
342013982021
CAAKRRVRWIIWAAC
c-optP715FreeFreeCyclic(Cys1-Cys15)LAll Alanine replaced by β-alanine SyntheticAntimicrobialFor 0, 0.5, 1, 3, 6, and 24 h at 37 °C100 μM9Human serum proteaseUPLC-MS Human serumIn VitroNoneNoneMIC(µM) = 142 for Pseudomonas aeruginosa in growth media MH,MIC(µM) = 71 for E.coli in growth media MH,MIC(µM) > 142 for K. pneumoniae in growth media MH,MIC(µM) = ND for A. baumannii in growth media MH,MIC(µM) > 142 for VRE in growth media MH,MIC(µM) = 142 for MRSA in growth media MH
4918
342013982021
PKILKKCRRDSDCPGACICRGNGYCKRRVRWIIWC
[L6-optP7]-Mco35FreeFreeCyclic(Cys-Cys Multiple Disulfide Loops)LNoneSyntheticAntimicrobialFor 0, 0.5, 1, 3, 6, and 24 h at 37 °C100 μM435Human serum proteaseUPLC-MS Human serumIn VitroNoneNoneMIC(µM) = 62 for Pseudomonas aeruginosa in growth media MH,MIC(µM) = 62 for E.coli in growth media MH,MIC(µM) = 62 for K. pneumoniae in growth media MH,MIC(µM) = 62 for A. baumannii in growth media MH,MIC(µM) > 62 for VRE in growth media MH,MIC(µM) > 62 for MRSA in growth media MH
4919
341633522021
YHPYKEIEQLIELANYQVLS
OPT20FreeFreeLinearLNoneDerived from the QKHPD-containing region of NCX1Binds To Pser68-PlmAliquots of 50 μl were collected at different time points (0–48 h)300 μM0.86Human serum proteaseMass spectrometryHuman serum In VitroNoneNoneN.A.
4920
341633522021
NMP-YKEIEQLIELANYQV
NOPT16OPT substituted with an N-methyl proline at position 1FreeLinearLNoneDerived from OPTBinds To Pser68-PlmAliquots of 50 μl were collected at different time points (0–48 h)300 μM14.9Human serum proteaseMass spectrometryHuman serum In VitroNoneNoneN.A.
4921
341224002021
RFGRFLRKIRRFRPKVTITIQGSARFG
CATH227FreeFreeLinearLNoneCationic chicken heterophil-derived peptideImmunomodulatory15 min at 37°C10 µg/mL302 ± 34.5Human serum proteaseHPLCHuman serum In VitroNoneNoneThe cytotoxicity of CbTP was lower than that of parental peptide CATH2
4922
341224002021
RKDVY
TP55FreeFreeLinearLNonederived from thymopoietinImmunomodulatory15 min at 37°C10 µg/mL3.2 ± 0.5Human serum proteaseHPLCHuman serum In VitroNoneNoneThe cytotoxicity of CbTP was lower than that of parental peptide CATH2
4923
341224002021
RFGRFLRKIRRFRRKDVY
CbTP18FreeTP5 conjugationLinearLNoneA hybrid peptide combining TP5 and fragments of CATH2Immunomodulatory15 min at 37°C10 µg/mL353 ± 41.3Human serum proteaseHPLCHuman serum In VitroNoneNoneCbTP induced cytotoxicity in a dose-dependent manner, while even a high dose (80 µg/mL) of CbTP was nontoxic to RAW264.7 cells
4924
340642912021
RGDfK
111In-DOTA-EB-cRGDfK5Radiolabelled with 111ln, DOTA, EvansBlue dyeFreeCyclicLNoneSyntheticFor Spect imaging and potential theranosticBlood samples (10 μL) were collected by heart puncture under 2% isoflurane anesthesia at 0.083, 0.5, 2, 4, 24, 48, 72, 96, and 168 h1.85 MBq 77.3 (Terminal Half Life)U-87 mg tumor bearing mice plasma proteaseRadioactivity assayU-87 mg tumor-bearing mice plasmaIn VivoNoneNoneIC50(nM) =71.7
4925
340642912021
RGDfK
111In-DOTA-cRGDfK5Radiolabelled with 111ln, DOTAFreeCyclicLNoneSyntheticFor Spect imaging and potential theranosticBlood samples (10 μL) were collected by heart puncture under 2% isoflurane anesthesia at 0.083, 0.5, 2, 4, 24, 48, 72, 96, and 168 h1.85 MBq 17.2 (Terminal Half Life)U-87 mg tumor bearing mice plasma proteaseRadioactivity assayU-87 mg tumor-bearing mice plasmaIn VivoNoneNoneIC50(nM) =35.2
4926
361330172021
KGSGSGCPRILMRCKQDSDCLAGCVCGPNGFCG
Fab–CKP-NLP30FreeFreeLinearLFab conjugation, Lys1 fatty acid conjugation (Palm)SyntheticPlatform for potential delivery of peptide like drug candidates37 °C for 24 hourN.A.75% Remained IntactN.A.SECN.A.In VitroNoneNoneN.A.
4927
361330172021
KGSGSGCPRILMRCKQDSDCLAGCVCGPNGFCG
CKP-NLP30FreeFreeLinearLAF488 labeled , Lys1 fatty acid conjugation (Palm)SyntheticPlatform for potential delivery of peptide like drug candidates37 °CN.A.1N.A.SECN.A.In VitroNoneNoneN.A.
4928
340487412021
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
Exendin-4 39FreeAmidationLinearLNoneSalivary gland of the lizard Heloderma suspectumAntidiabetesBlood samples were collected from the lateral tail vein at 0, 0.083, 0.25, 0.5, 1, 2, 3, 4, 6, 8 and 10 h0.07 mg/kg0.32 ± 0.04Male SD rats plasma proteaseELISAMale SD rats plasmaIn VivoPDB id: 7MLLNoneEC50(nM) = 1.79 ± 0.47 (EC50 values represent the concentration (nM) of agonists to simulate half-maximum GLP-1 receptor cAMP activation)
4929
340487412021
HGEGTFTSDLSMQMEEEAVLLFIEWLMNGGPSSGAPPPSC
M440FreeCys addition at C terminalLinearLM, R amino acid substitutionsSyntheticAntidiabetesBlood samples were collected from the lateral tail vein at 0, 0.083, 0.25, 0.5, 1, 2, 3, 4, 6, 8 and 10 h0.07 mg/kg1.80 ± 0.23Male SD rats plasma proteaseELISAMale SD rats plasmaIn VivoNoneNoneEC50(nM) = 38.49 ± 4.58 (EC50 values represent the concentration (nM) of agonists to simulate half-maximum GLP-1 receptor cAMP activation)
4930
339694562021
H-Aib-EGTFTSDVSSYLEGQAAKEFIAWLVRGRG
Semaglutide31FreeFreeLinearLAib modification at position 2, Lys26 side chain conjugated with (ADO-linker-Glu-C18)GLP-1 analogsAntidiabetesBlood samples for PK assessment were obtained during the first 9 days of dosing (7–45 samples per subject) and following the last dose on day 10 (16–38 samples per subject)N.A.158Human plasma protease LC-MSHuman plasma (Healthy subjects)In Vivohttps://pmc.ncbi.nlm.nih.gov/articles/PMC8736331/NoneN.A.
4931
339694562021
H-Aib-EGTFTSDVSSYLEGQAAKEFIAWLVRGRG
Semaglutide31FreeFreeLinearLAib modification at position 2, Lys26 side chain conjugated with (ADO-linker-Glu-C18)GLP-1 analogsAntidiabetesBlood samples for PK assessment were obtained during the first 9 days of dosing (7–45 samples per subject) and following the last dose on day 10 (16–38 samples per subject)N.A.146Human plasma protease LC-MSHuman plasma (Subjects with T2D)In Vivohttps://pmc.ncbi.nlm.nih.gov/articles/PMC8736331/NoneN.A.
4932
339400582021
gqsehhmrvysf
OPBP-112FreeFreeLinearDSubstituition of A with Y at position 10Derived from H12AnticancerCo-incubation of OPBP-1 with 10% human serum for 0 h, 1 h, 2 h, 4 h, 8 h, 16 h, 24 h, 32 h and 48 h.8 mg/kg0.33 ± 0.01Male SD rats plasma proteaseRP-HPLCMale SD rats plasmaIn VivoNoneNoneAfter 2 weeks of daily administration of 0.5 mg/kg OPBP-1, the tumor growth was significantly inhibited in CT26 and B16-OVA models.
4933
339400582021
gqsehhmrvysf
OPBP-112FreeFreeLinearDSubstituition of A with Y at position 10Derived from H12AnticancerCo-incubation of OPBP-1 with 10% human serum for 0 h, 1 h, 2 h, 4 h, 8 h, 16 h, 24 h, 32 h and 48 h.20 mg/kg8.69 ± 1.19Male SD rats plasma proteaseRP-HPLCMale SD rats plasmaIn VivoNoneNoneAfter 2 weeks of daily administration of 0.5 mg/kg OPBP-1, the tumor growth was significantly inhibited in CT26 and B16-OVA models.
4934
339400582021
gqsehhmrvysf
OPBP-1@TMC12FreeFreeLinearDSubstituition of A with Y at position 10Derived from H12AnticancerCo-incubation of OPBP-1 with 10% human serum for 0 h, 1 h, 2 h, 4 h, 8 h, 16 h, 24 h, 32 h and 48 h.20 mg/kg14.55 ± 1.43Male SD rats plasma proteaseRP-HPLCMale SD rats plasmaIn VivoNoneNoneAfter 2 weeks of daily administration of 0.5 mg/kg OPBP-1, the tumor growth was significantly inhibited in CT26 and B16-OVA models.
