For older version click here.

Please wait...

Browsing by Length

Browse Results:

Filter by Year
From
Upto
IDPMIDYEARSequenceNameLengthN-ter MODC-ter MODLinear/CyclicChiralityChem-MODOriginNatureIncubation TimeConcentrationHalf LifeUnits Half LifeProteaseAssayTest SampleVivo/VitroReferencePatent No.Activity
1067
153221252004
DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA
Aβ(1 €“ 42)42FreeFreeLinearLNoneDerivative of human Aprecursor protein APP771Neurodegenerative121 minutes2x107 cpm of 125I-Aβ40 peptide2.8Mouse plasma proteasesRadioactivity measured by scintillation counterIntravenouly injected into male B6SJLF1/J mice and blood samples collected from tail vein to prepare plasma samplesin vivoNoneNoneNeurodegeneration caused by oligomerization
1080
115536912001
KKKQYTSIHHGVVEVDAAVTPEERHLSKMQQNGYENPTYKFFEQMQNIATVIVITLVML
APP-C5959FreeFreeLinearLNoneAmyloid precursor protein derivativeRegulator of synapse formation2 hoursNot mentioned~5Fetal calf serum proteasesPulse chase experimentBHK cell linein vitroNoneNoneNot reported
1081
115536912001
KKKQYTSIHHGVVEVDAAVTPEERHLSKMQQNGYENPTYKFFEQMQNIATVIVITLVML
APP-C5959FreeFreeLinearLNoneAmyloid precursor protein derivativeRegulator of synapse formation2 hoursNot mentioned~5Fetal calf serum proteasesPulse chase experimentPrimary cultures of neurons from PS1 knockout mice's 14 day embryosin vitroNoneNoneNot reported
1108
152468692004
YAEGTFISDYSIAMDKIHQQDFVNWLLAQKGKKNDWKHNITQ
GIP42FreeFreeLinearLNoneGastrointestinal incretin hormonePotentiate postprandial insulin secretion and glucose clearance12 hours2mM6Human plasma proteaseRadioimmunoassayHuman plasmain vitro8446620NonecAMP EC50=21.8 ±1.5nM
1109
152468692004
Y-Abu-EGTFISDYSIAMDKIHQQDFVNWLLAQKGKKNDWKHNITQ
(Abu2)GIP42FreeFreeLinearL2-aminobutyric acid (Abu)SyntheticPotentiate postprandial insulin secretion and glucose clearance12 hours2mM7.1Human plasma proteaseRadioimmunoassayHuman plasmain vitroNoneNonecAMP EC50=36.8 ±1.6nM
1111
152468692004
YAEGTFISDYSIAMDKIHQQDFVNWLLAQKGKKNDWKHNITQ
GIP42FreeFreeLinearLNoneGastrointestinal incretin hormonePotentiate postprandial insulin secretion and glucose clearance12 hours2mM>12Human plasma proteases except DPPRadioimmunoassayHuman plasma+DPA (DPA is DPP inhibitor)in vitro8446620NonecAMP EC50=21.8 ±1.5nM
1221
205934702010
GGFAEGTFTSDVSSYLEGQAAKEFIAWLVKGRPSSGAPPPS
Peptide 141FreeAmidationLinearLNoneSynthetic dipeptide extended GLP-analogsRegulate blood glucose168 hoursNot mentioned0.9NoneHPLCPBSin vitroNoneNoneNot reported
1222
205934702010
GGFAEGTFTSDVSSYLEGQAAKEFIAWLVKGRPSSGAPPPS
Peptide 241FreeAmidationLinearLNoneSynthetic dipeptide extended GLP-analogsRegulate blood glucose168 hoursNot mentioned1.1NoneHPLCPBSin vitroNoneNoneNot reported
1223
205934702010
GFFAEGTFTSDVSSYLEGQAAKEFIAWLVKGRPSSGAPPPS
Peptide 341FreeAmidationLinearLNoneSynthetic dipeptide extended GLP-analogsRegulate blood glucose168 hoursNot mentioned0.7NoneHPLCPBSin vitroNoneNoneNot reported
1224
205934702010
GfFAEGTFTSDVSSYLEGQAAKEFIAWLVKGRPSSGAPPPS
Peptide 441FreeAmidationLinearMixNoneSynthetic dipeptide extended GLP-analogsRegulate blood glucose168 hoursNot mentioned0.9NoneHPLCPBSin vitroNoneNoneNot reported
1225
205934702010
GVFAEGTFTSDVSSYLEGQAAKEFIAWLVKGRPSSGAPPPS
Peptide 541FreeAmidationLinearLNoneSynthetic dipeptide extended GLP-analogsRegulate blood glucose168 hoursNot mentioned4.7NoneHPLCPBSin vitroNoneNoneNot reported
1226
205934702010
GvFAEGTFTSDVSSYLEGQAAKEFIAWLVKGRPSSGAPPPS
Peptide 641FreeAmidationLinearMixNoneSynthetic dipeptide extended GLP-analogsRegulate blood glucose168 hoursNot mentioned5.1NoneHPLCPBSin vitroNoneNoneNot reported
1227
205934702010
G-tBu-FAEGTFTSDVSSYLEGQAAKEFIAWLVKGRPSSGAPPPS
Peptide 741FreeAmidationLinearLtBu=tertiary butylSynthetic dipeptide extended GLP-analogsRegulate blood glucose168 hoursNot mentioned>168NoneHPLCPBSin vitroNoneNoneNot reported
1228
205934702010
G-PhG-FAEGTFTSDVSSYLEGQAAKEFIAWLVKGRPSSGAPPPS
Peptide 841FreeAmidationLinearLPhG=phenylglycineSynthetic dipeptide extended GLP-analogsRegulate blood glucose168 hoursNot mentioned0.5NoneHPLCPBSin vitroNoneNoneNot reported
1229
205934702010
G-Aib-FAEGTFTSDVSSYLEGQAAKEFIAWLVKGRPSSGAPPPS
Peptide 941FreeAmidationLinearLAib=α-aminoisobutyric acidSynthetic dipeptide extended GLP-analogsRegulate blood glucose168 hoursNot mentioned0.8NoneHPLCPBSin vitroNoneNoneNot reported
1230
205934702010
GVFAEGTFTSDVSSYLEGQAAKEFIAWLVKGRPSSGAPPPS
Peptide 1041FreeAmidationLinearLNoneSynthetic dipeptide extended GLP-analogsRegulate blood glucose168 hoursNot mentioned20.4NoneHPLCPBSin vitroNoneNoneNot reported
1231
205934702010
FGFAEGTFTSDVSSYLEGQAAKEFIAWLVKGRPSSGAPPPS
Peptide 1141FreeAmidationLinearLNoneSynthetic dipeptide extended GLP-analogsRegulate blood glucose168 hoursNot mentioned2.5NoneHPLCPBSin vitroNoneNoneEC50=0.23 ±0.10nM
1232
205934702010
FAFAEGTFTSDVSSYLEGQAAKEFIAWLVKGRPSSGAPPPS
Peptide 1241FreeAmidationLinearLNoneSynthetic dipeptide extended GLP-analogsRegulate blood glucose168 hoursNot mentioned2.8NoneHPLCPBSin vitroNoneNoneNot reported
1233
205934702010
FaFAEGTFTSDVSSYLEGQAAKEFIAWLVKGRPSSGAPPPS
Peptide 1341FreeAmidationLinearLNoneSynthetic dipeptide extended GLP-analogsRegulate blood glucose168 hoursNot mentioned2.4NoneHPLCPBSin vitroNoneNoneNot reported
1234
205934702010
FFFAEGTFTSDVSSYLEGQAAKEFIAWLVKGRPSSGAPPPS
Peptide 1441FreeAmidationLinearLNoneSynthetic dipeptide extended GLP-analogsRegulate blood glucose168 hoursNot mentioned33.3NoneHPLCPBSin vitroNoneNoneNot reported
1235
205934702010
FfFAEGTFTSDVSSYLEGQAAKEFIAWLVKGRPSSGAPPPS
Peptide 1541FreeAmidationLinearLNoneSynthetic dipeptide extended GLP-analogsRegulate blood glucose168 hoursNot mentioned7.7NoneHPLCPBSin vitroNoneNoneEC50=0.77 ±0.25
1236
205934702010
FVFAEGTFTSDVSSYLEGQAAKEFIAWLVKGRPSSGAPPPS
Peptide 1641FreeAmidationLinearLNoneSynthetic dipeptide extended GLP-analogsRegulate blood glucose168 hoursNot mentioned>168NoneHPLCPBSin vitroNoneNoneNot reported
1237
205934702010
FvFAEGTFTSDVSSYLEGQAAKEFIAWLVKGRPSSGAPPPS
Peptide 1741FreeAmidationLinearLNoneSynthetic dipeptide extended GLP-analogsRegulate blood glucose168 hoursNot mentioned50.6NoneHPLCPBSin vitroNoneNoneEC50=0.04 ±0.06nM
1238
205934702010
FVFAEGTFTSDVSSYLEGQAAKEFIAWLVKGRPSSGAPPPS
Peptide 1841FreeAmidationLinearLNoneSynthetic dipeptide extended GLP-analogsRegulate blood glucose168 hoursNot mentioned64NoneHPLCPBSin vitroNoneNoneEC50=2.07 ±0.41nM
1683
98226651998
MLPGLALLLLAAWTARALEVPYPYDVPDYASNKGAIIGLMVGGVVIATVIVITLVVMLKKKQYEQKLISEEDL
H26-57C74FreeFreeLinearLNoneAmyloid precursor proteinNot mentioned40 minutesNot mentioned8γ-secretasePulse chase experimentHuman embryonic kidney cellsin vitroNoneNoneNot mentioned
1684
98226651998
MLPGLALLLLAAWTARALEVPYPYDVPDYASNKGAIIGLMVGGVVIATVIVITLVVMLKKKQYEQKLISEEDL
H26-57C74FreeFreeLinearLNoneAmyloid precursor proteinNot mentioned40 minutesNot mentioned1γ-secretase (protease) Lactacystin(protease inhibitor)Pulse chase experimentHuman embryonic kidney cellsin vitroNoneNoneNot mentioned
1685
98226651998
MLPGLALLLLAAWTARALEVPYPYDVPDYASNKGAIIGLMVGGVVIATVIVITLVVMLKKKQYEQKLISEEDL
H26-57C74FreeFreeLinearLNoneAmyloid precursor proteinNot mentioned40 minutesNot mentioned10γ-secretase (protease) ALLN(protease inhibitor)Pulse chase experimentHuman embryonic kidney cellsin vitroNoneNoneNot mentioned
1697
82220931993
VVYTDCTESGQNLCLCEGSNVCGQGNKCILGSDGEKNQCVTGEGTPKPQSHNDGDFEEIPEEYLQ
Recombinant hirudin65FreeFreeLinearLNoneNot availableAnticoagulantNot reported1000ng/ml2 to 3Not mentionedELISAHuman blood samplein vivoNoneNoneNot mentioned
1749
160999412005
ELRMSSSYPTGLADVKAGPAQTLIRPQDMKGASRSPEDSSPDAARIRV
proADM 45 €“92 (Adrenomedullin)48FreeFreeLinearLNoneSynthetically synthesised proADM 45 €“92Vasodilatory peptideNot reported0.29nmol/L22Human blood proteasesSandwich immunoluminometric AssayHuman blood plasmain vitroNoneNoneNot given
1971
185530942008
HPLGSPGSASDLETSGLQEQRNHLQGKLSELQVEQTSLEPLQESPRTPGVWKSREVATEGIRGHRKMVLYTLRAPR
NT-proBNP76FreeFreeLinearLNonePro-Brain natriuretic peptideVasodilatorNot reportedNot mentioned~120Human blood proteasesELISAHuman plasmain vitroNoneNoneNot available
2011
172924922007
NPMYNAVSNADLMDFKNLLDHLEEKMPLEDEVVPPQVLSEPNEEAGAALSPLPEVPPWTGEVSPAQRDGGALGRGPWDSSDRSALLKSKLRALLTAPR
NT-ANP98FreeFreeLinearLNoneANP (A- type natriuretic peptide)Natriuretic, diuretic and vasorelaxantNot reported650fmol/ml1Human blood proteasesRadioimmunoassayHuman bloodin vitroNoneNoneNot mentioned
2059
216649382011
HAECTFTSDVSSYLEGQAAKEFIAWLCKGRGCPSSGAPPPSGGGGG
GLP715a46FreeFreeLinearLNoneProglucagon moleculeAnti-hyperglycemic hormoneNot reported300 μg/kg48Rat blood proteasesELISASerum of rats (Subcutaneous injection)in vivoNoneNoneBinding constants to the GLP-1 receptor= 6.18 ± 1.27nM
2103
N.A.2009
EACNLPIVRGPCIAFFPRWAFDAVKGKCVLFPYGGCQGNGNKFYSEKECREYCGVP
DX-89056FreeFreeLinearLNoneKunitz domain peptideProtease inhibitorN.A.Not mentioned165Rabbit blood proteasesI-125 radiolabelling methodRabbit plasma (Intravenous)in vivoNoneEP2090589A1Inhibition constt (Ki) 6 ±1 pM
2104
N.A.2009
EACNLPIVRGPCIAFFPRWAFDAVKGKCVLFPYGGCQGNGNKFYSEKECREYCGVP
Human Serum Albumin-DX-89056Human serum albuminFreeLinearLNoneKunitz domain peptideProtease inhibitorN.A.Not mentioned3500Rabbit blood proteasesI-125 radiolabelling methodRabbit plasma (Intravenous)in vivoNoneEP2090589A1Inhibition constt (Ki) 7 ±1 pM
2105
N.A.2009
EACNLPIVRGPCIAFFPRWAFDAVKGKCVLFPYGGCQGNGNKFYSEKECREYCGVP
DX-89056FreeFreeLinearLNoneKunitz domain peptideProtease inhibitorN.A.Not mentioned79.44Mouse blood proteasesI-125 radiolabelling methodMouse plasma (Intravenous)in vivoNoneEP2090589A1Not mentioned
2106
N.A.2009
EACNLPIVRGPCIAFFPRWAFDAVKGKCVLFPYGGCQGNGNKFYSEKECREYCGVP
DX-890-Human Serum Albumin56FreeHuman serum albuminLinearLNoneKunitz domain peptideProtease inhibitorN.A.Not mentioned380Mouse blood proteasesI-125 radiolabelling methodMouse plasma (Intravenous)in vivoNoneEP2090589A1Not mentioned
2163
N.A.2011
CFGLKLDRIGSMSGLGCVQQRKESKKPPAKLQPRESKKPPAKLQPR
Chimeric CNP-E46FreeFreeCyclic (C1-C17)LNoneCNP-22 (C-type natriuretic peptide)Third member of natriuretic peptide family with multiple functionsN.A.10 nm/ Kg18.4Rat blood proteasesCompetitive RadioimmunoassayRat plasma (Intravenous)in vivoNoneEP2277890A1Not mentioned
2164
N.A.2011
RPQLKAPPKKSEKRQQVCFGLKLDRIGSMSGLGCVQQRKESKKPPAKLQPR
Chimeric CNP-F51FreeFreeCyclic (C18-C34)LNoneCNP-22 (C-type natriuretic peptide)Third member of natriuretic peptide family with multiple functionsN.A.10 nm/ Kg17.38Rat blood proteasesCompetitive RadioimmunoassayRat plasma (Intravenous)in vivoNoneEP2277890A1Not mentioned
2170
N.A.2011
DLRVDTKSRAAWARLLQEHPNARKYKGANKKGLSKGGLSKGCFGLKLDRIGSMSGLGC
CNP-53 (C-type natriuretic peptide)58FreeFreeCyclic (C42-C58)LNoneCNP-58 (C-type natriuretic peptide)Third member of natriuretic peptide family with multiple functionsN.A.10 nm/ Kg15.72Rat blood proteasesCompetitive RadioimmunoassayRat plasma (Intravenous)in vivoNoneEP2277890A1Not mentioned
2205
N.A.2009
SEEPPISLDLTFHLLREVLEMARAEQLAQQAHSNRKLMEII
Human Corticotropic releasing factor (hCRF)41FreeFreeLinearLNoneHypothalamusInhibitor of edema and inflammationN.A.100 micro g/ Kg62.6Not mentionedELISARat plasma (Subcutaneous)in vivoNoneWO2009027844Not mentioned
2206
N.A.2009
SEEPPISLDLTFHLLREVLEMARAEQLAQQAHSNRKLMEII
Human Corticotropic releasing factor (hCRF)41FreeFreeLinearLNoneHypothalamusInhibitor of edema and inflammationN.A.1000 micro g/ Kg72.1Not mentionedELISARat plasma (Subcutaneous)in vivoNoneWO2009027844Not mentioned
2266
14180021992
GPETLCGAELVDALQFVCGDRGFYFNKPTGYGYGSSRRAPQTGIVDECCFRSCDLRRLMYCAPLKPAKSA
Somatomedin c70FreeFreeLinearLNoneHuman liverGrowth hormoneNot given129.4 ng20Human serum proteasesPeptide specific immunoassayHuman serum samplein vitroPMID 632300NoneSomatomedin C is a prerequisite for normal muscle homeostasis which is disrupted in fibromyalgia. Regression analysis shows that ~7 % low level of somatomedin c in case of fibromyalgia patients.