4935
339188532021
TSQVRQNYHQDSEAAINRQINLELYASYVYLSMSYYFDRDDVALKNFAKYFLHQSHEEREHAEKLMKLQNQRGGRIFLQDIKKPDCDDWESGLNAMECALHLEKNVNQSLLELHKLATDKNDPHLCDFIETHYLNEQVKAIKELGDHVTNLRKMGAPESGLAEYLFDKHTLG
HFn/DOX172FreeFreeLinearLNoneSyntheticAntitumorBlood samples were collected from the retro orbital sinus at fixed time points (10, 30 min, 1, 2, 4, 8, 12, 24, 36, 48 h) at 37 °C3.0 mg/kg3.07 ± 0.06SD rats serum proteaseFluorescence spectrometrySD rats serumIn VivoPDB id: 3AJONoneIC50 (μg mL−1) = 0.49 ± 0.11
4936
339188532021
TSQVRQNYHQDSEAAINRQINLELYASYVYLSMSYYFDRDDVALKNFAKYFLHQSHEEREHAEKLMKLQNQRGGRIFLQDIKKPDCDDWESGLNAMECALHLEKNVNQSLLELHKLATDKNDPHLCDFIETHYLNEQVKAIKELGDHVTNLRKMGAPESGLAEYLFDKHTLG-GGGSGGGTGGGSGGG-GFLG-ASPAAPAPAPAAPAPSAPAASPAAPAPASPAAPAPSAPA-GGSGG
HFn-PAS/DOX235Free15aa linker, enzyme cleavable site, PAS(40), 5 aa flexible linker conjugated at C terminus LinearLNoneSyntheticAntitumorBlood samples were collected from the retro orbital sinus at fixed time points (10, 30 min, 1, 2, 4, 8, 12, 24, 36, 48 h) at 37 °C3.0 mg/kg14.96 ± 0.29SD rats serum proteaseFluorescence spectrometrySD rats serumIn VivoPDB id: 3AJONoneIC50 (μg mL−1) = 0.38 ± 0.09
4937
339188532021
TSQVRQNYHQDSEAAINRQINLELYASYVYLSMSYYFDRDDVALKNFAKYFLHQSHEEREHAEKLMKLQNQRGGRIFLQDIKKPDCDDWESGLNAMECALHLEKNVNQSLLELHKLATDKNDPHLCDFIETHYLNEQVKAIKELGDHVTNLRKMGAPESGLAEYLFDKHTLG-GGGSGGGTGGGSGGG-GFLG-ASPAAPAPAPAAPAPSAPAASPAAPAPASPAAPAPSAPA-GGSGG-RGDK
HFn-GFLG-PAS-RGDK/DOX239FreeAdd RGDK tretapeptide to HFn-PAS C-terminusLinearLNoneSyntheticAntitumorBlood samples were collected from the retro orbital sinus at fixed time points (10, 30 min, 1, 2, 4, 8, 12, 24, 36, 48 h) at 37 °C3.0 mg/kg17.61 ± 0.39SD rats serum proteaseFluorescence spectrometrySD rats serumIn VivoPDB id: 3AJONoneIC50 (μg mL−1) = 0.17 ± 0.01
4938
339188532021
TSQVRQNYHQDSEAAINRQINLELYASYVYLSMSYYFDRDDVALKNFAKYFLHQSHEEREHAEKLMKLQNQRGGRIFLQDIKKPDCDDWESGLNAMECALHLEKNVNQSLLELHKLATDKNDPHLCDFIETHYLNEQVKAIKELGDHVTNLRKMGAPESGLAEYLFDKHTLG-GGGSGGGTGGGSGGG-PLGLAG-ASPAAPAPAPAAPAPSAPAASPAAPAPASPAAPAPSAPA-GGSGG-RGDK
HFn-PLGLAG-PAS-RGDK/DOX241FreeAdd RGDK tretapeptide to HFn-PAS C-terminus and substituite enzyme cleavable linker with PLGLAGLinearLNoneSyntheticAntitumorBlood samples were collected from the retro orbital sinus at fixed time points (10, 30 min, 1, 2, 4, 8, 12, 24, 36, 48 h) at 37 °C3.0 mg/kg18.93 ± 0.61SD rats serum proteaseFluorescence spectrometrySD rats serumIn VivoPDB id: 3AJONoneIC50 (μg mL−1) = 0.18 ± 0.04
4939
338948382021
KCNTATCATQRLAEFLRHSSNNFGPIlpptnvgsntp
Cagrilintide 37FreeAmidationCyclic (Cys-Cys Disulfide Bond)MixLPPTNVGSNTP all D-amino acids, Lipidation on Lys1amylin analogueAntiobesityBlood samples for pharmacokinetic testing were collected before dosing at baseline (week 0) and at weekly visits, and after the last dose (week 19) at 4, 8, 12, 24, 48, 72, 96, 168, 336, 504, 672, 840, and 1008 h after dosing0·16 − 4·5 mg159 – 195Human plasma protease N.A.Human plasmaIn Vivopubchem CID: 171397054NoneN.A.
4940
338948382021
H-Aib-EGTFTSDVSSYLEGQAAKEFIAWLVRGRG
Semaglutide31FreeFreeLinearLAib modification at position 2, Lys26 side chain conjugated with (ADO-linker-Glu-C18)GLP-1 analogsAntidiabetesBlood samples for pharmacokinetic testing were collected before dosing at baseline (week 0) and at weekly visits, and after the last dose (week 19) at 4, 8, 12, 24, 48, 72, 96, 168, 336, 504, 672, 840, and 1008 h after dosing2·4 mg145 – 165Human plasma protease N.A.Human plasmaIn VivoNoneNoneN.A.
4941
338254692021
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
Native Ex439FreeAmidationLinearLNoneGLP-1 analogsAntidiabetesBlood sample (20 μL) was obtained from the leg veins and using a pipette added into 80 μL of PBS solution (containing EDTA) at 40 s, 25 min, 50 min, 1.2 h, 1.6 h, 2 h, 4.8 h, 6.5 h, 8.5 h, 10 h, and 24 h after injection.75 nmol/kg0.72 ± 0.07C57Bl/6 mice plasma proteaseFluorescence assayC57BL/6 mice plasmaIn VivoNoneNoneEC50 values = 0.99 nM for Ex4 (GLP-1 Receptor Activation Potency)
4942
338254692021
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPSLPETGGG
FITC-labeled Ex4−DNP 944FITC-AhxEx4 linked to DNP9 = Dinitro phenol by (PEG)n spacerLinearLNoneGLP-1 analogsAntidiabetesBlood sample (20 μL) was obtained from the leg veins and using a pipette added into 80 μL of PBS solution (containing EDTA) at 40 s, 25 min, 50 min, 1.2 h, 1.6 h, 2 h, 4.8 h, 6.5 h, 8.5 h, 10 h, and 24 h after injection.75 nmol/kg2.07 ± 0.05C57Bl/6 mice plasma proteaseFluorescence assayC57BL/6 mice plasmaIn VivoNoneNoneEC50 values = 0.99 nM for Ex4 (GLP-1 Receptor Activation Potency)
4943
338254692021
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPSLPETGGG
FITC-labeled Ex4−DNP 1044FITC-AhxEx4 linked to DNP10 = Dinitro phenol by (PEG)n spacerLinearLNoneGLP-1 analogsAntidiabetesBlood sample (20 μL) was obtained from the leg veins and using a pipette added into 80 μL of PBS solution (containing EDTA) at 40 s, 25 min, 50 min, 1.2 h, 1.6 h, 2 h, 4.8 h, 6.5 h, 8.5 h, 10 h, and 24 h after injection.75 nmol/kg3.55 ± 0.33C57Bl/6 mice plasma proteaseFluorescence assayC57BL/6 mice plasmaIn VivoNoneNoneEC50 values = 0.99 nM for Ex4 (GLP-1 Receptor Activation Potency)
4944
338254692021
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPSLPETGGG
FITC-labeled Ex4−DNP 1144FITC-AhxEx4 linked to DNP11 = Dinitro phenol by (PEG)n spacerLinearLNoneGLP-1 analogsAntidiabetesBlood sample (20 μL) was obtained from the leg veins and using a pipette added into 80 μL of PBS solution (containing EDTA) at 40 s, 25 min, 50 min, 1.2 h, 1.6 h, 2 h, 4.8 h, 6.5 h, 8.5 h, 10 h, and 24 h after injection.75 nmol/kg2.62 ± 0.17C57Bl/6 mice plasma proteaseFluorescence assayC57BL/6 mice plasmaIn VivoNoneNoneEC50 values = 0.99 nM for Ex4 (GLP-1 Receptor Activation Potency)
4945
338225912021
KX
PEG−DNP-Lys conjugates 6C1DNPPEG20 KDa, MeOLinearLGDM linker with a two-carbon spacer between the β-carbon and the triazole, Mod = NC−, X = Structure given in paper (n=0)SyntheticIncreases Half LifepH 7.4N.A.87 (b-Elimination Half-Life)N.A.N.A.N.A.In VitroNoneNoneN.A.
4946
338225912021
KX
PEG−DNP-Lys conjugates 6C1DNPPEG20 KDa, MeOLinearLGDM linker with a two-carbon spacer between the β-carbon and the triazole, Mod = NC−, X = Structure given in paper (n=0)SyntheticIncreases Half LifepH 7.4N.A.87 (b-Elimination Half-Life)N.A.N.A.N.A.In VitroNoneNoneN.A.
4947
338225912021
KX
PEG−DNP-Lys conjugates 6C1DNPPEG20 KDa, MeOLinearLGDM linker with a two-carbon spacer between the β-carbon and the triazole, Mod = NC−, X = Structure given in paper (n=0)SyntheticIncreases Half LifepH 7.4N.A.1030 (b-Elimination Half-Life)N.A.N.A.N.A.In VitroNoneNoneN.A.
4948
338225912021
KX
PEG−DNP-Lys conjugates 71DNPPEG20 KDa, MeOLinearLGDM linker with a three-carbon spacer between the β-carbon and the triazole, Mod = PhSO2−, X = Structure given in paper (n=1)SyntheticIncreases Half LifepH 7.4N.A.256 (b-Elimination Half-Life)N.A.N.A.N.A.In VitroNoneNoneN.A.