2296
66059721984
SQEPPISLDLTFHLLREVLEMTKADQLAQQAHSNRKLLDIA
Ovine corticotropic releasing factor41FreeFreeLinearLNoneParaventricular nucleus (PVN) of the hypothalamusUsed as a diagnostic test in disease affecting the Hypothalamic pituitary axis0, 2, 5, 7,10,15, 20, 25, 30, 45, 60, 90, 120, 150, and 180 min.76 μg16.2 (t1/2 fast)Human blood plasma proteasesRadioimmunoassay and HPLC analysisIntravenous administration to human plasmain vivohttp://www.anaspec.com/products/product.asp?id=322NoneNot reported
2297
66059721984
SQEPPISLDLTFHLLREVLEMTKADQLAQQAHSNRKLLDIA
Ovine corticotropic releasing factor41FreeFreeLinearLNoneParaventricular nucleus (PVN) of the hypothalamusUsed as a diagnostic test in disease affecting the Hypothalamic pituitary axis0, 2, 5, 7,10,15, 20, 25, 30, 45, 60, 90, 120, 150, and 180 min.85 μg13.3 (t1/2 fast)Human blood plasma proteasesRadioimmunoassay and HPLC analysisIntravenous administration to human plasmain vivohttp://www.anaspec.com/products/product.asp?id=322NoneNot reported
2298
66059721984
SQEPPISLDLTFHLLREVLEMTKADQLAQQAHSNRKLLDIA
Ovine corticotropic releasing factor41FreeFreeLinearLNoneParaventricular nucleus (PVN) of the hypothalamusUsed as a diagnostic test in disease affecting the Hypothalamic pituitary axis0, 2, 5, 7,10,15, 20, 25, 30, 45, 60, 90, 120, 150, and 180 min.75 μg12.4 (t1/2 fast)Human blood plasma proteasesRadioimmunoassay and HPLC analysisIntravenous administration to human plasmain vivohttp://www.anaspec.com/products/product.asp?id=322NoneNot reported
2299
66059721984
SQEPPISLDLTFHLLREVLEMTKADQLAQQAHSNRKLLDIA
Ovine corticotropic releasing factor41FreeFreeLinearLNoneParaventricular nucleus (PVN) of the hypothalamusUsed as a diagnostic test in disease affecting the Hypothalamic pituitary axis0, 2, 5, 7,10,15, 20, 25, 30, 45, 60, 90, 120, 150, and 180 min.75 μg12.7 (t1/2 fast)Human blood plasma proteasesRadioimmunoassay and HPLC analysisIntravenous administration to human plasmain vivohttp://www.anaspec.com/products/product.asp?id=322NoneNot reported
2300
66059721984
SQEPPISLDLTFHLLREVLEMTKADQLAQQAHSNRKLLDIA
Ovine corticotropic releasing factor41FreeFreeLinearLNoneParaventricular nucleus (PVN) of the hypothalamusUsed as a diagnostic test in disease affecting the Hypothalamic pituitary axis0, 2, 5, 7,10,15, 20, 25, 30, 45, 60, 90, 120, 150, and 180 min.90 μg5.6 (t1/2 fast)Human blood plasma proteasesRadioimmunoassay and HPLC analysisIntravenous administration to human plasmain vivohttp://www.anaspec.com/products/product.asp?id=322NoneNot reported
2301
66059721984
SQEPPISLDLTFHLLREVLEMTKADQLAQQAHSNRKLLDIA
Ovine corticotropic releasing factor41FreeFreeLinearLNoneParaventricular nucleus (PVN) of the hypothalamusUsed as a diagnostic test in disease affecting the Hypothalamic pituitary axis0, 2, 5, 7,10,15, 20, 25, 30, 45, 60, 90, 120, 150, and 180 min.80 μg9.4 (t1/2 fast)Human blood plasma proteasesRadioimmunoassay and HPLC analysisIntravenous administration to human plasmain vivohttp://www.anaspec.com/products/product.asp?id=322NoneNot reported
2302
66059721984
SQEPPISLDLTFHLLREVLEMTKADQLAQQAHSNRKLLDIA
Ovine corticotropic releasing factor41FreeFreeLinearLNoneParaventricular nucleus (PVN) of the hypothalamusUsed as a diagnostic test in disease affecting the Hypothalamic pituitary axis0, 2, 5, 7,10,15, 20, 25, 30, 45, 60, 90, 120, 150, and 180 min.80 μg11.6 (mean t1/2 fast)Human blood plasma proteasesRadioimmunoassay and HPLC analysisIntravenous administration to human plasmain vivohttp://www.anaspec.com/products/product.asp?id=322NoneNot reported
2303
66059721984
SQEPPISLDLTFHLLREVLEMTKADQLAQQAHSNRKLLDIA
Ovine corticotropic releasing factor41FreeFreeLinearLNoneParaventricular nucleus (PVN) of the hypothalamusUsed as a diagnostic test in disease affecting the Hypothalamic pituitary axis0, 2, 5, 7,10,15, 20, 25, 30, 45, 60, 90, 120, 150, and 180 min.76 μg70.8 (t1/2 slow)Human blood plasma proteasesRadioimmunoassay and HPLC analysisIntravenous administration to human plasmain vivohttp://www.anaspec.com/products/product.asp?id=322NoneNot reported
2304
66059721984
SQEPPISLDLTFHLLREVLEMTKADQLAQQAHSNRKLLDIA
Ovine corticotropic releasing factor41FreeFreeLinearLNoneParaventricular nucleus (PVN) of the hypothalamusUsed as a diagnostic test in disease affecting the Hypothalamic pituitary axis0, 2, 5, 7,10,15, 20, 25, 30, 45, 60, 90, 120, 150, and 180 min.85 μg49.5 (t1/2 slow)Human blood plasma proteasesRadioimmunoassay and HPLC analysisIntravenous administration to human plasmain vivohttp://www.anaspec.com/products/product.asp?id=322NoneNot reported
2305
66059721984
SQEPPISLDLTFHLLREVLEMTKADQLAQQAHSNRKLLDIA
Ovine corticotropic releasing factor41FreeFreeLinearLNoneParaventricular nucleus (PVN) of the hypothalamusUsed as a diagnostic test in disease affecting the Hypothalamic pituitary axis0, 2, 5, 7,10,15, 20, 25, 30, 45, 60, 90, 120, 150, and 180 min.75 μg95.4 (t1/2 slow)Human blood plasma proteasesRadioimmunoassay and HPLC analysisIntravenous administration to human plasmain vivohttp://www.anaspec.com/products/product.asp?id=322NoneNot reported
2306
66059721984
SQEPPISLDLTFHLLREVLEMTKADQLAQQAHSNRKLLDIA
Ovine corticotropic releasing factor41FreeFreeLinearLNoneParaventricular nucleus (PVN) of the hypothalamusUsed as a diagnostic test in disease affecting the Hypothalamic pituitary axis0, 2, 5, 7,10,15, 20, 25, 30, 45, 60, 90, 120, 150, and 180 min.75 μg90.8 (t1/2 slow)Human blood plasma proteasesRadioimmunoassay and HPLC analysisIntravenous administration to human plasmain vivohttp://www.anaspec.com/products/product.asp?id=322NoneNot reported
2307
66059721984
SQEPPISLDLTFHLLREVLEMTKADQLAQQAHSNRKLLDIA
Ovine corticotropic releasing factor41FreeFreeLinearLNoneParaventricular nucleus (PVN) of the hypothalamusUsed as a diagnostic test in disease affecting the Hypothalamic pituitary axis0, 2, 5, 7,10,15, 20, 25, 30, 45, 60, 90, 120, 150, and 180 min.90 μg47.9 (t1/2 slow)Human blood plasma proteasesRadioimmunoassay and HPLC analysisIntravenous administration to human plasmain vivohttp://www.anaspec.com/products/product.asp?id=322NoneNot reported
2308
66059721984
SQEPPISLDLTFHLLREVLEMTKADQLAQQAHSNRKLLDIA
Ovine corticotropic releasing factor41FreeFreeLinearLNoneParaventricular nucleus (PVN) of the hypothalamusUsed as a diagnostic test in disease affecting the Hypothalamic pituitary axis0, 2, 5, 7,10,15, 20, 25, 30, 45, 60, 90, 120, 150, and 180 min.80 μg83.5 (t1/2 slow)Human blood plasma proteasesRadioimmunoassay and HPLC analysisIntravenous administration to human plasmain vivohttp://www.anaspec.com/products/product.asp?id=322NoneNot reported
2309
66059721984
SQEPPISLDLTFHLLREVLEMTKADQLAQQAHSNRKLLDIA
Ovine corticotropic releasing factor41FreeFreeLinearLNoneParaventricular nucleus (PVN) of the hypothalamusUsed as a diagnostic test in disease affecting the Hypothalamic pituitary axis0, 2, 5, 7,10,15, 20, 25, 30, 45, 60, 90, 120, 150, and 180 min.80 μg73.0 (mean t1/2 slow)Human blood plasma proteasesRadioimmunoassay and HPLC analysisIntravenous administration to human plasmain vivohttp://www.anaspec.com/products/product.asp?id=322NoneNot reported
2392
111455792001
GPETLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSA
Insulin like growth factor 1 (IGF-1)70FreeFreeLinearLI125 radiolabelingHuman IGF-1Regulate somatic growth and cellular proliferation1, 5, 15, and 30 min and at 1, 2, 4, 8, and 24 h15 μCi(0.2 ml)0.033 ±0.004 (t1/2 α)Rat blood proteasesTCA precipitationIntravenous injection into ratin vivoPMID:7758431NoneHuman articular cartilage explant is taken and cultured in humidified environment, explant is treated with 40ng/ml of IGF-1, E3A,F49A for 5 days. Proteoglycan synthesis(matrix) synthesis is increased ~ 3 times in E3A/F49A treated sampleas compare to control as measured by scientillation counter.