4949
338225912021
KX
PEG−DNP-Lys conjugates 71DNPPEG20 KDa, MeOLinearLGDM linker with a three-carbon spacer between the β-carbon and the triazole, Mod = PhSO2−, X = Structure given in paper (n=1)SyntheticIncreases Half LifepH 7.4N.A.724 (b-Elimination Half-Life)N.A.N.A.N.A.In VitroNoneNoneN.A.
4950
338225912021
KX
PEG−DNP-Lys conjugates 71DNPPEG20 KDa, MeOLinearLGDM linker with a three-carbon spacer between the β-carbon and the triazole, Mod = PhSO2−, X = Structure given in paper (n=1)SyntheticIncreases Half LifepH 7.4N.A.2490 (b-Elimination Half-Life)N.A.N.A.N.A.In VitroNoneNoneN.A.
4951
338225912021
KX
PEG−DNP-Lys conjugates 81DNPPEG20 KDa, MeOLinearLGDM linker with a four-carbon spacer between the β-carbon and the triazole, Mod = MeSO2−, X = Structure given in paper (n=2)SyntheticIncreases Half LifepH 7.4N.A.1570 (b-Elimination Half-Life)N.A.N.A.N.A.In VitroNoneNoneN.A.
4952
338225912021
KX
PEG−DNP-Lys conjugates 81DNPPEG20 KDa, MeOLinearLGDM linker with a four-carbon spacer between the β-carbon and the triazole, Mod = MeSO2−, X = Structure given in paper (n=2)SyntheticIncreases Half LifepH 7.4N.A.5310 (b-Elimination Half-Life)N.A.N.A.N.A.In VitroNoneNoneN.A.
4953
338130912021
SGQYASHCWCWRDPGRSGGSK
FITC-TPP121FITC labelledFreeLinearLNoneSyntheticAnticancerBlood samples (20μL) were obtained at different points (0, 5, 30 min, 1,2, 4, 6, 9, 24 h) via tail bleeding4 mg/kg<10 (Blood Clearance Half Life)Mice blood plasma proteaseFluorescence spectrometryMice blood plasmaIn VivoNoneNoneN.A.
4954
338130912021
SGQYASHCWCWRDPGRSGGSK
TPP1 (SPIO NP@M-P)21FITC labelledFreeLinearLNoneSyntheticAnticancerBlood samples (20μL) were obtained at different points (0, 5, 30 min, 1,2, 4, 6, 9, 24 h) via tail bleeding4 mg/kg6 (Blood Clearance Half Life)Mice blood plasma proteaseFluorescence spectrometryMice blood plasmaIn VivoNoneNoneN.A.
4955
337918632021
DRVYIHP
125I-Ang1–77FreeFreeLinearL125I labeledSyntheticRole in Renal and Cardiovascular HomeostasisBlood samples (∼200 µL) were collected from the cannula into heparinized tubes before dosing and 5, 10, 15, 30, and 45 min and 1, 1.5, 2, and 3 h after administration4.5 mM0.6Rats plasma proteaseRadioactivity assayRats plasma In VivoNoneNoneAng1–7 exhibited 4.2±0.1%, 3.7±0.6%, 4.4±0.2%, and 2.6±0.4% binding capacity in D.D. water, PBS 50 mM, PBS10mM, and acetate bufer, respectively
4956
337918632021
DRVYIHP
125I-Ang Conj.7Thiol bisphosphonate,Maleimidopropionyl,PEG conjugated at N terminusFreeLinearL125I labeledSyntheticRole in Renal and Cardiovascular HomeostasisBlood samples (∼200 µL) were collected from the cannula into heparinized tubes before dosing and 5, 10, 15, 30, and 45 min and 1, 1.5, 2, and 3 h after administration4.5 mM3.4Rats plasma proteaseRadioactivity assayRats plasma In VivoNoneNoneAng Conj. values were 20.4±0.5%,6.8±0.6%, 8.4±0.2%, and 11.6±0.2%
4957
337918632021
DRVYIHP
125I-Ang Conj7Thiol bisphosphonate,Maleimidopropionyl,PEG conjugated at N terminusFreeLinearL125I labeledSyntheticRole in Renal and Cardiovascular HomeostasisBlood samples (∼200 µL) were collected from the cannula into heparinized tubes before dosing and 5, 10, 15, 30, and 45 min and 1, 1.5, 2, and 3 h after administration4.5 mM6.6Rats plasma proteaseRadioactivity assayRats plasma In VivoNoneNoneAng Conj. values were 20.4±0.5%,6.8±0.6%, 8.4±0.2%, and 11.6±0.2%
4958
337066862021
HMSMQEGAVTGEGQAAKEFIAWLVKGRVRADLVGDAFDV
TB01-339FreeFreeLinearLNoneSyntheticAntidiabetes250 ul blood samples were collected via jugular vein cannula at these time points: pre-dose, 0.0833, 0.25, 0.5, 1, 2, 4, 8, 24, 48, 72, 96, 168, 240 and 336 hours post dose.10 mg/kg~1Rats plasma proteaseELISARats plasma In VivoNoneNoneTB59-2 binds specifically to the GLP-1 R with an EC50 of 15.5 nM, TB-59-2 is a potent agonist in the cAMP assay with a similar EC50 as the GLP-1 7–36 peptide, TB59-2 can also induce the β-arrestin recruitment in GLP-1 R expression cells
4959
337066862021
HAEGTFTSNVSSYLEGQAAKEFIAWLVKGR
TB59-230GLP-1 7–36 peptide is linked to the light chain N-terminal of the TB01-2 antibody via a (G4S)x3 linkerFreeLinearLNoneSyntheticAntidiabetes250 ul blood samples were collected via jugular vein cannula at these time points: pre-dose, 0.0833, 0.25, 0.5, 1, 2, 4, 8, 24, 48, 72, 96, 168, 240 and 336 hours post dose.10 mg/kg>2Rats plasma proteaseELISARats plasma In VivoNoneNoneTB59-2 binds specifically to the GLP-1 R with an EC50 of 15.5 nM, TB-59-2 is a potent agonist in the cAMP assay with a similar EC50 as the GLP-1 7–36 peptide, TB59-2 can also induce the β-arrestin recruitment in GLP-1 R expression cells
4960
336744012021
pCl-F-cyclo(c-Y-(D-4-amino-Phe)(Cbm))-KTC)y
177Lu-DOTA-LM39DOTAAmidationCyclic(C-C NC terminal bond)MixDOTA-LM3 conjugation, Cbm = Carbamoyl, 177Lu labeling, pCl-Phe = P-Chloro PhenyalanineSST analogTreating Metastatic Neuroendocrine Neoplasms (Nens)N.A.7 ± 1 GBq 76Whole bodyDosimetrywhole body In VivoNoneNonePartial Remission: 17 patients (36.2%), Stable Disease: 23 patients (48.9%), Progressive Disease: 7 patients (14.9%) (The efficacy of the peptide 177Lu-DOTA-LM3 for peptide receptor radionuclide therapy (PRRT) in patients with metastatic neuroendocrine neoplasms )
4961
336744012021
pCl-Phe-cyclo(c-Y-(D-4-amino-Phe)(Cbm))-KTC)y
177Lu-DOTA-LM39DOTAAmidationCyclicMixDOTA-LM3 conjugation, Cbm = Carbamoyl, 177Lu labeling, pCl-Phe = P-Chloro PhenyalanineSST analogTreating Metastatic Neuroendocrine Neoplasms (Nens)N.A.7 ± 1 GBq 92Human kidney homogenate proteaseDosimetryHuman kidney homogenate In VivoNoneNonePartial Remission: 17 patients (36.2%), Stable Disease: 23 patients (48.9%), Progressive Disease: 7 patients (14.9%) (The efficacy of the peptide 177Lu-DOTA-LM3 for peptide receptor radionuclide therapy (PRRT) in patients with metastatic neuroendocrine neoplasms )
4962
336744012021
pCl-Phe-cyclo(c-Y-(D-4-amino-Phe)(Cbm))-KTC)y
177Lu-DOTA-LM39DOTAAmidationCyclicMixDOTA-LM3 conjugation, Cbm = Carbamoyl, 177Lu labeling, pCl-Phe = P-Chloro PhenyalanineSST analogTreating Metastatic Neuroendocrine Neoplasms (Nens)N.A.7 ± 1 GBq 97Human spleenDosimetryHuman spleenIn VivoNoneNonePartial Remission: 17 patients (36.2%), Stable Disease: 23 patients (48.9%), Progressive Disease: 7 patients (14.9%) (The efficacy of the peptide 177Lu-DOTA-LM3 for peptide receptor radionuclide therapy (PRRT) in patients with metastatic neuroendocrine neoplasms )
4963
336744012021
pCl-Phe-cyclo(c-Y-(D-4-amino-Phe)(Cbm))-KTC)y
177Lu-DOTA-LM39DOTAAmidationCyclicMixDOTA-LM3 conjugation, Cbm = Carbamoyl, 177Lu labeling, pCl-Phe = P-Chloro PhenyalanineSST analogTreating Metastatic Neuroendocrine Neoplasms (Nens)N.A.7 ± 1 GBq 111Human metastasesDosimetryHuman metastasesIn VivoNoneNonePartial Remission: 17 patients (36.2%), Stable Disease: 23 patients (48.9%), Progressive Disease: 7 patients (14.9%) (The efficacy of the peptide 177Lu-DOTA-LM3 for peptide receptor radionuclide therapy (PRRT) in patients with metastatic neuroendocrine neoplasms )