2393
111455792001
GPETLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSA
Insulin like growth factor 1 (IGF-1)70FreeFreeLinearLI125 radiolabelingHuman IGF-1Regulate somatic growth and cellular proliferation1, 5, 15, and 30 min and at 1, 2, 4, 8, and 24 h15 μCi(0.2 ml)1.22 ±0.237 (t1/2 β)Rat blood proteasesTCA precipitationIntravenous injection into ratin vivoPMID:7758431NoneHuman articular cartilage explant is taken and cultured in humidified environment, explant is treated with 40ng/ml of IGF-1, E3A,F49A for 5 days. Proteoglycan synthesis(matrix) synthesis is increased ~ 3 times in E3A/F49A treated sampleas compare to control as measured by scientillation counter.
2394
111455792001
GPETLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSA
Insulin like growth factor 1 (IGF-1)70FreeFreeLinearLI125 radiolabelingHuman IGF-1Regulate somatic growth and cellular proliferation1, 5, 15, and 30 min and at 1, 2, 4, 8, and 24 h15 μCi(0.2 ml)5.88 ±0.374 (t1/2 Î¥)Rat blood proteasesTCA precipitationIntravenous injection into ratin vivoPMID:7758431NoneHuman articular cartilage explant is taken and cultured in humidified environment, explant is treated with 40ng/ml of IGF-1, E3A,F49A for 5 days. Proteoglycan synthesis(matrix) synthesis is increased ~ 3 times in E3A/F49A treated sampleas compare to control as measured by scientillation counter.
2395
111455792001
GPETLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSA
Analogue of Insulin like growth factor 1 (F49A)70FreeFreeLinearLI125 radiolabelingHuman IGF-1Regulate somatic growth and cellular proliferation1, 5, 15, and 30 min and at 1, 2, 4, 8, and 24 h15 μCi(0.2 ml)0.064 ±0.052 (t1/2 α)Rat blood proteasesTCA precipitationIntravenous injection into ratin vivoPMID:7758431NoneHuman articular cartilage explant is taken and cultured in humidified environment, explant is treated with 40ng/ml of IGF-1, E3A,F49A for 5 days. Proteoglycan synthesis(matrix) synthesis is increased ~ 3 times in E3A/F49A treated sampleas compare to control as measured by scientillation counter.
2396
111455792001
GPETLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSA
Analogue of Insulin like growth factor 1 (F49A)70FreeFreeLinearLI125 radiolabelingHuman IGF-1Regulate somatic growth and cellular proliferation1, 5, 15, and 30 min and at 1, 2, 4, 8, and 24 h15 μCi(0.2 ml)0.971 ±0.336 (t1/2 β)Rat blood proteasesTCA precipitationIntravenous injection into ratin vivoPMID:7758431NoneHuman articular cartilage explant is taken and cultured in humidified environment, explant is treated with 40ng/ml of IGF-1, E3A,F49A for 5 days. Proteoglycan synthesis(matrix) synthesis is increased ~ 3 times in E3A/F49A treated sampleas compare to control as measured by scientillation counter.
2397
111455792001
GPETLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSA
Analogue of Insulin like growth factor 1 (F49A)70FreeFreeLinearLI125 radiolabelingHuman IGF-1Regulate somatic growth and cellular proliferation1, 5, 15, and 30 min and at 1, 2, 4, 8, and 24 h15 μCi(0.2 ml)8.97 ±4.50 (t1/2 Î¥)Rat blood proteasesTCA precipitationIntravenous injection into ratin vivoPMID:7758431NoneHuman articular cartilage explant is taken and cultured in humidified environment, explant is treated with 40ng/ml of IGF-1, E3A,F49A for 5 days. Proteoglycan synthesis(matrix) synthesis is increased ~ 3 times in E3A/F49A treated sampleas compare to control as measured by scientillation counter.
2398
111455792001
GPATLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSA
Analogue of Insulin like growth factor 1 (E3A/F49A)70FreeFreeLinearLI125 radiolabelingHuman IGF-1Regulate somatic growth and cellular proliferation1, 5, 15, and 30 min and at 1, 2, 4, 8, and 24 h15 μCi(0.2 ml)0.032 ±0.005 (t1/2 α)Rat blood proteasesTCA precipitationIntravenous injection into ratin vivoPMID:7758431NoneHuman articular cartilage explant is taken and cultured in humidified environment, explant is treated with 40ng/ml of IGF-1, E3A,F49A for 5 days. Proteoglycan synthesis(matrix) synthesis is increased ~ 3 times in E3A/F49A treated sampleas compare to control as measured by scientillation counter.
2399
111455792001
GPATLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSA
Analogue of Insulin like growth factor 1 (E3A/F49A)70FreeFreeLinearLI125 radiolabelingHuman IGF-1Regulate somatic growth and cellular proliferation1, 5, 15, and 30 min and at 1, 2, 4, 8, and 24 h15 μCi(0.2 ml)0.321 ±0.0.091 (t1/2 β)Rat blood proteasesTCA precipitationIntravenous injection into ratin vivoPMID:7758431NoneHuman articular cartilage explant is taken and cultured in humidified environment, explant is treated with 40ng/ml of IGF-1, E3A,F49A for 5 days. Proteoglycan synthesis(matrix) synthesis is increased ~ 3 times in E3A/F49A treated sampleas compare to control as measured by scientillation counter.
2400
111455792001
GPATLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSA
Analogue of Insulin like growth factor 1 (E3A/F49A)70FreeFreeLinearLI125 radiolabelingHuman IGF-1Regulate somatic growth and cellular proliferation1, 5, 15, and 30 min and at 1, 2, 4, 8, and 24 h15 μCi(0.2 ml)6.23 ±1.47 (t1/2 Î¥)Rat blood proteasesTCA precipitationIntravenous injection into ratin vivoPMID:7758431NoneHuman articular cartilage explant is taken and cultured in humidified environment, explant is treated with 40ng/ml of IGF-1, E3A,F49A for 5 days. Proteoglycan synthesis(matrix) synthesis is increased ~ 3 times in E3A/F49A treated sampleas compare to control as measured by scientillation counter.
2401
18248071991
AELRCMCIKTTSGIHPKNIQSLEVIGKGTHCNQVEVIATLKDGRKICLDPDAPRIKKIVQKKLAGDESAD
naP-2 (Neutrophil-activatingprotein-2)70FreeFreeLinearLNonebeta- thromboglobulinInflammatory peptide48 hours20 pmol/site65-75Rabbit blood proteasesNot mentionedIntradermal injection in rabbitin vivoNoneNoneP- 2 elicited inflammatory responses (neutrophil emigration, edema formation at 20 pmol/l
2424
75616321995
GPETLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSA
Insulin-like growth factor-I (IGF-I)70FreeFreeLinearLI125 labelingHuman IGF-1Growth Hormone5, 10, 20, 30 or 60 min8.6ng8Rat Stomach luminal flushing proteasesTCA precipitationRat Stomach luminal flushingin vitro632300NoneStimulate gut growth and repair
2425
75616321995
GPETLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSA
Insulin-like growth factor-I (IGF-I)70FreeFreeLinearLI125 labelingHuman IGF-1Growth Hormone5, 10, 20, 30 or 60 min8.6ng5Rat Stomach luminal flushing proteasesAntibody assayRat Stomach luminal flushingin vitro632300NoneStimulate gut growth and repair
2426
75616321995
GPETLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSA
Insulin-like growth factor-I (IGF-I)70FreeFreeLinearLI125 labelingHuman IGF-1Growth Hormone5, 10, 20, 30 or 60 min8.6ng2.5Rat Stomach luminal flushing proteasesReceptor-precipitable radioactivityRat Stomach luminal flushingin vitro632300NoneStimulate gut growth and repair
2427
75616321995
GPETLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSA
Insulin-like growth factor-I (IGF-I)70FreeFreeLinearLI125 labelingHuman IGF-1Growth Hormone2-5, 5, 7-5, 10 or 20min8.6ng2Rat Duodenum luminal flushing proteasesTCA precipitationRat Duodenum luminal flushingin vitro632300NoneStimulate gut growth and repair
2428
75616321995
GPETLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSA
Insulin-like growth factor-I (IGF-I)70FreeFreeLinearLI125 labelingHuman IGF-1Growth Hormone2-5, 5, 7-5, 10 or 20min8.6ng2Rat Duodenum luminal flushing proteasesAntibody assayRat Duodenum luminal flushingin vitro632300NoneStimulate gut growth and repair
2429
75616321995
GPETLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSA
Insulin-like growth factor-I (IGF-I)70FreeFreeLinearLI125 labelingHuman IGF-1Growth Hormone2-5, 5, 7-5, 10 or 20min8.6ng2Rat Duodenum luminal flushing proteasesReceptor-precipitable radioactivityRat Duodenum luminal flushingin vitro632300NoneStimulate gut growth and repair
2430
75616321995
GPETLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSA
Insulin-like growth factor-I (IGF-I)70FreeFreeLinearLI125 labelingHuman IGF-1Growth Hormone2-5, 5, 7-5, 10 or 20min8.6ng2Rat Ileum luminal flushing proteasesTCA precipitationRat Ileum luminal flushingin vitro632300NoneStimulate gut growth and repair
2431
75616321995
GPETLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSA
Insulin-like growth factor-I (IGF-I)70FreeFreeLinearLI125 labelingHuman IGF-1Growth Hormone2-5, 5, 7-5, 10 or 20min8.6ng2Rat Ileum luminal flushing proteasesAntibody assayRat Ileum luminal flushingin vitro632300NoneStimulate gut growth and repair
2432
75616321995
GPETLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSA
Insulin-like growth factor-I (IGF-I)70FreeFreeLinearLI125 labelingHuman IGF-1Growth Hormone2-5, 5, 7-5, 10 or 20min8.6ng2Rat Ileum luminal flushing proteasesReceptor-precipitable radioactivityRat Ileum luminal flushingin vitro632300NoneStimulate gut growth and repair
2433
75616321995
GPETLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSA
Insulin-like growth factor-I (IGF-I)70FreeFreeLinearLI125 labelingHuman IGF-1Growth Hormone5, 10, 20, 30 or 60 min8.6ng38Rat Colon luminal flushing proteasesTCA precipitationRat Colon luminal flushingin vitro632300NoneStimulate gut growth and repair
2434
75616321995
GPETLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSA
Insulin-like growth factor-I (IGF-I)70FreeFreeLinearLI125 labelingHuman IGF-1Growth Hormone5, 10, 20, 30 or 60 min8.6ng33Rat Colon luminal flushing proteasesAntibody assayRat Colon luminal flushingin vitro632300NoneStimulate gut growth and repair
2435
75616321995
GPETLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSA
Insulin-like growth factor-I (IGF-I)70FreeFreeLinearLI125 labelingHuman IGF-1Growth Hormone5, 10, 20, 30 or 60 min8.6ng16Rat Colon luminal flushing proteasesReceptor-precipitable radioactivityRat Colon luminal flushingin vitro632300NoneStimulate gut growth and repair
2436
75616321995
MFPAMPLSSLFVNGPRTLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSA
LR(3) insulin-like growth factor-I (IGF-I)8313 amino acid extension peptide at the N-terminus of IGF-IFreeLinearLI125 labelingAnalogue of IGF-IGrowth Hormone5, 10, 20, 30 or 60 min8.6ng50Rat Stomach luminal flushing proteasesTCA precipitationRat Stomach luminal flushingin vivohttp://www.cellsciences.com/content/p-detail.asp?rNoneProtect the growth factor by steric hindrance of cleavage sites.
2437
75616321995
MFPAMPLSSLFVNGPRTLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSA
LR(3) insulin-like growth factor-I (IGF-I)8313 amino acid extension peptide at the N-terminus of IGF-IFreeLinearLI125 labelingAnalogue of IGF-IGrowth Hormone2-5, 5, 7-5, 10 or 20min8.6ng2Rat Duodenum luminal flushing proteasesTCA precipitationRat Duodenum luminal flushingin vivohttp://www.cellsciences.com/content/p-detail.asp?rNoneProtect the growth factor by steric hindrance of cleavage sites.
2438
75616321995
MFPAMPLSSLFVNGPRTLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSA
LR(3) insulin-like growth factor-I (IGF-I)8313 amino acid extension peptide at the N-terminus of IGF-IFreeLinearLI125 labelingAnalogue of IGF-IGrowth Hormone2-5, 5, 7-5, 10 or 20min8.6ng2Rat Ileum luminal flushing proteasesTCA precipitationRat Ileum luminal flushingin vivohttp://www.cellsciences.com/content/p-detail.asp?rNoneProtect the growth factor by steric hindrance of cleavage sites.
2439
75616321995
MFPAMPLSSLFVNGPRTLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSA
LR(3) insulin-like growth factor-I (IGF-I)8313 amino acid extension peptide at the N-terminus of IGF-IFreeLinearLI125 labelingAnalogue of IGF-IGrowth Hormone5, 10, 20, 30 or 60 min8.6ng60Rat Colon luminal flushing proteasesTCA precipitationRat Colon luminal flushingin vivohttp://www.cellsciences.com/content/p-detail.asp?rNoneProtect the growth factor by steric hindrance of cleavage sites.