4964
336720392021
HGEGTFTSDVSSYLEGQAAKEFIAWLVRGRC
GLP1_8G37C-HSA31FreeHSALinearLSubstituition of amino acid G at position 2GLP-1 analogsAntidiabetesBlood samples (<70 μL) were collected from the retroorbital venous sinus at 0.16, 1, 3, 6, 12, and 24 h after conjugate administration10 nmol/kg3.2 (T1/2a)BALB/c mice plasma proteaseSandwich ELISABALB/c mice plasma In VivoNoneNoneEC50= 1340 nM ( In vitro measurement of cAMP production by GLP-1R-overexpressing HEK-293 cells) 
4965
336720392021
HAGTFTSDVSSYLEGQAAKEFIAWLVRGRC
GLP1_8A37C-HSA30FreeHSALinearLSubstituition of amino acid A at position 2GLP-1 analogsAntidiabetesBlood samples (<70 μL) were collected from the retroorbital venous sinus at 0.16, 1, 3, 6, 12, and 24 h after conjugate administration10 nmol/kg3.3 (T1/2a)BALB/c mice plasma proteaseSandwich ELISABALB/c mice plasma In VivoNoneNoneEC50=185 nM ( In vitro measurement of cAMP production by GLP-1R-overexpressing HEK-293 cells) 
4966
336720392021
HGEGTFTSDVSSYLEGQAAKEFIAWLVRGRC
GLP1_8G37C-HSA31FreeHSALinearLSubstituition of amino acid G at position 2GLP-1 analogsAntidiabetesBlood samples (<70 μL) were collected from the retroorbital venous sinus at 0.16, 1, 3, 6, 12, and 24 h after conjugate administration10 nmol/kg9 ( T1/2b)BALB/c mice plasma proteaseSandwich ELISABALB/c mice plasma In VivoNoneNoneEC50= 1340 nM ( In vitro measurement of cAMP production by GLP-1R-overexpressing HEK-293 cells) 
4967
336720392021
HAGTFTSDVSSYLEGQAAKEFIAWLVRGRC
GLP1_8A37C-HSA30FreeHSALinearLSubstituition of amino acid A at position 2GLP-1 analogsAntidiabetesBlood samples (<70 μL) were collected from the retroorbital venous sinus at 0.16, 1, 3, 6, 12, and 24 h after conjugate administration10 nmol/kg7.1 (T1/2b)BALB/c mice plasma proteaseSandwich ELISABALB/c mice plasma In VivoNoneNoneEC50=185 nM ( In vitro measurement of cAMP production by GLP-1R-overexpressing HEK-293 cells) 
4968
336655012021
Poly(L-glutamic acid)
PLG-PtnFreeCisplatin (CDDP) is complexed with the carboxyl groups of the L-glutamic acidLinearLNoneSyntheticAnticancerAt predefined time points 5, 15, and 30 min, and 1, 3, 6, 12, and 24 h, 200.0 μL of blood samples were collected from the orbital cavities of rats3 mg/kg1.9Rats plasma proteaseICP-MSRats plasma In VivoNoneNoneIC50 (μg mL−1) = 4.8 in SKOV3 cells 
4969
336655012021
Poly(L-glutamic acid)
PEG-PLG-PtnPEGylationCisplatin (CDDP) is complexed with the carboxyl groups of the L-glutamic acidLinearLPEGylationSyntheticAnticancerAt predefined time points 5, 15, and 30 min, and 1, 3, 6, 12, and 24 h, 200.0 μL of blood samples were collected from the orbital cavities of rats3 mg/kg8.8Rats plasma proteaseICP-MSRats plasma In VivoNoneNoneIC50 (μg mL−1) = 11 in SKOV3 cells 
4970
336655012021
Poly(L-glutamic acid)
PEG-pHe-PLG-Pt (pH 7.4) nPEG-CDMCisplatin (CDDP) is complexed with the carboxyl groups of the L-glutamic acidLinearLPoly(L-glutamic acid) is grafted with methoxy poly(ethylene glycol) (PEG) using a pH-sensitive linker, 2-propionic-3-methylmaleic anhydride = CDMSyntheticAnticancerAt predefined time points 5, 15, and 30 min, and 1, 3, 6, 12, and 24 h, 200.0 μL of blood samples were collected from the orbital cavities of rats3 mg/kg7.9Rats plasma proteaseICP-MSRats plasma In VivoNoneNoneIC50 (μg mL−1) = 8.5 in SKOV3 cells 
4971
336655012021
Poly(L-glutamic acid)
PEG-pHe-PLG-Pt (pH 6.5) nPEG-CDMCisplatin (CDDP) is complexed with the carboxyl groups of the L-glutamic acidLinearLPoly(L-glutamic acid) is grafted with methoxy poly(ethylene glycol) (PEG) using a pH-sensitive linker, CDM = 2-propionic-3-methylmaleic anhydride SyntheticAnticancerAt predefined time points 5, 15, and 30 min, and 1, 3, 6, 12, and 24 h, 200.0 μL of blood samples were collected from the orbital cavities of rats3 mg/kgN.A.Rats plasma proteaseICP-MSRats plasma In VivoNoneNoneIC50 (μg mL−1) = 5.8 in SKOV3 cells 
4972
336655012021
PLGLAG-Poly(L-glutamic acid)
PEG-MMP-PLG-Pt n+6PEGylationCisplatin (CDDP) is complexed with the carboxyl groups of the L-glutamic acidLinearLPEGylation through an MMP-sensitive peptide linker (PLGLAG), CDM = 2-propionic-3-methylmaleic anhydride SyntheticAnticancerAt predefined time points 5, 15, and 30 min, and 1, 3, 6, 12, and 24 h, 200.0 μL of blood samples were collected from the orbital cavities of rats3 mg/kg7.8Rats plasma proteaseICP-MSRats plasma In VivoNoneNoneIC50 (μg mL−1) = 6.9 in SKOV3 cells 
4973
336563232021
PTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLTFKFYMPKKATELKHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLISNINVIVLELKGSETTFMCEYADETATIVEFLNRWITFSQSIISTLT
IL-2132FreeFreeCyclic (C57-C104 Disulfide Bond)LNoneSyntheticAnticancer, Autoimmune diseases treatmentSerum samples were collected at 10 min and 2, 6, 12, 20, and 36 h for group I and 1, 4, 8, 16, 24, and 48 h for group II by retro-orbital bleeding, . Serum samples were collected at 0, 2, 5, 20, 30, and 45 min for group I and 10 min and 1, 2, 4, 6, and 8 h for group II by retro-orbital bleeding0.6 mg/kg0.041 ± 0.006 (T1/2a )Mouse plasma proteaseSandwich ELISAMouse plasmaIn Vivopdb id: 5LQB and https://pubs.acs.org/doi/suppl/10.1021/acs.bioconjchem.1c00062/suppl_file/bc1c00062_si_001.pdfNoneKD (M) = (1.952 ± 0.130) × 10−8 for IL-2
4974
336563232021
PTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLTFKFYMPKKATELKHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLISNINVIVLELKGSETTFMCEYADETATIVEFLNRWITFCQSIISTLT-(ED)6-LPETGGGK
B6146FreeLys146 contains Fatty acid moiety which introduces 8-amino-3,6-dioxaoctanoic acid (AEEA) and glutamic acidCyclic (C57-C104 Disulfide Bond) In IL-2LNoneSyntheticAnticancer, Autoimmune diseases treatmentSerum samples were collected at 10 min and 2, 6, 12, 20, and 36 h for group I and 1, 4, 8, 16, 24, and 48 h for group II by retro-orbital bleeding, . Serum samples were collected at 0, 2, 5, 20, 30, and 45 min for group I and 10 min and 1, 2, 4, 6, and 8 h for group II by retro-orbital bleeding0.6 mg/kg0.613 ± 0.063(T1/2a )Mouse plasma proteaseSandwich ELISAMouse plasmaIn Vivopdb id: 5LQB and https://pubs.acs.org/doi/suppl/10.1021/acs.bioconjchem.1c00062/suppl_file/bc1c00062_si_001.pdfNoneKD (M) = (1.952 ± 0.130) × 10−8 for IL-2
4975
336563232021
PTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLTFKFYMPKKATELKHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLISNINVIVLELKGSETTFMCEYADETATIVEFLNRWITFCQSIISTLT-(ED)6-LPETGGGK