2474
81940821993
NSDSECPLSHDGYCLHDGVCMYIEALDKYACNCVVGYIGERCQYRDLKWWELR
Epidermal Growth Factor (EGF)53FreeFreeLinearLI125 labelingEpidermal Growth FactorGrowth factor135 minutes1420 Ci/mmol12.4 (dissociation t1/2)Proteases present in human meningiomaAutoradiographyFresh surgically excised human meningioma specimensin vitro4636327NoneHigh concentrations (10-4-10 -2 M) of suramin inhibited 125I-EGF binding to meningioma sections with ICs0's of 3.2 + 0.4 × 1 0 - 4 M
2477
85426721995
YRQSMNQGSRSTGCRFGTCTMQKLAHQIYQFTDKDKDGMAPRNKISPQGY
Adrenomedullin (AM)50FreeAmidationLinearLNoneHuman pheochromocytomaHypotensive peptide30 minutes1.0 nmol/kg, dissolved in saline1.05 ±0.04Rat blood proteasesRadioimmunoassaySpontaneously hypertensive rats (SHR)in vivoNoneNoneThe mean maximal changes in MBP at doses of 0.3, 1.0 and 3.0nmol/kg of AM were -24.0, -78.5, -92.3mmHg.
2478
85426721995
YRQSMNQGSRSTGCRFGTCTMQKLAHQIYQFTDKDKDGMAPRNKISPQGY
Adrenomedullin (AM)51FreeAmidationLinearLNoneHuman pheochromocytomaHypotensive peptide30 minutes1.0 nmol/kg, dissolved in saline1.19 ±0.09Rat blood proteasesRadioimmunoassayWistar-Kyoto ratsin vivoNoneNoneThe mean maximal changes in MBP at doses of 0.3, 1.0 and 3.0nmol/kg of AM were - 12.4, -46.6, -61.6 mmHg.
2479
85426721995
YRQSMNQGSRSTGCRFGTCTMQKLAHQIYQFTDKDKDGMAPRNKISPQGY
Adrenomedullin (AM)52FreeAmidationLinearLNoneHuman pheochromocytomaHypotensive peptide30 minutes1.0 nmol/kg, dissolved in saline18.1 ±1.4Rat blood proteasesRadioimmunoassaySpontaneously hypertensive rats (SHR)in vivoNoneNoneThe mean maximal changes in MBP at doses of 0.3, 1.0 and 3.0nmol/kg of AM were -24.0, -78.5, -92.3mmHg.
2480
85426721995
YRQSMNQGSRSTGCRFGTCTMQKLAHQIYQFTDKDKDGMAPRNKISPQGY
Adrenomedullin (AM)53FreeAmidationLinearLNoneHuman pheochromocytomaHypotensive peptide30 minutes1.0 nmol/kg, dissolved in saline16.3 ±1.2Rat blood proteasesRadioimmunoassayWistar-Kyoto ratsin vivoNoneNoneThe mean maximal changes in MBP at doses of 0.3, 1.0 and 3.0nmol/kg of AM were - 12.4, -46.6, -61.6 mmHg.
2496
191653532009
HPLGSPGSASDLETSGLQEQRNHLQGKLSELQVEQTSLEPLQESPRTPGVWKSREVATEGIRGHRKMVLYTLRAPR
NT pro-BNP (N-terminal Pro-Brain natriuretic Peptide)76FreeFreeLinearLNoneBrain Natriuretic PeptideDiuretic,natriuretic and vasodilatory peptideNot mentionedNot mentioned60-120Human plasma proteasesNot mentionedHuman plasmain vitrohttp://www.phoenixpeptide.com/catalog/product_infoNoneNT-pro-BNP is an independent predictor of postoperative myocardial injury in patients undergoing vascular surgery
2511
157404582005
YRQSMNQGSRSTGCRFGTCTMQKLAHQIYQFTDKDKDGMAPRNKISPQGY
Rat AM (Adrenomedullin)50FreeFreeLinearLNoneHuman pheochromocytomaHypotensive peptide30 minutes200 μl2 (distribution t1/2)Rat blood proteasesCompetitive RadioimmunoassayIntravenous administration in Ratin vivohttp://www.anaspec.com/products/product.asp?id=304NoneNot reported
2512
157404582005
YRQSMNQGSRSTGCRFGTCTMQKLAHQIYQFTDKDKDGMAPRNKISPQGY
Rat AM (Adrenomedullin)50FreeFreeLinearLNoneHuman pheochromocytomaHypotensive peptide30 minutes200 μl15.9 (elimination t1/2)Rat blood proteasesCompetitive RadioimmunoassayIntravenous administration in Ratin vivohttp://www.anaspec.com/products/product.asp?id=304NoneNot reported
2525
38716101985
PSSSLHLHRRITHHRRLGCFRSSGSLLNNAMKGGVDDEITLSAYITMALLESSLPDTDP
Rat α1- proteinase inhibitor60FreeFreeLinearLGlycosylationRat serumProtelytic activities regulating peptide5 minutes, 30 minutes, 1 hour, 4 hour and 7 hourNot mentioned170 (for glycosylated α1- proteinase inhibitor)Rat serum proteasesRadioimmunoassayWistar ratsin vivohttp://www.uniprot.org/uniprot/Q9JMK6NoneProtect tissue against proteolytic attack by leukocyte elastase
2526
38716101985
PSSSLHLHRRITHHRRLGCFRSSGSLLNNAMKGGVDDEITLSAYITMALLESSLPDTDP
Rat α1- proteinase inhibitor60FreeFreeLinearLNoneRat serumProtelytic activities regulating peptide5 minutes, 30 minutes, 1 hour, 4 hour and 7 hourNot mentioned30 (for unglycosylated α1- proteinase inhibitor)Rat serum proteasesRadioimmunoassayWistar ratsin vivohttp://www.uniprot.org/uniprot/Q9JMK6NoneProtect tissue against proteolytic attack by leukocyte elastase
2532
185864402008
HPLGSPGSASDLETSGLQEQRNHLQGKLSELQVEQTSLEPLQESPRTPGVWKSREVATEGIRGHRKMVLYTLRAPR
NT pro-BNP (N-terminal pro B-type natriuretic peptide)76FreeFreeLinearLNoneB-type Natriuretic peptideDiuretic, Natriuretic and vasodilatory peptideNot mentionedNot mentioned120Human serum proteasesNot mentionedHumansin vivohttp://www.phoenixpeptide.com/catalog/product_infoNoneNT-pro-BNP (using a cutoff value of >308 pg/mL) is an independent predictor of postoperative myocardial injury in patients undergoing vascular surgery
2533
106079402000
GPETLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSA
Insulin-like growth factor-I (IGF-I)70FreeFreeLinearLI125 labelingHuman IGF-1Promotes formation and repair of bone, stimulates body protein and glucose metabolism and increases glomerular filtration rate and renal plasma flow5, 30, 120 and 240 min100 μl3.2 ±0.1 (t1/2α)Rat blood proteasesRadioimmunoassay and bi-exponential equation that describes a two-compartment modelIntravenous bolus administration in Ratin vivo632300Noneinfusion of 125I-IGF-I into rats, 0 ·003 ±0 ·001% (mean ±S.E.M, n=6) of total infused, intact 125I-IGF-I had appeared per milliliter of wound fluid.
2534
106079402000
GPETLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSA
Insulin-like growth factor-I (IGF-I)70FreeFreeLinearLI125 labelingHuman IGF-1Promotes formation and repair of bone, stimulates body protein and glucose metabolism and increases glomerular filtration rate and renal plasma flow5, 30, 120 and 240 min100 μl4.9 ±0.02 (t1/2α)Rat blood proteasesRadioimmunoassay and bi-exponential equation that describes a two-compartment modelIntravenous bolus administration in Ratin vivo632300Noneinfusion of 125I-IGF-I into rats, 0 ·003 ±0 ·001% (mean ±S.E.M, n=6) of total infused, intact 125I-IGF-I had appeared per milliliter of wound fluid.
2535
106079402000
MFPAMPLSSLFVNGPRTLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSA
LR(3) insulin-like growth factor-I (IGF-I)83FreeFreeLinearLI125 labelingAnalogue of IGF-IPromotes formation and repair of bone, stimulates body protein and glucose metabolism and increases glomerular filtration rate and renal plasma flow5, 30, 120 and 240 min100 μl2.8 ±0.1 (t1/2α)Rat blood proteasesRadioimmunoassay and bi-exponential equation that describes a two-compartment modelIntravenous bolus administration in Ratin vivohttp://www.cellsciences.com/content/p-detail.asp?rNoneAt 5 min 0 ·01 ± 0 ·001% (mean ± S.E.M, n = 6, P < 0 ·001) of total infused intact 125I-LR3IGF-I had appeared per milliliter of wound fluid.
2536
106079402000
MFPAMPLSSLFVNGPRTLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSA
LR(3) insulin-like growth factor-I (IGF-I)83FreeFreeLinearLI125 labelingAnalogue of IGF-IPromotes formation and repair of bone, stimulates body protein and glucose metabolism and increases glomerular filtration rate and renal plasma flow5, 30, 120 and 240 min100 μl4.6 ±0.5 (t1/2α)Rat blood proteasesRadioimmunoassay and bi-exponential equation that describes a two-compartment modelIntravenous bolus administration in Ratin vivohttp://www.cellsciences.com/content/p-detail.asp?rNoneAt 5 min 0 ·01 ± 0 ·001% (mean ± S.E.M, n = 6, P < 0 ·001) of total infused intact 125I-LR3IGF-I had appeared per milliliter of wound fluid.
2537
106079402000
GPETLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSA
Insulin-like growth factor-I (IGF-I)70FreeFreeLinearLI125 labelingHuman IGF-1Promotes formation and repair of bone, stimulates body protein and glucose metabolism and increases glomerular filtration rate and renal plasma flow5, 30, 120 and 240 min100 μl203 ±10.2 (t1/2β)Rat blood proteasesRadioimmunoassay and bi-exponential equation that describes a two-compartment modelIntravenous bolus administration in Ratin vivo632300Noneinfusion of 125I-IGF-I into rats, 0 ·003 ±0 ·001% (mean ±S.E.M, n=6) of total infused, intact 125I-IGF-I had appeared per milliliter of wound fluid.
2538
106079402000
GPETLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSA
Insulin-like growth factor-I (IGF-I)70FreeFreeLinearLI125 labelingHuman IGF-1Promotes formation and repair of bone, stimulates body protein and glucose metabolism and increases glomerular filtration rate and renal plasma flow5, 30, 120 and 240 min100 μl185.4 ±4.7 (t1/2β)Rat blood proteasesRadioimmunoassay and bi-exponential equation that describes a two-compartment modelIntravenous bolus administration in Ratin vivo632300Noneinfusion of 125I-IGF-I into rats, 0 ·003 ±0 ·001% (mean ±S.E.M, n=6) of total infused, intact 125I-IGF-I had appeared per milliliter of wound fluid.
2539
106079402000
MFPAMPLSSLFVNGPRTLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSA
LR(3) insulin-like growth factor-I (IGF-I)83FreeFreeLinearLI125 labelingAnalogue of IGF-IPromotes formation and repair of bone, stimulates body protein and glucose metabolism and increases glomerular filtration rate and renal plasma flow5, 30, 120 and 240 min100 μl111.1 ±3.9 (t1/2β)Rat blood proteasesRadioimmunoassay and bi-exponential equation that describes a two-compartment modelIntravenous bolus administration in Ratin vivohttp://www.cellsciences.com/content/p-detail.asp?rNoneAt 5 min 0 ·01 ± 0 ·001% (mean ± S.E.M, n = 6, P < 0 ·001) of total infused intact 125I-LR3IGF-I had appeared per milliliter of wound fluid.
2540
106079402000
MFPAMPLSSLFVNGPRTLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSA
LR(3) insulin-like growth factor-I (IGF-I)83FreeFreeLinearLI125 labelingAnalogue of IGF-IPromotes formation and repair of bone, stimulates body protein and glucose metabolism and increases glomerular filtration rate and renal plasma flow5, 30, 120 and 240 min100 μl140.2 ±2.5 (t1/2β)Rat blood proteasesRadioimmunoassay and bi-exponential equation that describes a two-compartment modelIntravenous bolus administration in Ratin vivohttp://www.cellsciences.com/content/p-detail.asp?rNoneAt 5 min 0 ·01 ± 0 ·001% (mean ± S.E.M, n = 6, P < 0 ·001) of total infused intact 125I-LR3IGF-I had appeared per milliliter of wound fluid.