B6 control146FreeLys146 contains Fatty acid moiety which introduces 8-amino-3,6-dioxaoctanoic acid (AEEA) and glutamic acidCyclic (C57-C104 Disulfide Bond) In IL-2LNoneSyntheticAnticancer, Autoimmune diseases treatmentSerum samples were collected at 0, 5, and 30 min and 2, 6, and 12 h for group I and 2, 10, and 60 min and 4, 8, and 24 h for group II by retro-orbital bleeding0.6 mg/kg0.035 ± 0.014(T1/2a )Mouse plasma proteaseSandwich ELISAMouse plasmaIn Vivopdb id: 5LQB and https://pubs.acs.org/doi/suppl/10.1021/acs.bioconjchem.1c00062/suppl_file/bc1c00062_si_001.pdfNoneKD (M) = (1.952 ± 0.130) × 10−8 for IL-2
4976
336563232021
PTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLTFKFYMPKKATELKHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLISNINVIVLELKGSETTFMCEYADETATIVEFLNRWITFSQSIISTLT
IL-2132FreeFreeCyclic (C57-C104 Disulfide Bond)LNoneSyntheticAnticancer, Autoimmune diseases treatmentSerum samples were collected at 10 min and 2, 6, 12, 20, and 36 h for group I and 1, 4, 8, 16, 24, and 48 h for group II by retro-orbital bleeding, . Serum samples were collected at 0, 2, 5, 20, 30, and 45 min for group I and 10 min and 1, 2, 4, 6, and 8 h for group II by retro-orbital bleeding0.6 mg/kg0.273 ± 0.040(T1/2b)Mouse plasma proteaseSandwich ELISAMouse plasmaIn Vivopdb id: 5LQB and https://pubs.acs.org/doi/suppl/10.1021/acs.bioconjchem.1c00062/suppl_file/bc1c00062_si_001.pdfNoneKD (M) = (1.952 ± 0.130) × 10−8 for IL-2
4977
336563232021
PTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLTFKFYMPKKATELKHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLISNINVIVLELKGSETTFMCEYADETATIVEFLNRWITFCQSIISTLT-(ED)6-LPETGGGK
B6146FreeLys146 contains Fatty acid moiety which introduces 8-amino-3,6-dioxaoctanoic acid (AEEA) and glutamic acidCyclic (C57-C104 Disulfide Bond) In IL-2LNoneSyntheticAnticancer, Autoimmune diseases treatmentSerum samples were collected at 10 min and 2, 6, 12, 20, and 36 h for group I and 1, 4, 8, 16, 24, and 48 h for group II by retro-orbital bleeding, . Serum samples were collected at 0, 2, 5, 20, 30, and 45 min for group I and 10 min and 1, 2, 4, 6, and 8 h for group II by retro-orbital bleeding0.6 mg/kg3.595 ± 0.518(T1/2b)Mouse plasma proteaseSandwich ELISAMouse plasmaIn Vivopdb id: 5LQB and https://pubs.acs.org/doi/suppl/10.1021/acs.bioconjchem.1c00062/suppl_file/bc1c00062_si_001.pdfNoneKD (M) = (1.952 ± 0.130) × 10−8 for IL-2
4978
336563232021
PTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLTFKFYMPKKATELKHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLISNINVIVLELKGSETTFMCEYADETATIVEFLNRWITFCQSIISTLT-(ED)6-LPETGGGK
B6 control146FreeLys146 contains Fatty acid moiety which introduces 8-amino-3,6-dioxaoctanoic acid (AEEA) and glutamic acidCyclic (C57-C104 Disulfide Bond) In IL-2LNoneSyntheticAnticancer, Autoimmune diseases treatmentSerum samples were collected at 0, 5, and 30 min and 2, 6, and 12 h for group I and 2, 10, and 60 min and 4, 8, and 24 h for group II by retro-orbital bleeding0.6 mg/kg0.196 ± 0.114(T1/2b)Mouse plasma proteaseSandwich ELISAMouse plasmaIn Vivopdb id: 5LQB and https://pubs.acs.org/doi/suppl/10.1021/acs.bioconjchem.1c00062/suppl_file/bc1c00062_si_001.pdfNoneKD (M) = (1.952 ± 0.130) × 10−8 for IL-2
4979
336501552021
DYKDDDDKDYKDDDDKDYKDDDDKMDTARIAVVGAGVVGLSTAVCISKLVPRCSVTIISDKFTPDTTSDVAAGMLIPHTYPDTPIHTQKQWFRETFNHLFAIANSAEAGDAGVHLVSGWQIFQSTPTEEVPFWADVVLGFRKMTEAELKKFPQYVFGQAFTTLKCECPAYLPWLEKRIKGSGGWTLTRRIEDLWELHPSFDIVVNCSGLGSRQLAGDSKIFPVRGQVLQVQAPWVEHFIRDGSGLTYIYPGTSHVTLGGTRQKGDWNLSPDAENSREILSRCCALEPSLHGACNIREKVGLRPYRPGVRLQTELLARDGQRLPVVHHYGHGSGGISVHWGTALEAARLVSECVHALRTPIPKSNL
3XFLAG-hDASPO_3413653XFLAG labellingFreeLinearLNoneFound in the hippocampus of female patients affected by Alzheimer's diseaseDegradation Of D-Aspartate ( D-Asp)10 hours2 μg≈ 100U87 cells lysate proteaseWestern blottingU87 cells lysate with cycloheximide (CHX)In VivoNoneNoneN.A.
4980
336501552021
DYKDDDDKDYKDDDDKDYKDDDDKMRPARHWETRFGARDFGGFQDCFFRDRLMDTARIAVVGAGVVGLSTAVCISKLVPRCSVTIISDKFTPDTTSDVAAGMLIPHTYPDTPIHTQKQWFRETFNHLFAIANSAEAGDAGVHLVSGWQIFQSTPTEEVPFWADVVLGFRKMTEAELKKFPQYVFGQAFTTLKCECPAYLPWLEKRIKGSGGWTLTRRIEDLWELHPSFDIVVNCSGLGSRQLAGDSKIFPVRGQVLQVQAPWVEHFIRDGSGLTYIYPGTSHVTLGGTRQKGDWNLSPDAENSREILSRCCALEPSLHGACNIREKVGLRPYRPGVRLQTELLARDGQRLPVVHHYGHGSGGISVHWGTALEAARLVSECVHALRTPIPKSNL
3XFLAG-hDASPO_3693933XFLAG labellingFreeLinearLNoneFound in the hippocampus of female patients affected by Alzheimer's diseaseDegradation Of D-Aspartate ( D-Asp)10 hours2 μg≈ 100U87 cells lysate proteaseWestern blottingU87 cells lysate with cycloheximide (CHX)In VivoNoneNoneN.A.
4981
336077002021
KEIVSRNKRRYQEDGRKKRRQRRR
Tat-K1324FreeFreeLinearLNoneSyntheticTreatment of Ischemic StrokePlasma samples were taken at pre-dose, 5, 10, 15, 20, 30, 45 min, and 1, 1.5, 2, 3, 4, 5, 6 h after the beginning of intravenous infusion1 mg0.26 ± 0.02Human plasma protease UPLC–MS/MSHuman plasmaIn VivoNoneNoneN.A.
4982
336077002021
KEIVSRNKRRYQEDGRKKRRQRRR
Tat-K1324FreeFreeLinearLNoneSyntheticTreatment of Ischemic StrokePlasma samples were taken at pre-dose, 5, 10, 15, 20, 30, 45 min, and 1, 1.5, 2, 3, 4, 5, 6 h after the beginning of intravenous infusion4 mg 0.36 ± 0.04Human plasma protease UPLC–MS/MSHuman plasmaIn VivoNoneNoneN.A.
4983
336077002021
KEIVSRNKRRYQEDGRKKRRQRRR
Tat-K1324FreeFreeLinearLNoneSyntheticTreatment of Ischemic StrokePlasma samples were taken at pre-dose, 5, 10, 15, 20, 30, 45 min, and 1, 1.5, 2, 3, 4, 5, 6 h after the beginning of intravenous infusion10 mg0.45 ± 0.05Human plasma protease UPLC–MS/MSHuman plasmaIn VivoNoneNoneN.A.
4984
336077002021
KEIVSRNKRRYQEDGRKKRRQRRR
Tat-K1324FreeFreeLinearLNoneSyntheticTreatment of Ischemic StrokePlasma samples were taken at pre-dose, 5, 10, 15, 20, 30, 45 min, and 1, 1.5, 2, 3, 4, 5, 6 h after the beginning of intravenous infusion20 mg0.55 ± 0.07Human plasma protease UPLC–MS/MSHuman plasmaIn VivoNoneNoneN.A.
4985
336077002021
KEIVSRNKRRYQEDGRKKRRQRRR
Tat-K1324FreeFreeLinearLNoneSyntheticTreatment of Ischemic StrokePlasma samples were taken at pre-dose, 5, 10, 15, 20, 30, 45 min, and 1, 1.5, 2, 3, 4, 5, 6 h after the beginning of intravenous infusion30 mg0.70 ± 0.08Human plasma protease UPLC–MS/MSHuman plasmaIn VivoNoneNoneN.A.
4986
336077002021
KEIVSRNKRRYQEDGRKKRRQRRR
Tat-K1324FreeFreeLinearLNoneSyntheticTreatment of Ischemic Strokeplasma samples were taken at pre-dose, 5, 10, 15, 20, 30, 45 min, and 1, 1.5, 2, 3, 4, 5, 6 h after the beginning of intravenous infusion45 mg0.73 ± 0.05Human plasma protease UPLC–MS/MSHuman plasmaIn VivoNoneNoneN.A.
4987
336077002021
KEIVSRNKRRYQEDGRKKRRQRRR
Tat-K1324FreeFreeLinearLNoneSyntheticTreatment of Ischemic Strokeplasma samples were taken at pre-dose, 5, 10, 15, 20, 30, 45 min, and 1, 1.5, 2, 3, 4, 5, 6 h after the beginning of intravenous infusion60 mg0.78 ± 0.06Human plasma protease UPLC–MS/MSHuman plasmaIn VivoNoneNoneN.A.