2596
169823232006
(GGLYACHMGPITX1AVCQPLRX2)2Beta-ala-PEG
Hematide42AcetylationBeta-alanine-PEGLinearLX1-Napthyl-alanine, X2-SarcosineSynthetic dimeric peptideErythropoiesis stimulating agentNot mentioned0.138 mg/kg23.1 ±4.3Rat plasma proteasesCompetitive ELISARat plasma (Dose i/v adminstered)in vivoNoneNoneIC50 = 37pM for HuEPOr/125I-EPO competition binding assay, EC50 =460 pM for cell proliferation stimulation
2597
169823232006
(GGLYACHMGPITX1AVCQPLRX2)2Beta-ala-PEG
Hematide42AcetylationBeta-alanine-PEGLinearLX1-Napthyl-alanine, X2-SarcosineSynthetic dimeric peptideErythropoiesis stimulating agentNot mentioned0.69mg/kg21.5 ±3.6Rat plasma proteasesCompetitive ELISARat plasma (Dose i/v adminstered)in vivoNoneNoneIC50 = 37pM for HuEPOr/125I-EPO competition binding assay, EC50 =460 pM for cell proliferation stimulation
2598
169823232006
(GGLYACHMGPITX1AVCQPLRX2)2Beta-ala-PEG
Hematide42AcetylationBeta-alanine-PEGLinearLX1-Napthyl-alanine, X2-SarcosineSynthetic dimeric peptideErythropoiesis stimulating agentNot mentioned1.38 mg/kg22.2 ±1.7Rat plasma proteasesCompetitive ELISARat plasma (Dose i/v adminstered)in vivoNoneNoneIC50 = 37pM for HuEPOr/125I-EPO competition binding assay, EC50 =460 pM for cell proliferation stimulation
2599
169823232006
(GGLYACHMGPITX1AVCQPLRX2)2Beta-ala-PEG
Hematide42AcetylationBeta-alanine-PEGLinearLX1-Napthyl-alanine, X2-SarcosineSynthetic dimeric peptideErythropoiesis stimulating agentNot mentioned6.9 mg/kg27.5 ±3.7Rat plasma proteasesCompetitive ELISARat plasma (Dose i/v adminstered)in vivoNoneNoneIC50 = 37pM for HuEPOr/125I-EPO competition binding assay, EC50 =460 pM for cell proliferation stimulation
2600
169823232006
(GGLYACHMGPITX1AVCQPLRX2)2Beta-ala-PEG
Hematide42AcetylationBeta-alanine-PEGLinearLX1-Napthyl-alanine, X2-SarcosineSynthetic dimeric peptideErythropoiesis stimulating agentNot mentioned13.8 mg/kg30.7 ±2.6Rat plasma proteasesCompetitive ELISARat plasma (Dose i/v adminstered)in vivoNoneNoneIC50 = 37pM for HuEPOr/125I-EPO competition binding assay, EC50 =460 pM for cell proliferation stimulation
2601
169823232006
(GGLYACHMGPITX1AVCQPLRX2)2Beta-ala-PEG
Hematide42AcetylationBeta-alanine-PEGLinearLX1-Napthyl-alanine, X2-SarcosineSynthetic dimeric peptideErythropoiesis stimulating agentNot mentioned9.87 mg/kg47.8Rat plasma proteases(rat chronic renal insufficiency (CRI) model)Competitive ELISARat(rat chronic renal insufficiency (CRI) model) plasma (Dose i/v adminstered)in vivoNoneNoneIC50 = 37pM for HuEPOr/125I-EPO competition binding assay, EC50 =460 pM for cell proliferation stimulation
2602
169823232006
(GGLYACHMGPITX1AVCQPLRX2)2Beta-ala-PEG
Hematide42AcetylationBeta-alanine-PEGLinearLX1-Napthyl-alanine, X2-SarcosineSynthetic dimeric peptideErythropoiesis stimulating agentNot mentioned0.02 mg/kg14.6 ±4.3Monkey plasma proteasesCompetitive ELISAMonkey plasma (Dose i/v adminstered)in vivoNoneNoneIC50 = 37pM for HuEPOr/125I-EPO competition binding assay, EC50 =460 pM for cell proliferation stimulation
2603
169823232006
(GGLYACHMGPITX1AVCQPLRX2)2Beta-ala-PEG
Hematide42AcetylationBeta-alanine-PEGLinearLX1-Napthyl-alanine, X2-SarcosineSynthetic dimeric peptideErythropoiesis stimulating agentNot mentioned0.1 mg/kg16.4 ±1.7Monkey plasma proteasesCompetitive ELISAMonkey plasma (Dose i/v adminstered)in vivoNoneNoneIC50 = 37pM for HuEPOr/125I-EPO competition binding assay, EC50 =460 pM for cell proliferation stimulation
2604
169823232006
(GGLYACHMGPITX1AVCQPLRX2)2Beta-ala-PEG
Hematide42AcetylationBeta-alanine-PEGLinearLX1-Napthyl-alanine, X2-SarcosineSynthetic dimeric peptideErythropoiesis stimulating agentNot mentioned0.475 mg/kg29.9 ±9.4Monkey plasma proteasesCompetitive ELISAMonkey plasma (Dose i/v adminstered)in vivoNoneNoneIC50 = 37pM for HuEPOr/125I-EPO competition binding assay, EC50 =460 pM for cell proliferation stimulation
2605
169823232006
(GGLYACHMGPITX1AVCQPLRX2)2Beta-ala-PEG
Hematide42AcetylationBeta-alanine-PEGLinearLX1-Napthyl-alanine, X2-SarcosineSynthetic dimeric peptideErythropoiesis stimulating agentNot mentioned1.35 mg/kg59.7 ±2.9Monkey plasma proteasesCompetitive ELISAMonkey plasma (Dose i/v adminstered)in vivoNoneNoneIC50 = 37pM for HuEPOr/125I-EPO competition binding assay, EC50 =460 pM for cell proliferation stimulation
2672
222639692012
SLRRSSCFGGRMDRIGAQSGLGCNSFRYGS(GGS)4GG-Fc region
3m (monomer Atrial natriuretic peptide- Fc )42FreeFc regionCyclic (C7-C23 & C-residues of Fc region)LNoneSynthetic ANP peptides linked to the N-terminus of recombinantly expressed Fc using native chemical ligation.Natriuretic and vasodilator4-72 hours0.5mg/kg of protein4.5Rat plasma proteasesELISAFemale Wistar rats Plasmain vivoNoneNoneNot reported
2673
222639692012
{[SLRRSSCFGGRMDRIGAQSGLGCNSFRY(GGS)3GG]2}-Fc region
2d (Atrial natriuretic peptide- Fc dimer)78FreeFc regionCyclic (C7-C23 & C-residues of Fc region)LNoneSynthetic ANP peptides linked to the N-terminus of recombinantly expressed Fc using native chemical ligation.Natriuretic and vasodilator4-72 hours0.5mg/kg of protein2.8Rat plasma proteasesELISAFemale Wistar rats Plasmain vivoNoneNoneNot reported
2674
222639692012
{[SLRRSSCFGGRMDRIGAQSGLGCNSFRYGS(GGS)4GG]2}-Fc region
3d (Atrial natriuretic peptide- Fc dimer)84FreeFc regionCyclic (C7-C23 & C-residues of Fc region)LNoneSynthetic ANP peptides linked to the N-terminus of recombinantly expressed Fc using native chemical ligation.Natriuretic and vasodilator4-72 hours0.5mg/kg of protein5.5Rat plasma proteasesELISAFemale Wistar rats Plasmain vivoNoneNoneNot reported
2686
250256262014
MKFTLFSVLVVLLIATFVAADDCPRICTADFRPVCGTPSGGRRSANRTFGNQCSLDSHNCLNKGDTYDKLHDGECK
Vasotab TY76FreeFreeLinearLNoneSalivary glands of the horsefly ofTabanus yaoVasodialator and anti-thrombic1-480 minutes5mg/kg>1Mouse plasma proteasesELISAKunming Mouse plasma (Dose i/v injected)in vivoNoneNoneAt the dosages of 5,10, and 20 nmol/kg, vasotab TY inhibited thrombus formation by47.2, 72.2, and 86.1%, respectively.
2687
250256262014
MKFTLFSVLVVLLIATFVAADDCPRICTADFRPVCGTPSGGRRSANRTFGNQCSLDSHNCLNKGDTYDKLHDGECK
Vasotab TY76FreeFreeLinearLNoneSalivary glands of the horsefly ofTabanus yaoVasodialator and anti-thrombic1-480 minutes5mg/kg50Mouse lungs proteasesELISAKunming Mouse lungs (Dose i/v injected)in vivoNoneNoneAt the dosages of 5,10, and 20 nmol/kg, vasotab TY inhibited thrombus formation by47.2, 72.2, and 86.1%, respectively.
2718
257710002015
MWQRPSSWIEGRFPHSDAVFTDQYTRLRKQLAAKKYLQSLKQKRY
MHDBAY (Recombinant PACAP-derived peptide)45FreeFreeLinearLNoneSynthetic (Pituitary adenylate cyclase-activating peptides (PACAPs) derived peptide)Insulin secretion stimulant37 C, 48 Hours10 µM9.71Fxa(Facor Xa)HPLC-ESI/MS/MSBuffer containing peptide samplein vitroNoneNoneAUC for glucose -stimulated 1st phase insulin secretion in MHDBAY-treated mice (20nmol/kg) is 2.26 fold higher than control
2719
257710002015
MWQRPSSWIEGRFPHSDAVFTDQYTRLRKQLAAKKYLQSLKQKRY
MHDBAY (Recombinant PACAP-derived peptide)45FreeFreeLinearLNoneSynthetic (Pituitary adenylate cyclase-activating peptides (PACAPs) derived peptide)Insulin secretion stimulant37 C, 48 Hours10 µM16.31Fxa(Facor Xa)HPLC-ESI/MS/MSPeptide sample + HASin vitroNoneNoneAUC for glucose -stimulated 1st phase insulin secretion in MHDBAY-treated mice (20nmol/kg) is 2.26 fold higher than control
2720
257710002015
MWQRPSSWIEGRFPHSDAVFTDQYTRLRKQLAAKKYLQSLKQKRY
MHDBAY (Recombinant PACAP-derived peptide)45FreeFreeLinearLNoneSynthetic (Pituitary adenylate cyclase-activating peptides (PACAPs) derived peptide)Insulin secretion stimulant0.5-24 hours0.5 mg/kg16.72Fxa(Facor Xa) and DPP-IVLC-MS/MSPeptide sample + HSA +Fxa + DPP IV(Dose i/v injected)in vitroNoneNoneAUC for glucose -stimulated 1st phase insulin secretion in MHDBAY-treated mice (20nmol/kg) is 2.26 fold higher than control
2721
257710002015
MWQRPSSWIEGRFPHSDAVFTDQYTRLRKQLAAKKYLQSLKQKRY
MHDBAY (Recombinant PACAP-derived peptide)45FreeFreeLinearLNoneSynthetic (Pituitary adenylate cyclase-activating peptides (PACAPs) derived peptide)Insulin secretion stimulant0.5-24 hours0.5 mg/kg12.19db/db mice plasma proteasesLC-MS/MS(Dose i/v injected)Mice plasmain vivoNoneNoneAUC for glucose -stimulated 1st phase insulin secretion in MHDBAY-treated mice (20nmol/kg) is 2.26 fold higher than control
2722
257710002015
MWQRPSSWIEGRFPHSDAVFTDQYTRLRKQLAAKKYLQSLKQKRY
MHDBAY (Recombinant PACAP-derived peptide)45FreeFreeLinearLNoneSynthetic (Pituitary adenylate cyclase-activating peptides (PACAPs) derived peptide)Insulin secretion stimulant0.5-24 hours0.5 mg/kg>12Rabbit plasma proteasesLC-MS/MSNew Zealand White Rabbit plasma (Dose i/v injected)in vivoNoneNoneAUC for glucose -stimulated 1st phase insulin secretion in MHDBAY-treated mice (20nmol/kg) is 2.26 fold higher than control
2755
262221802015
YA/EGTFISDYSIAMDKIHQQDFVNWLLAQKGKKNDWKHNITQ
GIP (1-42) (Glucosedependent insulinotropic polypeptide)42FreeFreeLinearLNoneProprotein of gastrointestinal tractAntihyperglycemic or incretin effect(Stimulate Insulin release in glucose dependent manner)Room Temp0.4 µMMay-20Human plasma proteases + DPP IVMSEDTA plasmain vitroNoneNoneNot reported
2756
262221802015
YA/EGTFISDYSIAMDKIHQQDFVNWLLAQKGKKNDWKHNITQ
GIP (1-42) (Glucosedependent insulinotropic polypeptide)42FreeFreeLinearLNoneProprotein of gastrointestinal tractAntihyperglycemic or incretin effect(Stimulate Insulin release in glucose dependent manner)Room Temp0.4 µMMay-20Human serum proteases + DPP IVMSSerumin vitroNoneNoneNot reported
2757
262221802015
YA/EGTFISDYSIAMDKIHQQDFVNWLLAQKGKKNDWKHNITQ
GIP (1-42) (Glucosedependent insulinotropic polypeptide)42FreeFreeLinearLNoneProprotein of gastrointestinal tractAntihyperglycemic or incretin effect(Stimulate Insulin release in glucose dependent manner)Room Temp0.4 µM>96Human plasma proteases + DPP IVMSP800 plasmain vitroNoneNoneNot reported
2798
248747042014
YRQSMNNFQGLRSFGCRFGTCTVQKLAHQIYQFTDKDKDNVAPRSKISPQGY
AM(adrenomedullin)52FreeAmidationCyclic (Ringed structure formed by C16-C21)LNoneIsolated from Human pheochromocytomaVasodilator and cardiovascular protectionNot mentioned3nmol/kg Dose0.62 ±0.02 (1st plasma half life)Rat plasma proteasesELISAMale Wistar rats plasmain vivohttp://www.genscript.com/peptide/RP11288-AdrenomedNoneNative human AM peptide elevated intracellular cAMP levels in a dose-dependent manner with pEC50 and Emax values of 8.59 ± 0.90 and9.30 ± 0.26 nmol/well
2799
248747042014