4988
336071652021
RRPYIL
NT(8:13)6FreeFreeLinearLNoneNeuropeptideAnalgesicPlasma collected at 0, 1, 2, 5, 10, 30 and 60 min0.156 mM0.98 ± 0.08Rats plasma proteaseUPLC-MSRats plasma In VivoNoneNone(Binding) Ki (nM) = 1.65 ± 0.06 for hNTS1
4989
336071652021
KKPYIL
JMV4386Both Arg residues in positions 1 and 2 were replaced by two LysFreeLinearLNoneDerived from NTAnalgesic without hypothermiaPlasma collected at 0, 1, 2, 5, 10, 30 and 60 min0.156 mM1.57 ± 0.27Rats plasma proteaseUPLC-MSRats plasma In VivoNoneNone(Binding) Ki (nM) = 4.00 ± 0.35 for hNTS1
4990
336071652021
KΨ[CH2NH]KPYIL
JMV4496FreeFreeLinearLArg8-Arg9 was replaced by a reduced amine bond (Ψ[CH2NH]) between Lys8-Lys9 Derived from NTAnalgesic without hypothermiaPlasma collected at 0, 1, 2, 5, 10, 30 and 60 min0.156 mM8.37 ± 2.02Rats plasma proteaseUPLC-MSRats plasma In VivoNoneNone(Binding) Ki (nM) = 2.02 ± 0.80 for hNTS1
4991
336071652021
KΨ[CH2NH]K-Sip-YIL
JMV51706FreeFreeLinearLPro10 was then substituted by the silylated proline analog silaproline(Sip) , Arg8-Arg9 was replaced by a reduced amine bond (Ψ[CH2NH]) between Lys8-Lys9 Derived from NTAnalgesic without hypothermiaPlasma collected at 0, 1, 2, 5, 10, 30 and 60 min0.156 mM22.1 ± 1.9Rats plasma proteaseUPLC-MSRats plasma In VivoNoneNone(Binding) Ki (nM) = 296 ± 51 for hNTS1
4992
336071652021
KΨ[CH2NH]KPYI-TMSAla
JMV52066Freesubstitution of Leu13 by the (L)-(Trimethylsilyl)-Alanine (TMSAla) LinearLArg8-Arg9 was replaced by a reduced amine bond (Ψ[CH2NH]) between Lys8-Lys9 Derived from NTAnalgesic without hypothermiaPlasma collected at 0, 1, 2, 5, 10, 30 and 60 min0.156 mM2.13 ± 0.19Rats plasma proteaseUPLC-MSRats plasma In VivoNoneNone(Binding) Ki (nM) = 2.45 ± 0.17 for hNTS1
4993
336071652021
KΨ[CH2NH]K-Sip-YI-TMSAla
JMV52966FreeFreeLinearLDi-substitution with both Sip and TMSAla, Arg8-Arg9 was replaced by a reduced amine bond (Ψ[CH2NH]) between Lys8-Lys9 Derived from NTAnalgesic without hypothermiaPlasma collected at 0, 1, 2, 5, 10, 30 and 60 min0.156 mM20.6 ± 4.15Rats plasma proteaseUPLC-MSRats plasma In VivoNoneNone(Binding) Ki (nM) = 610 ± 31 for hNTS1
4994
335558582021
LEGREKVRAQI-Aib-Aib-EGMSTWS-Aib-RKK
B10-33 (Cpd 58)24AcetylationAmidationLinearLLys24 conjugated with(-(γE)3-C16), AibSyntheticTreatment of Cardiovascular DiseasesBlood samples were collected from individual animals at the following time points: 0.083, 0.25, 0.5, 1, 3, 6, 8, 24, 48, and 72 h1 mg/kg4.3Rats plasma proteaseLCHRMSRats plasma In VivoNoneNoneEC50 nM = 17.6 ± 8.1(97%) in OVCAR5 cells
4995
335558582021
LEGREKVRAQI-Aib-Aib-EGMSTWS-Aib-RK-PEG12-K
B10-33 (Cpd 59)24AcetylationAmidationLinearLLys24 conjugated with (-(γE)3-C16), PEGylation,Aib,NleSyntheticTreatment of Cardiovascular DiseasesBlood samples were collected from individual animals at the following time points: 0.083, 0.25, 0.5, 1, 3, 6, 8, 24, 48, and 72 h1 mg/kg8.9Rats plasma proteaseLCHRMSRats plasma In VivoNoneNoneEC50 nM = 3.6 ± 2.0 (88%) in OVCAR5 cells
4996
335558582021
LEGREKVRAQI-Aib-Aib-EG-Nle-STWS-Aib-RK-PEG12-K
Cpd 60(B10-33 )24AcetylationAmidationLinearLLys24 conjugated with (-(γE)3-C16), PEGylation,Aib,NleSyntheticTreatment of Cardiovascular DiseasesBlood samples were collected from individual animals at the following time points: 0.083, 0.25, 0.5, 1, 3, 6, 8, 24, 48, and 72 h1 mg/kg6.4Rats plasma proteaseLCHRMSRats plasma In VivoNoneNoneEC50 nM = 3.2 ± 2.1 (74%) in OVCAR5 cells
4997
335558582021
LEGREKVRAQI-Aib-Aib-EG-Nle-STWS-Aib-RK-PEG12-K
Cpd 61(B10-33 )24AcetylationAmidationLinearLLys24 conjugated with (-(γE)3-C18), PEGylation,Aib,NleSyntheticTreatment of Cardiovascular DiseasesN.A.1 mg/kg4.8Rats plasma proteaseLCHRMSRats plasma In VivoNoneNoneEC50 nM = 1.0 ± 0.9 (79%) in OVCAR5 cells
4998
335558582021
LEGREKVRAKI-Aib-Aib-EG-Nle-STWS-Aib-RKK-PEG12-K
Cpd 62(B10-33 )24AcetylationAmidationLinearLLys24 conjugated with (-(γE)3-C18), PEGylation,Aib,Nle,acetylation at Lys10 and Lys23SyntheticTreatment of Cardiovascular DiseasesN.A.1 mg/kg4.3Rats plasma proteaseLCHRMSRats plasma In VivoNoneNoneEC50 nM = 0.6 ± 0.4 (95%) in OVCAR5 cells
4999
335558582021
LEGREKVRAKI-Aib-Aib-EG-Nle-STWS-Aib-RKKK
Cpd 63(B10-33 )24AcetylationAmidationLinearLLys24 conjugated with (-(PEG2)3-(γE)3-C16), PEGylation,Aib,Nle,acetylation at Lys10 and Lys23SyntheticTreatment of Cardiovascular DiseasesN.A.1 mg/kg5.7Rats plasma proteaseLCHRMSRats plasma In VivoNoneNoneEC50 nM = 1.0 ± 0.6 (80%) in OVCAR5 cells
5000
335558582021
LEGREKVRAKI-Aib-Aib-EG-Nle-STWS-Aib-RKKK
Cpd 64(B10-33 )24AcetylationAmidationLinearLLys24 conjugated with (-(PEG2)3-(γE)3-C18), PEGylation,Aib,Nle,acetylation at Lys10 and Lys23SyntheticTreatment of Cardiovascular DiseasesN.A.1 mg/kg3.9Rats plasma proteaseLCHRMSRats plasma In VivoNoneNoneEC50 nM = 0.2 ± 0.1 (89%) in OVCAR5 cells
5001
335558582021
LEGREKVRAKI-Aib-Aib-EG-Nle-STWS-Aib-RKK-(PEG2)3-K
Cpd 65(B10-33 )24AcetylationAmidationLinearLLys24 conjugated with (-(γE)3-C18), PEGylation,Aib,Nle,acetylation at Lys10 and Lys23SyntheticTreatment of Cardiovascular DiseasesN.A.1 mg/kg3.4Rats plasma proteaseLCHRMSRats plasma In VivoNoneNoneEC50 nM = 0.1 ± 0.1 (88%) in OVCAR5 cells
5002
335558582021
LEGREKVRAKI-Aib-Aib-EG-Nle-STWS-Aib-RKK-(PDGA)3-K
Cpd 66(B10-33 )24AcetylationAmidationLinearLLys24 conjugated with (-(γE)3-C18), PEGylation,Aib,Nle,acetylation at Lys10 and Lys23SyntheticTreatment of Cardiovascular DiseasesN.A.1 mg/kg3.96Rats plasma proteaseLCHRMSRats plasma In VivoNoneNoneEC50 nM = 0.4 ± 0.2 (88%) in OVCAR5 cells
5003
335558582021
LEGREKVRA-X19-I-Aib-Aib-EG-X25-STWS-Aib-RKKK
Cpd 67(B10-33 )24AcetylationAmidationLinearLLys24 conjugated with (-(PEG2)3-(γE)3-C16-OH), PEGylation,Aib,Nle,acetylation at Lys10 and Lys23SyntheticTreatment of Cardiovascular DiseasesN.A.1 mg/kgN.A.Rats plasma proteaseLCHRMSRats plasma In VivoNoneNoneEC50 nM = 809 ± 20 (70%) in OVCAR5 cells
5004
335558582021
LEGREKVRAKI-Aib-Aib-EG-Nle-STWS-Aib-RKKK
Cpd 68(B10-33 )24AcetylationAmidationLinearLLys24 conjugated with (-(PEG2)3-(γE)3-C18-OH), PEGylation,Aib,Nle,acetylation at Lys10 and Lys23SyntheticTreatment of Cardiovascular DiseasesN.A.1 mg/kgN.A.Rats plasma proteaseLCHRMSRats plasma In VivoNoneNoneEC50 nM = 368 ± 76 (75%) in OVCAR5 cells
5005
333915052021
APGSYTGSAPGVASGFTFSNYGMHIYYDSSKMNYADTVKGSHYVVDVGGGGSGGGGSGGGGSQASQDIGNWLAGATSLADLQAYNTPWTAPGSYTGSAPGAGCKNFFWKTFTSC
[125I]SST-scFv8D3115125I labeledscFv of 8D3 is added to SSTCyclic (Disulfide Bond Bw C-C Of SST)LSerine, threonine and glycine were added to the linker SyntheticTreatment of Alzheimer's diseasesEight microliter blood samples from the tail vein were obtained at 0.5, 1, 2, 4, 6 and 24-h post injection0.44±0.08 MBq6Mice plasma proteaseRadioactivity assayMice plasmaIn VivoNoneNoneThe measured activation of neprilysin by SST-scFv8D3 preserved around 70% of the activation obtained by SST alone 
5006
333875932021
CDLPQTHSLGSRRTLMLLAQMRKISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE
Wild-type (IFN)165FreeFreeLinearLNoneHuman derivedAntiviral, AntiproliferativeBlood samples were taken at different times post-injection 100000 U0.9 ± 0.1 (T1/2 Elimination)Rats plasma proteaseSandwich ELISARats plasma In VivoPDB id: 1ITFNoneAntiviral SBA (IU/ng) = 201 ± 9 in wild-type IFN, Antiproliferative SBA (IU/ng) = 240 ± 50
5007
333875932021
APARSPSPSTQPWECDLPQTHSLGSRRTLMLLAQMRRISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE
GMOP-IFN179GM-CSF O-glycosylated PeptideFreeLinearLNoneSyntheticAntiviral, AntiproliferativeBlood samples were taken at different times post-injection 100000 U3.0 ± 0.4(T1/2 Elimination)Rats plasma proteaseSandwich ELISARats plasma In VivoPDB id: 1ITFNoneAntiviral SBA (IU/ng) = 190 ± 30 in GMOP-IFN, Antiproliferative SBA (IU/ng) = 280 ± 40 
5008
333875932021
APARSPSPTPTPTPT-CDLPQTHSLGSRRTLMLLAQMRRISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE
mGMOP-IFN180Modified GOMPFreeLinearLNoneSyntheticAntiviral, AntiproliferativeBlood samples were taken at different times post-injection 100000 U2.5 ± 0.2 (T1/2 Elimination)Rats plasma proteaseSandwich ELISARats plasmaIn VivoPDB id: 1ITFNoneAntiviral SBA (IU/ng) = 280 ± 50 in mGMOP-IFN, Antiproliferative SBA (IU/ng = 95 ± 5 
5009
332459512021
YAEGTFISDYSIAMDKIRQQNFVNWLLAQKGKKSDWKHNITQ
GIP(1–42)42FreeFreeLinearLNoneSecreted by entero-endocrine K cells located in the proximal intestineInsulinotrophic EffectBlood samples (50 μL) were drawn from the retro-orbital plexus at t = 0, 1, 3, 5, 10 and 20 min25 nmol/kg93 ± 2 Mouse plasma proteaseRIAMouse plasmaIn Vivohttps://pdf.sciencedirectassets.com/271102/1-s2.0-S0014579300X09702/1-s2.0-0014579381802888/main.pdf?X-Amz-Security-Token=IQoJb3JpZ2luX2VjEIr%2F%2F%2F%2F%2F%2F%2F%2F%2F%2FwEaCXVzLWVhc3QtMSJHMEUCIQD62SR4A%2B4hs8dyDimRd8i4eqjFdUt5lDROOjPQfQfVdAIgCzazhyIQYpOf0Ptr2TaxQcJ0gfc0tFJSvp00rqp72KMqsgUIExAFGgwwNTkwMDM1NDY4NjUiDFKOQuOPiilKRo0IGiqPBYnEsqS8aZVPDGyG07f6LcX2zV6C1BU1jQ%2BiYzudplRLnaMGn2dzKqD0IgA3jsmhp7CPygQevWTs4Ed1E%2FEvWjuhN8AOvlXEs2Af0t7zL6%2Ba6LtjwN7ZRUIgQGtEhxXKjkWXm9SbXNXu%2FW%2B0ZCHb36rhKfxxcw6e3m0TTTQ5VBU5YtjFRc9KPiAZsUvrVg42y6wbkYdoImtbRueY2e67MmEBizqQ12ayvDeaiudwbYmOGBGr%2BGvimIbEui5OYl1NgebT3Q8%2F%2F5MQ6z0bJxhTQQvplmdG7ymlRrCWfaYdi6ama4%2FpLbZKNVGuU9hscZNpcQUayR82zK3CBh9HRLr%2BTXe6OyFGBRn56BpJ1b%2Bh7qQZYMWBDZGMQdNungv743HpUHMuIxKAt3%2B8SEJ1WkfsIsptsTXEJ%2Fe5Pe2WTSkejT7b9WNpvYncidJCF2lT8NW9RfAw8mc7boYYiFuzqfjULjJV2W6KiXDtf%2F3yQmIV8VRa6hHVovZEQlYpMNpkWgqXznwKL5Lf%2FVUx09SOMK8MoHIWUbF8kgKRM9zGxSs3lPKU7g5gnTqcLwgUKBTnYjjS%2Bm0kz5A4Y4PRE0NI5L4Uy4iF0moVtD6fcXJ7uceU5ofMjnk4jTbla86W0LkLEI6VxBLN2vyWJ%2BkiKXE0GmT7xerhOiY%2FJt74ImPgZVDf6nKzoNAKgoEW5yIBW8X8eRQhNQgbPrCSTSwcAW%2BCoULg4xS3aG87frYuj3ZSUb1DOHzkIRq5G9yj7EjgVbroxu2hh3g9YytLb2PpbvOVSTe%2B%2F2zm04ZibPDOd9UEZQPhgDMGQLnEQ0oKpHU3xaThRzRdTnF%2B6Va%2F7nTk9HXfj3MLfKH3vRbkHVcuODJZVomDO2Awq9mnuQY6sQFg6uBpRDSJbdGuJM4MBWHMJAuiWcghOQq8RAfYeWwCKcdeeLjIPYYpXygg22s0S36%2BiClhIk6QXuPZWihQ%2BbG2PEAcUOIXqLpPHTWwmjGIGrKcTPHPEJKRYKb6HCmW5yCqSEXiKCKgJXX2OzfABfGdtJxraYtj94rVu3tUZ2J1%2Bp4icKKPMKSJaHNBTuKzqNmpvnDyVRDiT0L2iJhacy9SB9TOXT9U0gMzOfOZeQk%2Famo%3D&X-Amz-Algorithm=AWS4-HMAC-SHA256&X-Amz-Date=20241105T104258Z&X-Amz-SignedHeaders=host&X-Amz-Expires=300&X-Amz-Credential=ASIAQ3PHCVTY7EKIR4FY%2F20241105%2Fus-east-1%2Fs3%2Faws4_request&X-Amz-Signature=da086866fd5ae7aa1850a8ed33269fdcc94d601135b6ec16e293756e1d2b3045&hash=fbb1651e9188cb1c761d3e5215af03584aadf82583c0ccbb7e874e4504a450ee&host=68042c943591013ac2b2430a89b270f6af2c76d8dfd086a07176afe7c76c2c61&pii=0014579381802888&tid=spdf-dbd1ce2d-f820-4e78-8534-eac97584de70&sid=5ffdcf685136184f4559b673ec8c38454df3gxrqb&type=NoneN.A.
5010
332459512021
YAEGTFISDYSIAMDKIRQQNFVNWLLAQKGKKSDWKHNITQ
GIP(1–42)42FreeFreeLinearLNoneSecreted by entero-endocrine K cells located in the proximal intestineInsulinotrophic EffectBlood samples (50 μL) were drawn from the retro-orbital plexus at t = 0, 1, 3, 5, 10 and 20 min and then co-incubation with Val-Pyr25 nmol/kg5 ± 0.6Mouse plasma proteaseRIAMouse plasmaIn Vivohttps://pdf.sciencedirectassets.com/271102/1-s2.0-S0014579300X09702/1-s2.0-0014579381802888/main.pdf?X-Amz-Security-Token=IQoJb3JpZ2luX2VjEIr%2F%2F%2F%2F%2F%2F%2F%2F%2F%2FwEaCXVzLWVhc3QtMSJHMEUCIQD62SR4A%2B4hs8dyDimRd8i4eqjFdUt5lDROOjPQfQfVdAIgCzazhyIQYpOf0Ptr2TaxQcJ0gfc0tFJSvp00rqp72KMqsgUIExAFGgwwNTkwMDM1NDY4NjUiDFKOQuOPiilKRo0IGiqPBYnEsqS8aZVPDGyG07f6LcX2zV6C1BU1jQ%2BiYzudplRLnaMGn2dzKqD0IgA3jsmhp7CPygQevWTs4Ed1E%2FEvWjuhN8AOvlXEs2Af0t7zL6%2Ba6LtjwN7ZRUIgQGtEhxXKjkWXm9SbXNXu%2FW%2B0ZCHb36rhKfxxcw6e3m0TTTQ5VBU5YtjFRc9KPiAZsUvrVg42y6wbkYdoImtbRueY2e67MmEBizqQ12ayvDeaiudwbYmOGBGr%2BGvimIbEui5OYl1NgebT3Q8%2F%2F5MQ6z0bJxhTQQvplmdG7ymlRrCWfaYdi6ama4%2FpLbZKNVGuU9hscZNpcQUayR82zK3CBh9HRLr%2BTXe6OyFGBRn56BpJ1b%2Bh7qQZYMWBDZGMQdNungv743HpUHMuIxKAt3%2B8SEJ1WkfsIsptsTXEJ%2Fe5Pe2WTSkejT7b9WNpvYncidJCF2lT8NW9RfAw8mc7boYYiFuzqfjULjJV2W6KiXDtf%2F3yQmIV8VRa6hHVovZEQlYpMNpkWgqXznwKL5Lf%2FVUx09SOMK8MoHIWUbF8kgKRM9zGxSs3lPKU7g5gnTqcLwgUKBTnYjjS%2Bm0kz5A4Y4PRE0NI5L4Uy4iF0moVtD6fcXJ7uceU5ofMjnk4jTbla86W0LkLEI6VxBLN2vyWJ%2BkiKXE0GmT7xerhOiY%2FJt74ImPgZVDf6nKzoNAKgoEW5yIBW8X8eRQhNQgbPrCSTSwcAW%2BCoULg4xS3aG87frYuj3ZSUb1DOHzkIRq5G9yj7EjgVbroxu2hh3g9YytLb2PpbvOVSTe%2B%2F2zm04ZibPDOd9UEZQPhgDMGQLnEQ0oKpHU3xaThRzRdTnF%2B6Va%2F7nTk9HXfj3MLfKH3vRbkHVcuODJZVomDO2Awq9mnuQY6sQFg6uBpRDSJbdGuJM4MBWHMJAuiWcghOQq8RAfYeWwCKcdeeLjIPYYpXygg22s0S36%2BiClhIk6QXuPZWihQ%2BbG2PEAcUOIXqLpPHTWwmjGIGrKcTPHPEJKRYKb6HCmW5yCqSEXiKCKgJXX2OzfABfGdtJxraYtj94rVu3tUZ2J1%2Bp4icKKPMKSJaHNBTuKzqNmpvnDyVRDiT0L2iJhacy9SB9TOXT9U0gMzOfOZeQk%2Famo%3D&X-Amz-Algorithm=AWS4-HMAC-SHA256&X-Amz-Date=20241105T104258Z&X-Amz-SignedHeaders=host&X-Amz-Expires=300&X-Amz-Credential=ASIAQ3PHCVTY7EKIR4FY%2F20241105%2Fus-east-1%2Fs3%2Faws4_request&X-Amz-Signature=da086866fd5ae7aa1850a8ed33269fdcc94d601135b6ec16e293756e1d2b3045&hash=fbb1651e9188cb1c761d3e5215af03584aadf82583c0ccbb7e874e4504a450ee&host=68042c943591013ac2b2430a89b270f6af2c76d8dfd086a07176afe7c76c2c61&pii=0014579381802888&tid=spdf-dbd1ce2d-f820-4e78-8534-eac97584de70&sid=5ffdcf685136184f4559b673ec8c38454df3gxrqb&type=NoneN.A.