YRQSMNNFQGLRSFGCRFGTCTVQKLAHQIYQFTDKDKDNVAPRSKISPQGY
AM(adrenomedullin)52FreeAmidationCyclic (Ringed structure formed by C16-C21)LNoneIsolated from Human pheochromocytomaVasodilator and cardiovascular protectionNot mentioned3nmol/kg Dose15.2 ±1.9 min (2nd plasma half life)Rat plasma proteasesELISAMale Wistar rats plasmain vivohttp://www.genscript.com/peptide/RP11288-AdrenomedNoneNative human AM peptide elevated intracellular cAMP levels in a dose-dependent manner with pEC50 and Emax values of 8.59 ± 0.90 and9.30 ± 0.26 nmol/well
2800
248747042014
YRQSMNNFQGLRSFGCRFGTCTVQKLAHQIYQFTDKDKDNVAPRSKISPQGY
PEGylated AM52PegylationAmidationCyclic (Ringed structure formed by C16-C21)LNoneIsolated from Human pheochromocytomaVasodilator and cardiovascular protectionNot mentioned3nmol/kg Dose4.87 ±0.68(1st plasma half life)Rat plasma proteasesELISAMale Wistar rats plasmain vivohttp://www.genscript.com/peptide/RP11288-AdrenomedNonePEGylated AM peptide elevated intracellular cAMP levels in a dose-dependent manner with pEC50 and Emax values of 8.519 ± 0.10 and9.44 ± 0.30 nmol/well
2801
248747042014
YRQSMNNFQGLRSFGCRFGTCTVQKLAHQIYQFTDKDKDNVAPRSKISPQGY
PEGylated AM52PegylationAmidationCyclic (Ringed structure formed by C16-C21)LNoneIsolated from Human pheochromocytomaVasodilator and cardiovascular protectionNot mentioned3nmol/kg Dose108 ±12 min (2nd plasma half life)Rat plasma proteasesELISAMale Wistar rats plasmain vivohttp://www.genscript.com/peptide/RP11288-AdrenomedNonePEGylated AM peptide elevated intracellular cAMP levels in a dose-dependent manner with pEC50 and Emax values of 8.519 ± 0.10 and9.44 ± 0.30 nmol/well
2816
13194551992
SEEPPISLDLTFHLLREVLEMARAEQLAQQAHSNRKLMEII
hCRH(Human Corticotropin Releasing Hormone)41FreeFreeLinearLNoneDerived from Pre-hormoneHormone causes Adrenocorticotropin secrection and neurotransmitter2.5-180 minutes100μg30.5 ±3.3Human plasma proteasesIRM(Immunoradiometric assays)Human plasmain vivo12379493None22.4 ± 8.1 ng/hour (ACTH response)
2817
13194551992
SEEPPISLDLTFHLLREVLEMARAEQLAQQAHSNRKLMEII
hCRH(Human Corticotropin Releasing Hormone)41FreeFreeLinearLNoneDerived from Pre-hormoneHormone causes Adrenocorticotropin secrection and neurotransmitter2.5-180 minutes100μg46.5 ±7.2Sheep plasma proteasesIRM(Immunoradiometric assays)Human plasmain vivo12379493None46.5 ± 6.4 ng/hour (ACTH response)
2818
13194551992
SQEPPISLVLTFHLLREVLEMTKADQLAQQAHSNRKLLDIA
oCRH(Ovine Corticotropin Releasing Hormone)41FreeFreeLinearLNoneDerived from Pre-hormoneHormone causes Adrenocorticotropin secrection and neurotransmitter2.5-180 minutes100μg42.8 ±6.4Human plasma proteasesIRM(Immunoradiometric assays)Sheep plasmain vivo6603620None39.9 ± 11.7 ng/hour (ACTH response)
2819
13194551992
SQEPPISLVLTFHLLREVLEMTKADQLAQQAHSNRKLLDIA
oCRH(Ovine Corticotropin Releasing Hormone)41FreeFreeLinearLNoneDerived from Pre-hormoneHormone causes Adrenocorticotropin secrection and neurotransmitter2.5-180 minutes100μg39.8 ±10.1Sheep plasma proteasesIRM(Immunoradiometric assays)Sheep plasmain vivo6603620None40.2 ± 8.4 ng/hour (ACTH response)
2836
16464651991
SQDSAERIQERLRNSKMAHSSSCFGQKIDRIGAVSRLGCDGLRQF
iso-rANP(1-45) (Recombinant atrial natriuretic peptide)45FreeFreeCyclic (C23-C39)LNoneDerived from ANP (Atrial natriuretic peptide)Natriuretic and vasodilatorBlood samples collected at 5-1800 seconds after peptide injecteion1 x 106 cpm130 ±13Rat plasma proteasesRadioimmunoassayMale Wistar rats plasma (Dose i/p injected)in vivoNoneNoneNot reported
2837
16464651991
SQDSAERIQERLRNSKMAHSSSCFGQKIDRIGAVSRLGCDGLRQF
iso-rANP(1-45) (Recombinant atrial natriuretic peptide)45FreeFreeCyclic (C23-C39)LNoneDerived from ANP (Atrial natriuretic peptide)Natriuretic and vasodilatorBlood samples collected at 5-1800 seconds after peptide injecteion1 x 106 cpm23.7 + 1.7 (α- t1/2)Rat plasma proteasesRadioimmunoassayMale Wistar rats plasma (Dose i/p injected)in vivoNoneNoneNot reported
2838
16464651991
SQDSAERIQERLRNSKMAHSSSCFGQKIDRIGAVSRLGCDGLRQF
iso-rANP(1-45) (Recombinant atrial natriuretic peptide)45FreeFreeCyclic (C23-C39)LNoneDerived from ANP (Atrial natriuretic peptide)Natriuretic and vasodilatorBlood samples collected at 5-1800 seconds after peptide injecteion1x 106 cpm164.3 ±9.0(β- t1/2)Rat plasma proteasesRadioimmunoassayMale Wistar rats plasma (Dose i/p injected)in vivoNoneNoneNot reported
2855
18891241991
AQKVNSGEPRAHLGALLARYIQQARKAPSGRMSVIKNLQNLDPSHRISDRDYMGWMDF
CCK58 (Cholecystokinin 58)58FreeAmidationLinearLNone Peptide hormone of the gastrointestinal systemStimulates digestion of fat & protein37 °C for 30-180 minutes1.6pmol45 ±5Normal Human plasma proteasesRadioimmunoassay and HPLCNormal Human plasmain vitroNoneNoneNot reported
2856
18891241991
AQKVNSGEPRAHLGALLARYIQQARKAPSGRMSVIKNLQNLDPSHRISDRDYMGWMDF
CCK58 (Cholecystokinin 58)58FreeAmidationLinearLNone Peptide hormone of the gastrointestinal systemStimulates digestion of fat & protein37 °C for 30-180 minutes1.6pmol69 ±8Normal Human blood proteasesRadioimmunoassay and HPLCNormal Human bloodin vitroNoneNoneNot reported
2857
18891241991
AQKVNSGEPRAHLGALLARYIQQARKAPSGRMSVIKNLQNLDPSHRISDRDYMGWMDF
CCK58 (Cholecystokinin 58)58FreeAmidationLinearLNone Peptide hormone of the gastrointestinal systemStimulates digestion of fat & protein37 °C for 30-180 minutes1.6pmol10.4 ±1.1Pancreatitis patients blood proteasesRadioimmunoassay and HPLCPancreatitis patient plasmain vitroNoneNoneNot reported
2858
18891241991
AQKVNSGEPRAHLGALLARYIQQARKAPSGRMSVIKNLQNLDPSHRISDRDYMGWMDF
CCK58 (Cholecystokinin 58)58FreeAmidationLinearLNone Peptide hormone of the gastrointestinal systemStimulates digestion of fat & protein37 °C for 30-180 minutes1.6pmol11.1 ±1Pancreatitis patients plasma proteasesRadioimmunoassay and HPLCPancreatitis patient bloodin vitroNoneNoneNot reported
2865
21622751990
HADGVFTSDFSKLLGQLSAKKYLESLMGKRVSSNISEDPVPV
PHV (Peptide histidine valine)42FreeFreeLinearLNonePeptide derived from Prepro-VIPVasodilatorNot mentioned5 pmol min-1 kg-137.5Human plasma proteasesRadioimmunoassayHuman plasmain vivoNoneNoneIt increases heart rate but not significantly
2881
29663451988
NPVYSAVSNTDLMDFKNLLDHLEEKMPVEDEVMPPQALSEQTDEAGAALSSLSEVPPWTGEVNPSQRDGGALGRGPWDPSDRSALLKSKLRALLAGPR
rANF(Asn1-Arg98) [Rat atrial natriuretic factor]98FreeFreeLinearLRadioiodinated peptide at Tyr-4Rat ANF derivative [Rat atrial natriuretic factor]Natriuretic, diuretic and vasorelaxant peptideNot mentioned10 X106 CPM54.8 ±3.9(2nd component)Rat plasma proteasesRadioimmunoassayMale Sprague-Dawley rats plasmain vivohttp://www.uniprot.org/uniprot/P01161NoneNot reported
2882
29663451988
NPVYSAVSNTDLMDFKNLLDHLEEKMPVEDEVMPPQALSEQTDEAGAALSSLSEVPPWTGEVNPSQRDGGALGRGPWDPSDRSALLKSKLRALLAGPR
rANF(Asn1-Arg98) [Rat atrial natriuretic factor]98FreeFreeLinearLRadioiodinated peptide at Tyr-4Rat ANF derivative [Rat atrial natriuretic factor]Natriuretic, diuretic and vasorelaxant peptideNot mentioned10 X106 CPM2.5 ±0.3(1st compent)Rat plasma proteasesRadioimmunoassayMale Sprague-Dawley rats plasmain vivohttp://www.uniprot.org/uniprot/P01162NoneNot reported
2883
29889191985
SQEPPISLVLTFHLLREVLEMTKADQLAQQAHSNRKLLDIA
r/hCRF(Human/rat corticotropin-releasing factor)41FreeFreeLinearLNonePeptide hormone secreted by hypothalamus Stimulates corticotropes to secrete adrenocorticotropic hormone (ACTH) Blood samples collected at 1-180 minutes after peptide injection10 µg/kg peptide injected to rhesus monkey4.0 ±1.2 (t1/2fast)Rhesus monkey proteasesRadioimmunoassayRhesus monkey plasmain vivoNoneNoneACTH increased by 1035 ± 226 %, cortisol increased by 123 ± 34% on 10 µg/kg dose
2884
29889191985
SQEPPISLVLTFHLLREVLEMTKADQLAQQAHSNRKLLDIA
r/hCRF(Human/rat corticotropin-releasing factor)41FreeFreeLinearLNonePeptide hormone secreted by hypothalamus Stimulates corticotropes to secrete adrenocorticotropic hormone (ACTH) Blood samples collected at 1-180 minutes after peptide injection100 µg/kg peptide injected to rhesus monkey1.5 ±0.5 (t1/2fast)Rhesus monkey proteasesRadioimmunoassayRhesus monkey plasmain vivoNoneNoneACTH increased by 1858 ± 452 %, cortisol increased by 231 ± 28% on 10 µg/kg dose
2885
29889191985
SEEPPISLDLTFHLLREVLEMARAEQLAQQAHSNRKLMEII
oCRF(Ovine corticotropin-releasing factor)41FreeFreeLinearLNonePeptide hormone secreted by hypothalamus Stimulates corticotropes to secrete adrenocorticotropic hormone (ACTH) Blood samples collected at 1-180 minutes after peptide injection1 µg/kg peptide injected to rhesus monkey3.6 ±1.1 (t1/2 fast)Rhesus monkey proteasesRadioimmunoassayRhesus monkey plasmain vivoNoneNoneACTH increased by 161 ± 40 %, cortisol increased by 78 ± 22 % on 10 µg/kg dose
2886
29889191985
SQEPPISLDLTFHLLREVLEMTKADQLAQQAHSNRKLLDIA
r/hCRF(Human/rat corticotropin-releasing factor)41FreeFreeLinearLNonePeptide hormone secreted by hypothalamus Stimulates corticotropes to secrete adrenocorticotropic hormone (ACTH) Blood samples collected at 1-180 minutes after peptide injection10 µg/kg peptide injected to rhesus monkey29.0 ±2.0(t1/2 slow)Rhesus monkey proteasesRadioimmunoassayRhesus monkey plasmain vivoNoneNoneACTH increased by 1858 ± 452 %, cortisol increased by 123 ± 28% on 10 µg/kg dose
2887
29889191985
SQEPPISLDLTFHLLREVLEMTKADQLAQQAHSNRKLLDIA
r/hCRF(Human/rat corticotropin-releasing factor)41FreeFreeLinearLNonePeptide hormone secreted by hypothalamus Stimulates corticotropes to secrete adrenocorticotropic hormone (ACTH) Blood samples collected at 1-180 minutes after peptide injection100 µg/kg peptide injected to rhesus monkey32.7 ±10.1 (t1/2 slow)Rhesus monkey proteasesRadioimmunoassayRhesus monkey plasmain vivoNoneNoneACTH increased by 1858 ± 452 %, cortisol increased by 231 ± 28% on 10 µg/kg dose
2888
29889191985
SEEPPISLDLTFHLLREVLEMARAEQLAQQAHSNRKLMEII
oCRF(Ovine corticotropin-releasing factor)41FreeFreeLinearLNonePeptide hormone secreted by hypothalamus Stimulates corticotropes to secrete adrenocorticotropic hormone (ACTH) Blood samples collected at 1-180 minutes after peptide injection1 µg/kg peptide injected to rhesus monkey44.3 +/= 6.7 (t1/2 slow)Rhesus monkey proteasesRadioimmunoassayRhesus monkey plasmain vivoNoneNoneACTH increased by 161 ± 40 %, cortisol increased by 78 ± 22 % on 10 µg/kg dose
2897
33793521988
GPETLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSA
IGF-1 (Insulin-like growth factor-I)70FreeFreeLinearLLabelled with 125IPurified from bovine colostrumMediates growth and developmentBlood collected 10 minutes to 30 hours after peptide infusion10mM/L6.0-7.0Lamb plasma proteasesRadioimmunoassay, Binding protein radioactivity assay and IGF-region radioactivityEight merino lambs plasmain vivoNoneNoneNot reported
2898
33793521988
GPETLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSA
Reduced IGF-1(Free form) (Insulin-like growth factor-I)70FreeFreeLinearLLabelled with 125I, Disulphide bond is reducedBovine IGF-1Mediates growth and developmentBlood collected 10 minutes to 30 hours after peptide infusion10mM/L0.8Lamb plasma proteasesRadioimmunoassay, Binding protein radioactivity assay and IGF-region radioactivityEight merino lambs plasmain vivoNoneNoneNot reported
2899
33793521988
GPETLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSA
Reduced IGF-1(bound form) (Insulin-like growth factor-I)70FreeFreeLinearLLabelled with 125I, Disulphide bond is reducedBovine IGF-1Mediates growth and developmentBlood collected 10 minutes to 30 hours after peptide infusion10mM/L6Lamb plasma proteasesRadioimmunoassay, Binding protein radioactivity assay and IGF-region radioactivityEight merino lambs plasmain vivoNoneNoneNot reported
2900
33793521988
GPETLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSA
S-CM IGF-1 (Insulin-like growth factor-I)70FreeFreeLinearLS-CM=S-carboxymethylatedBovine IGF-1Mediates growth and developmentBlood collected 10 minutes to 30 hours after peptide infusion10mM/L0.8-0.9Lamb plasma proteasesRadioimmunoassay, Binding protein radioactivity assay and IGF-region radioactivityEight merino lambs plasmain vivoNoneNoneNot reported
2938
24548051988
GPETLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSA
[125I]IGF-I70FreeFreeLinearLNoneHuman Recombinant peptideStmulates glycogen synthesisBlood collected 10 minutes to 6 hours after peptide injection1 µCi peptide injected to rhesus monkey100Proteases from Rat serumRadioimmunoassayRat Serumin vivoNoneNoneStimulates glycogen synthesis by the incorporation of [14C]glucose into glycogen in rat diaphragm
2939
24548051988
FVNQHLCGSHVDELQYLCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSA
[125I]B-chain mutant IGF-171FreeFreeLinearLNoneHuman Recombinant peptideStmulates glycogen synthesisBlood collected 10 minutes to 6 hours after peptide injection2 µCi peptide injected to rhesus monkey27.5Proteases from Rat serumRadioimmunoassayRat Serumin vivoNoneNoneStimulates glycogen synthesis by the incorporation of [14C]glucose into glycogen in rat diaphragm
2940
24548051988
GPQALCGAELVDALYLVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSA
[125I] [Gln3,Ala4,Tyr15,Leu16]IGF-170FreeFreeLinearLNoneHuman Recombinant peptideStmulates glycogen synthesisBlood collected 10 minutes to 6 hours after peptide injection3 µCi peptide injected to rhesus monkey26.9Proteases from Rat serumRadioimmunoassayRat Serumin vivoNoneNoneStimulates glycogen synthesis by the incorporation of [14C]glucose into glycogen in rat diaphragm
2955
31080681987
GPETLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSA
IGF-1 (Insulin-like growth factor-I)70FreeFreeLinearLNonePurified from bovine colostrumMediates growth and developmentBlood collected 12hours after peptide injection6 - 10 µg/Kg<15Proteases from chicken plasmaRadioimmunoassay(Dose i/v injected)Chicken plasmain vivoNoneNoneGH concentrations subsequent to TRH injection were significantly depressed45.1 and 48.2% in IGF-l-treated as compared with control chicks; and GRF-stimulated GH secretion was significantly decreased by IGF-I administration in (41.3%)
2956
16648041991
SQDSAFRIQERLRNSKMAHSSSCFGQKIDRIGAVSRLGCDGLRLF
Rat BNP-45 ( Brain natriuretic peptide-45)45FreeFreeCyclic (C23-C39)LNoneIsolated from rat heart and shown to be a circulating form of rat BNPCardiac Natriuretic PeptideBlood samples collected at 0.5-10 minutes post peptide injection2 µg/150ul saline45 (t1/2 alpha or initial phase t1/2)Proteases from Mice (WKY)plasmaRadioimmunoassay(Dose i/v injected)Mice (WKY) plasmain vivoNoneNoneUrinary sodi µM excretion (uEq/min per kg)= 0.43 ± 0.13, mean arterial pressure (mmHg) = 129 ± 1, Urinary cGMP excretion (pmol/min) = 27.0 ± 3.1
2957
16648041991
SQDSAFRIQERLRNSKMAHSSSCFGQKIDRIGAVSRLGCDGLRLF
Rat BNP-45 ( Brain natriuretic peptide-45)45FreeFreeCyclic (C23-C39)LNoneIsolated from rat heart and shown to be a circulating form of rat BNPCardiac Natriuretic PeptideBlood samples collected at 0.5-10 minutes post peptide injection2 µg/150ul saline6.95 (t 1/2 beta or 2nd phase t1/2)Proteases from Mice (WKY)plasmaRadioimmunoassay(Dose i/v injected)Mice (WKY) plasmain vivoNoneNoneUrinary sodi µM excretion (uEq/min per kg)= 0.43 ± 0.13, mean arterial pressure (mmHg) = 129 ± 1, Urinary cGMP excretion (pmol/min) = 27.0 ± 3.2
3012
85426721995
YRQSMNQGSRSTGCRFGTCTMQKLAHQIYQFTDKDKDGMAPRNKISPQGY
Rat adrenomedullin (AM)50FreeAmidationCyclic (C14-C19)LNoneMember of the calcitonin family of peptidesHypotensive effectBlood sample collected after 0.5-20 minutes after drug administration1.0nmol/Kg1.05 ±0.04 (1st phase elimination life)Proteases from SHR rat plasmaRadioimmunoassayRat(SHR) plasmain vivoNoneNoneMean maximal changes in MBP at doses of 0.3, 1.0 and 3.0nmol/kg of AM were -24.0, -78.5, -92.3mmHg for SHR, and - 12.4, -46.6, -61.6 mmHgfor WKY, respectively
3013
85426721995
YRQSMNQGSRSTGCRFGTCTMQKLAHQIYQFTDKDKDGMAPRNKISPQGY
Rat adrenomedullin (AM)50FreeAmidationCyclic (C14-C19)LNoneMember of the calcitonin family of peptidesHypotensive effectBlood sample collected after 0.5-20 minutes after drug administration1.0nmol/Kg1.19 ±0.09 (1st phase elimination life)Proteases from WKY rat plasmaRadioimmunoassayRat(WKY) plasmain vivoNoneNoneMean maximal changes in MBP at doses of 0.3, 1.0 and 3.0nmol/kg of AM were -24.0, -78.5, -92.3mmHg for SHR, and - 12.4, -46.6, -61.6 mmHgfor WKY, respectively
3014
85426721995
YRQSMNQGSRSTGCRFGTCTMQKLAHQIYQFTDKDKDGMAPRNKISPQGY
Rat adrenomedullin (AM)50FreeAmidationCyclic (C14-C19)LNoneMember of the calcitonin family of peptidesHypotensive effectBlood sample collected after 0.5-20 minutes after drug administration1.0nmol/Kg18.1 ±1.4 (2nd phase elimination life)Proteases from SHR rat plasmaRadioimmunoassayRat(SHR) plasmain vivoNoneNoneMean maximal changes in MBP at doses of 0.3, 1.0 and 3.0nmol/kg of AM were -24.0, -78.5, -92.3mmHg for SHR, and - 12.4, -46.6, -61.6 mmHgfor WKY, respectively
3015
85426721995
YRQSMNQGSRSTGCRFGTCTMQKLAHQIYQFTDKDKDGMAPRNKISPQGY
Rat adrenomedullin (AM)50FreeAmidationCyclic (C14-C19)LNoneMember of the calcitonin family of peptidesHypotensive effectBlood sample collected after 0.5-20 minutes after drug administration1.0nmol/Kg16.3 ±1.2 (2nd phase elimination life)Proteases from WKY rat plasmaRadioimmunoassayRat(WKY) plasmain vivoNoneNoneMean maximal changes in MBP at doses of 0.3, 1.0 and 3.0nmol/kg of AM were -24.0, -78.5, -92.3mmHg for SHR, and - 12.4, -46.6, -61.6 mmHgfor WKY, respectively
3122
212107102011
MCMPCFTTDHQMARKCDDCCGGKGRGKCYGPQCLCRGAGAAGG
Cyclic chlorotoxin(CTX)43FreeFreeCyclic (C2-C19, C5-C28, C16-C33, C20-C35)LN-hydroxysuccinimide ester(NHS-ester)modified Cy5.5 at Lysine 15,23 and 28Analog of CTXIdentify tumor foci with high sensitivity24 hours50μl of 40μM11Mice serum proteasesImaging system to measure fluorescent intensityIntravenous injection in two month old wild-type C57BL/6 micein vivohttp://www.drugbank.ca/drugs/DB00141NoneFluorescent efficiency (cm2) in the tumor compared with control mice=3.3 ±1.81
3126
227705642012
EWDREINNYTSLIHSLIEESQNQQEKNECELLELDKWASLW
HR2 (wild type) [HR2 regions of the HIV-1 envelope glycoprotein gp41]41FreeFreeLinearLNoneHR2 regions of the HIV-1 envelope glycoprotein gp41Inhibitor to prevent virus ˆ’host cell membrane fusionNot mentioned20μM37.2Bovine TrypsinTrypsin degradation assay, Analytical reverse phase HPLCSolutions of bovine trypsin and the peptide or PEG ˆ’peptide conjugate in 10 mM PBS (pH 7.4)in vitrohttp://www.drugbank.ca/drugs/DB00145NoneCell ˆ’Cell Fusion Inhibition Efficacy (IC50)=1.5 ± 0.1nM
3127
227705642012
CEWDREINNYTSLIHSLIEESQNQQEKNEQELLELDKWASLW
N-terminus of HR242FreeFreeLinearLNoneModified HR2 wild type peptideInhibitor to prevent virus ˆ’host cell membrane fusionNot mentioned20μM38.6Bovine TrypsinTrypsin degradation assay, Analytical reverse phase HPLCSolutions of bovine trypsin and the peptide or PEG ˆ’peptide conjugate in 10 mM PBS (pH 7.4)in vitrohttp://www.drugbank.ca/drugs/DB00146NoneNot mentioned
3128
227705642012
CEWDREINNYTSLIHSLIEESQNQQEKNEQELLELDKWASLW
N-terminus-PEG750 of HR242Pegylation-PEG750FreeLinearLNoneModified HR2 wild type peptideInhibitor to prevent virus ˆ’host cell membrane fusionNot mentioned20μM40Bovine TrypsinTrypsin degradation assay, Analytical reverse phase HPLCSolutions of bovine trypsin and the peptide or PEG ˆ’peptide conjugate in 10 mM PBS (pH 7.4)in vitrohttp://www.drugbank.ca/drugs/DB00147NoneCell ˆ’Cell Fusion Inhibition Efficacy (IC50)=7.2 ± 0.7nM
3129
227705642012
CEWDREINNYTSLIHSLIEESQNQQEKNEQELLELDKWASLW
N-terminus-PEG2000 of HR242Pegylation-PEG2000FreeLinearLNoneModified HR2 wild type peptideInhibitor to prevent virus ˆ’host cell membrane fusionNot mentioned20μM79.3Bovine TrypsinTrypsin degradation assay, Analytical reverse phase HPLCSolutions of bovine trypsin and the peptide or PEG ˆ’peptide conjugate in 10 mM PBS (pH 7.4)in vitrohttp://www.drugbank.ca/drugs/DB00148NoneCell ˆ’Cell Fusion Inhibition Efficacy (IC50)=11.2 ± 1.9nM
3130
227705642012
EWDREINNYTSLIHSLIEESQNQQEKNECELLELDKWASLW
R4C derivative of HR241FreeFreeLinearLNoneModified HR2 wild type peptideInhibitor to prevent virus ˆ’host cell membrane fusionNot mentioned20μM37.4Bovine TrypsinTrypsin degradation assay, Analytical reverse phase HPLCSolutions of bovine trypsin and the peptide or PEG ˆ’peptide conjugate in 10 mM PBS (pH 7.4)in vitrohttp://www.drugbank.ca/drugs/DB00149NoneNot mentioned
3131
227705642012
EWDREINNYTSLIHSLIEESQNQQEKNECELLELDKWASLW
R4C-PEG750 derivative of HR241FreeFreeLinearLPegylation-PEG750 of cysteine at 4th positionModified HR2 wild type peptideInhibitor to prevent virus ˆ’host cell membrane fusionNot mentioned20μM44.1Bovine TrypsinTrypsin degradation assay, Analytical reverse phase HPLCSolutions of bovine trypsin and the peptide or PEG ˆ’peptide conjugate in 10 mM PBS (pH 7.4)in vitrohttp://www.drugbank.ca/drugs/DB00150NoneCell ˆ’Cell Fusion Inhibition Efficacy (IC50)=5.1 ± 1.1nM
3132
227705642012
EWDREINNYTSLIHSLIEESQNQQEKNECELLELDKWASLW