5011
331354602021
HSQGTFTSDYSKYLDSRRAQDFVQWLMNT
Glucagon29FreeFreeLinearLNoneProduced by the alpha cells of the pancreasAntidiabetes1 day0.65 ng/kg/min from 1100 (120 min) till the end of the study at 1400 (300 min) 4.01 ± 1.19Human male blood proteaseTwo site ELISA Human male blood sampleIn Vivopdb id: 1GCNNoneN.A.
5012
331354602021
HSQGTFTSDYSKYLDSRRAQDFVQWLMNT
Glucagon29FreeFreeLinearLNoneProduced by the alpha cells of the pancreasAntidiabetes1 day0.65 ng/kg/min from 1100 (120 min) till the end of the study at 1400 (300 min) 3.94 ± 1.10Human female blood proteaseTwo site ELISA Human female blood sampleIn Vivopdb id: 1GCNNoneN.A.
5013
331354602021
HSQGTFTSDYSKYLDSRRAQDFVQWLMNT
Glucagon29FreeFreeLinearLNoneProduced by the alpha cells of the pancreasAntidiabetes1 day0.65 ng/kg/min from 1100 (120 min) till the end of the study at 1400 (300 min) 3.96 ± 1.12Human blood protease (All)Two site ELISA Human blood sample (All)In Vivopdb id: 1GCNNoneN.A.
5014
331298372021
VDKPPYLPRPRPIRrPGGr
OM19r-819FreeAmidationLinearMixreplacing L-Arg15,19 with D-Arg15,19Derived from the antibacterial peptide OM19RAntibacterialBlood samples were collected in 1.5 mL capacity disposable tubes at 0.125, 0.25, 0.5, 0.75, 1, 5, 10, 15, 30, 45, 60 and 75min1 mg/ml1.632 ± 0.34 (Elimination Half Life)Wistar rats blood proteaseN.A.Wistar rats blood sampleIn VivoNoneNoneMIC(μM) = 1 for OM19r -8 in E. coli ATCC25922, OM19r-8 and 250 mPEG5-OM19r-8 showed no cytotoxicity at the concentration up to 32 µM, hemolytic activity of OM19r-8 and mPEG5-OM19r-8 was < 10% at the determined concentration (1-128 μM), which was obviously superior to the control peptide melittin
5015
331298372021
VDKPPYLPRPRPIRrPGGr
mPEG5- OM19r-8 19mPEG5AmidationLinearMixreplacing L-Arg15,19 with D-Arg15,19Derived from the antibacterial peptide OM19RAntibacterialBlood samples were collected in 1.5 mL capacity disposable tubes at 0.125, 0.25, 0.5, 0.75, 1, 5, 10, 15, 30, 45, 60 and 75min1 mg/ml28.09 ± 2.81 (Elimination Half Life)Wistar rats blood proteaseN.A.Wistar rats blood sampleIn VivoNoneNoneMIC(μM) = 1 for OM19r -8 in E. coli ATCC25922, OM19r-8 and 250 mPEG5-OM19r-8 showed no cytotoxicity at the concentration up to 32 µM, hemolytic activity of OM19r-8 and mPEG5-OM19r-8 was < 10% at the determined concentration (1-128 μM), which was obviously superior to the control peptide melittin
5016
331298372021
VDKPPYLPRPRPIRrPGGr
OM19r-819FreeAmidationLinearMixreplacing L-Arg15,19 with D-Arg15,19Derived from the antibacterial peptide OM19RAntibacterialAliquots were analyzed after 0, 20, 30, 40, 60, 80, 90, 100, 120, 150, 180, 210, 240, 175 and 270min31.5 μmol/L71.10 ± 3.43Wistar rats blood plasma proteaseHPLCWistar rats blood plasmaIn VitroNoneNoneMIC(μM) = 1 for OM19r -8 in E. coli ATCC25922, OM19r-8 and 250 mPEG5-OM19r-8 showed no cytotoxicity at the concentration up to 32 µM, hemolytic activity of OM19r-8 and mPEG5-OM19r-8 was < 10% at the determined concentration (1-128 μM), which was obviously superior to the control peptide melittin
5017
331298372021
VDKPPYLPRPRPIRrPGGr
mPEG5- OM19r-8 19mPEG5AmidationLinearMixreplacing L-Arg15,19 with D-Arg15,19Derived from the antibacterial peptide OM19RAntibacterialAliquots were analyzed after 0, 20, 30, 40, 60, 80, 90, 100, 120, 150, 180, 210, 240, 270, 300, 400, 600 and 1000min31.5 μmol/L242.44 ± 39.21Wistar rats blood plasma proteaseHPLCWistar rats blood plasmaIn VitroNoneNoneMIC(μM) = 1 for OM19r -8 in E. coli ATCC25922, OM19r-8 and 250 mPEG5-OM19r-8 showed no cytotoxicity at the concentration up to 32 µM, hemolytic activity of OM19r-8 and mPEG5-OM19r-8 was < 10% at the determined concentration (1-128 μM), which was obviously superior to the control peptide melittin
5018
330493032021
HAEGTFTSDVSSYLEGQAAKEFIAWLVKGRGGSGGGGSGGGGSGGGGSLAEAKVLANRELDKYGVSDYYKNLINNAKTVEGVKALIDEILAALP
GLP-GA3-GS-L394FreeFreeLinearLGLP-1 linked with GA3 through L3 linker, FITC labeledSyntheticAntidiabetes8 h at 4 ◦C50 μg36.3 ± 7.8Mice plasma proteaseFluorescence assayMice plasmaIn VivoNoneNoneBased on the ELISA method, we also found that the fusion proteins containing GA3, ABD035 and ABDCon showed no significant difference in apparent affinity for HSA (P > 0.50)
5019
330493032021
HAEGTFTSDVSSYLEGQAAKEFIAWLVKGRGGSGGGGSGGGGSGGGGSLAEAKVLANRELDKYGVSDFYKRLINKAKVEGVEALKLHILAALP
GLPABD035-GS-L393FreeFreeLinearLGLP-1 linked with ABD035 through L3 linker, amino acid subsituitions with F,R,K,E,K,L,H, FITC labeledSyntheticAntidiabetes8 h at 4 ◦C50 μg31.3 ± 1.0Mice plasma proteaseFluorescence assayMice plasmaIn VivoNoneNoneBased on the ELISA method, we also found that the fusion proteins containing GA3, ABD035 and ABDCon showed no significant difference in apparent affinity for HSA (P > 0.50)
5020
330493032021
HAEGTFTSDVSSYLEGQAAKEFIAWLVKGRGGSGGGGSGGGGSGGGGSLKEAKEKAIEELKKAGITSDYYFDLINKAKTVEGVNALKDEILKA
GLP-ABDCon-GS-L393FreeFreeLinearLGLP-1 linked with ABDCon through L3 linker, amino acid subsituitions with K,E,K,I,E,K,I,T,F,D,K,N,K,K, FITC labeledSyntheticAntidiabetes8 h at 4 ◦C50 μg38.3 ± 2.7Mice plasma proteaseFluorescence assayMice plasmaIn VivoNoneNoneBased on the ELISA method, we also found that the fusion proteins containing GA3, ABD035 and ABDCon showed no significant difference in apparent affinity for HSA (P > 0.50)
5021
327780372021
RRWVRRVRRWVRRVVRVVRRWVRR
[14C]-WLBU224C14 labelingFreeLinearLNoneSyntheticAntimicrobialN.A.15 mg/kg22 (Radioactivity Half Life)CD1 female mice plasma proteaseRadiochromatographyCD1 female mice plasmaIn VivoNoneNoneN.A.
5022
338225912021
MKIILWLCVFGLFLATLFPISWQMPVESGLSSEDSASSESFASKIKRHGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPSG
MS−[Gln28]exenatide87FreeFreeLinearLConventional unsubstituted β-eliminative linker, linked by a GDM linker and Mod = (CH3)2NSO2−Exendin-4 analogsAntidiabetespH 7.4, 37 °CN.A.~2020 (Release Half Life)N.A.N.A.N.A.In VitroPDB id: 7MLLNoneN.A.
5023
338225912021
MKIILWLCVFGLFLATLFPISWQMPVESGLSSEDSASSESFASKIKRHGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPSG
MS−[Gln28]exenatide87FreeFreeLinearLConventional unsubstituted β-eliminative linkerExendin-4 analogsAntidiabetespH 7.4, 37 °CN.A.900 (Release Half Life)RatsN.A.RatsIn VivoPDB id: 7MLLNoneN.A.
5024
338225912021
MKIILWLCVFGLFLATLFPISWQMPVESGLSSEDSASSESFASKIKRHGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPSG
MS−[Gln28]exenatide87FreeFreeLinearLwith GDM linker and Mod = (CH3)2NSO2−Exendin-4 analogsAntidiabetespH 7.4, 37 °CN.A.~1800 (Release Half Life)N.A.N.A.N.A.In VitroPDB id: 7MLLNoneN.A.
5025
338225912021
MKIILWLCVFGLFLATLFPISWQMPVESGLSSEDSASSESFASKIKRHGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPSG
MS−[Gln28]exenatide87FreeFreeLinearLConventional unsubstituted β-eliminative linkerExendin-4 analogsAntidiabetespH 7.4, 37 °CN.A.750 (Release Half Life)RatsN.A.RatsIn VivoPDB id: 7MLLNoneN.A.
5026
338013822021
fQWAVGH
[177Lu]Lu-NeoB7Acetylation, 177Lu LabellingAminoethylamide -NH-CH(CH2-CH(CH3)2)2LinearMixNoneDerived from the antagonist GRPR peptide SB3Antitumor (Treatment of Gastrointestinal Stromal Tumors)N.A.N.A.40.2 (Distribution Half Life)N.A.N.A.N.A.N.A.https://pmc.ncbi.nlm.nih.gov/articles/PMC6150197/None[177Lu]Lu-NeoB tumor uptake in 400 pmol group mice (~11% ID/g) was found to be higher than that observed in 800 pmol group mice (~7% ID/g)