R4C-PEG2000 derivative of HR241FreeFreeLinearLPegylation-PEG2000 of cysteine at 4th positionModified HR2 wild type peptideInhibitor to prevent virus ˆ’host cell membrane fusionNot mentioned20μM67.4Bovine TrypsinTrypsin degradation assay, Analytical reverse phase HPLCSolutions of bovine trypsin and the peptide or PEG ˆ’peptide conjugate in 10 mM PBS (pH 7.4)in vitrohttp://www.drugbank.ca/drugs/DB00151NoneCell ˆ’Cell Fusion Inhibition Efficacy (IC50)=8.7 ± 1.3nM
3133
227705642012
EWDREINNYTSLIHSLIEESQNQQEKNECELLELDKWASLW
S11C derivative of HR241FreeFreeLinearLNoneModified HR2 wild type peptideInhibitor to prevent virus ˆ’host cell membrane fusionNot mentioned20μM38.9Bovine TrypsinTrypsin degradation assay, Analytical reverse phase HPLCSolutions of bovine trypsin and the peptide or PEG ˆ’peptide conjugate in 10 mM PBS (pH 7.4)in vitrohttp://www.drugbank.ca/drugs/DB00152NoneNot mentioned
3134
227705642012
EWDREINNYTSLIHSLIEESQNQQEKNECELLELDKWASLW
S11C-PEG750 derivative of HR241FreeFreeLinearLPegylation-PEG750 of cysteine at 11th positionModified HR2 wild type peptideInhibitor to prevent virus ˆ’host cell membrane fusionNot mentioned20μM50.2Bovine TrypsinTrypsin degradation assay, Analytical reverse phase HPLCSolutions of bovine trypsin and the peptide or PEG ˆ’peptide conjugate in 10 mM PBS (pH 7.4)in vitrohttp://www.drugbank.ca/drugs/DB00153NoneCell ˆ’Cell Fusion Inhibition Efficacy (IC50)=4.4 ± 0.8nM
3135
227705642012
EWDREINNYTSLIHSLIEESQNQQEKNECELLELDKWASLW
S11C-PEG2000 derivative of HR241FreeFreeLinearLPegylation-PEG2000 of cysteine at 11th positionModified HR2 wild type peptideInhibitor to prevent virus ˆ’host cell membrane fusionNot mentioned20μM91Bovine TrypsinTrypsin degradation assay, Analytical reverse phase HPLCSolutions of bovine trypsin and the peptide or PEG ˆ’peptide conjugate in 10 mM PBS (pH 7.4)in vitrohttp://www.drugbank.ca/drugs/DB00154NoneCell ˆ’Cell Fusion Inhibition Efficacy (IC50)=4.9 ± 0.5nM
3136
227705642012
EWDREINNYTSLIHSLIEESQNQQEKNECELLELDKWASLW
S15C derivative of HR241FreeFreeLinearLNoneModified HR2 wild type peptideInhibitor to prevent virus ˆ’host cell membrane fusionNot mentioned20μM39.9Bovine TrypsinTrypsin degradation assay, Analytical reverse phase HPLCSolutions of bovine trypsin and the peptide or PEG ˆ’peptide conjugate in 10 mM PBS (pH 7.4)in vitrohttp://www.drugbank.ca/drugs/DB00155NoneNot mentioned
3137
227705642012
EWDREINNYTSLIHSLIEESQNQQEKNECELLELDKWASLW
S15C-PEG750 derivative of HR241FreeFreeLinearLPegylation-PEG750 of cysteine at 15th positionModified HR2 wild type peptideInhibitor to prevent virus ˆ’host cell membrane fusionNot mentioned20μM53.7Bovine TrypsinTrypsin degradation assay, Analytical reverse phase HPLCSolutions of bovine trypsin and the peptide or PEG ˆ’peptide conjugate in 10 mM PBS (pH 7.4)in vitrohttp://www.drugbank.ca/drugs/DB00156NoneCell ˆ’Cell Fusion Inhibition Efficacy (IC50)=4.1 ± 1.0nM
3138
227705642012
EWDREINNYTSLIHSLIEESQNQQEKNECELLELDKWASLW
S15C-PEG2000 derivative of HR241FreeFreeLinearLPegylation-PEG2000 of cysteine at 15th positionModified HR2 wild type peptideInhibitor to prevent virus ˆ’host cell membrane fusionNot mentioned20μM82.4Bovine TrypsinTrypsin degradation assay, Analytical reverse phase HPLCSolutions of bovine trypsin and the peptide or PEG ˆ’peptide conjugate in 10 mM PBS (pH 7.4)in vitrohttp://www.drugbank.ca/drugs/DB00157NoneCell ˆ’Cell Fusion Inhibition Efficacy (IC50)=5.0 ± 0.5nM
3139
227705642012
EWDREINNYTSLIHSLIEESQNQQEKNECELLELDKWASLW
E18C derivative of HR241FreeFreeLinearLNoneModified HR2 wild type peptideInhibitor to prevent virus ˆ’host cell membrane fusionNot mentioned20μM38.4Bovine TrypsinTrypsin degradation assay, Analytical reverse phase HPLCSolutions of bovine trypsin and the peptide or PEG ˆ’peptide conjugate in 10 mM PBS (pH 7.4)in vitrohttp://www.drugbank.ca/drugs/DB00158NoneNot mentioned
3140
227705642012
EWDREINNYTSLIHSLIEESQNQQEKNECELLELDKWASLW
E18C-PEG750 derivative of HR241FreeFreeLinearLPegylation-PEG750 of cysteine at 18th positionModified HR2 wild type peptideInhibitor to prevent virus ˆ’host cell membrane fusionNot mentioned20μM50.3Bovine TrypsinTrypsin degradation assay, Analytical reverse phase HPLCSolutions of bovine trypsin and the peptide or PEG ˆ’peptide conjugate in 10 mM PBS (pH 7.4)in vitrohttp://www.drugbank.ca/drugs/DB00159NoneCell ˆ’Cell Fusion Inhibition Efficacy (IC50)=4.5 ± 1.0nM
3141
227705642012
EWDREINNYTSLIHSLIEESQNQQEKNECELLELDKWASLW
E18C-PEG2000 derivative of HR241FreeFreeLinearLPegylation-PEG2000 of cysteine at 18th positionModified HR2 wild type peptideInhibitor to prevent virus ˆ’host cell membrane fusionNot mentioned20μM81.3Bovine TrypsinTrypsin degradation assay, Analytical reverse phase HPLCSolutions of bovine trypsin and the peptide or PEG ˆ’peptide conjugate in 10 mM PBS (pH 7.4)in vitrohttp://www.drugbank.ca/drugs/DB00160NoneCell ˆ’Cell Fusion Inhibition Efficacy (IC50)=4.9 ± 0.6nM
3142
227705642012
EWDREINNYTSLIHSLIEESQNQQEKNECELLELDKWASLW
N22C derivative of HR241FreeFreeLinearLNoneModified HR2 wild type peptideInhibitor to prevent virus ˆ’host cell membrane fusionNot mentioned20μM38.9Bovine TrypsinTrypsin degradation assay, Analytical reverse phase HPLCSolutions of bovine trypsin and the peptide or PEG ˆ’peptide conjugate in 10 mM PBS (pH 7.4)in vitrohttp://www.drugbank.ca/drugs/DB00161NoneNot mentioned
3143
227705642012
EWDREINNYTSLIHSLIEESQNQQEKNECELLELDKWASLW
N22C-PEG750 derivative of HR241FreeFreeLinearLPegylation-PEG750 of cysteine at 22nd positionModified HR2 wild type peptideInhibitor to prevent virus ˆ’host cell membrane fusionNot mentioned20μM51.8Bovine TrypsinTrypsin degradation assay, Analytical reverse phase HPLCSolutions of bovine trypsin and the peptide or PEG ˆ’peptide conjugate in 10 mM PBS (pH 7.4)in vitrohttp://www.drugbank.ca/drugs/DB00162NoneCell ˆ’Cell Fusion Inhibition Efficacy (IC50)=4.2 ± 0.9nM
3144
227705642012
EWDREINNYTSLIHSLIEESQNQQEKNECELLELDKWASLW
N22C-PEG2000 derivative of HR241FreeFreeLinearLPegylation-PEG2000 of cysteine at22nd positionModified HR2 wild type peptideInhibitor to prevent virus ˆ’host cell membrane fusionNot mentioned20μM80.7Bovine TrypsinTrypsin degradation assay, Analytical reverse phase HPLCSolutions of bovine trypsin and the peptide or PEG ˆ’peptide conjugate in 10 mM PBS (pH 7.4)in vitrohttp://www.drugbank.ca/drugs/DB00163NoneCell ˆ’Cell Fusion Inhibition Efficacy (IC50)=5.1 ± 0.5nM
3145
227705642012
EWDREINNYTSLIHSLIEESQNQQEKNECELLELDKWASLW
Q29C derivative of HR241FreeFreeLinearLNoneModified HR2 wild type peptideInhibitor to prevent virus ˆ’host cell membrane fusionNot mentioned20μM38.6Bovine TrypsinTrypsin degradation assay, Analytical reverse phase HPLCSolutions of bovine trypsin and the peptide or PEG ˆ’peptide conjugate in 10 mM PBS (pH 7.4)in vitrohttp://www.drugbank.ca/drugs/DB00164NoneNot mentioned
3146
227705642012
EWDREINNYTSLIHSLIEESQNQQEKNECELLELDKWASLW
Q29C-PEG750 derivative of HR241FreeFreeLinearLPegylation-PEG750 of cysteine at 29th positionModified HR2 wild type peptideInhibitor to prevent virus ˆ’host cell membrane fusionNot mentioned20μM58.1Bovine TrypsinTrypsin degradation assay, Analytical reverse phase HPLCSolutions of bovine trypsin and the peptide or PEG ˆ’peptide conjugate in 10 mM PBS (pH 7.4)in vitrohttp://www.drugbank.ca/drugs/DB00165NoneCell ˆ’Cell Fusion Inhibition Efficacy (IC50)=5.2 ± 0.8nM
3147
227705642012
EWDREINNYTSLIHSLIEESQNQQEKNECELLELDKWASLW
Q29C-PEG2000 derivative of HR241FreeFreeLinearLPegylation-PEG2000 of cysteine at 29th positionModified HR2 wild type peptideInhibitor to prevent virus ˆ’host cell membrane fusionNot mentioned20μM84.1Bovine TrypsinTrypsin degradation assay, Analytical reverse phase HPLCSolutions of bovine trypsin and the peptide or PEG ˆ’peptide conjugate in 10 mM PBS (pH 7.4)in vitrohttp://www.drugbank.ca/drugs/DB00166NoneCell ˆ’Cell Fusion Inhibition Efficacy (IC50)=5.5 ± 0.5nM
3148
227705642012
EWDREINNYTSLIHSLIEESQNQQEKNEQELLELDKWASLWC
C terminus derivative of HR242FreeFreeLinearLNoneModified HR2 wild type peptideInhibitor to prevent virus ˆ’host cell membrane fusionNot mentioned20μM39Bovine TrypsinTrypsin degradation assay, Analytical reverse phase HPLCSolutions of bovine trypsin and the peptide or PEG ˆ’peptide conjugate in 10 mM PBS (pH 7.4)in vitrohttp://www.drugbank.ca/drugs/DB00167NoneNot mentioned
3149
227705642012
EWDREINNYTSLIHSLIEESQNQQEKNEQELLELDKWASLWC
C terminus-PEG750 derivative of HR242FreeFreeLinearLNoneModified HR2 wild type peptideInhibitor to prevent virus ˆ’host cell membrane fusionNot mentioned20μM81.2Bovine TrypsinTrypsin degradation assay, Analytical reverse phase HPLCSolutions of bovine trypsin and the peptide or PEG ˆ’peptide conjugate in 10 mM PBS (pH 7.4)in vitrohttp://www.drugbank.ca/drugs/DB00168NoneCell ˆ’Cell Fusion Inhibition Efficacy (IC50)=10.9 ± 2.2nM
3150
227705642012
EWDREINNYTSLIHSLIEESQNQQEKNEQELLELDKWASLWC
C terminus-PEG2000 derivative of HR242FreePegylation (PEG750)LinearLNoneModified HR2 wild type peptideInhibitor to prevent virus ˆ’host cell membrane fusionNot mentioned20μM126Bovine TrypsinTrypsin degradation assay, Analytical reverse phase HPLCSolutions of bovine trypsin and the peptide or PEG ˆ’peptide conjugate in 10 mM PBS (pH 7.4)in vitrohttp://www.drugbank.ca/drugs/DB00169NoneCell ˆ’Cell Fusion Inhibition Efficacy (IC50)=43.3 ± 14.8nM
3151
227705642012
EWDREINNYTSLIHSLIEECQNQQEKNEQELLELDKWASLW
S20C derivative of HR241FreePegylation (PEG2000)LinearLNoneModified HR2 wild type peptideInhibitor to prevent virus ˆ’host cell membrane fusionNot mentioned20μM38.6Bovine TrypsinTrypsin degradation assay, Analytical reverse phase HPLCSolutions of bovine trypsin and the peptide or PEG ˆ’peptide conjugate in 10 mM PBS (pH 7.4)in vitrohttp://www.drugbank.ca/drugs/DB00170NoneNot mentioned
3152
227705642012
EWDREINNYTSLIHSLIEECQNQQEKNEQELLELDKWASLW
S20C-PEG750 derivative of HR241FreeFreeLinearLPegylation-PEG750 of cysteine at 20th positionModified HR2 wild type peptideInhibitor to prevent virus ˆ’host cell membrane fusionNot mentioned20μM42Bovine TrypsinTrypsin degradation assay, Analytical reverse phase HPLCSolutions of bovine trypsin and the peptide or PEG ˆ’peptide conjugate in 10 mM PBS (pH 7.4)in vitrohttp://www.drugbank.ca/drugs/DB00171NoneCell ˆ’Cell Fusion Inhibition Efficacy (IC50)>400
3153
227705642012
EWDREINNYTSLIHSLIEECQNQQEKNEQELLELDKWASLW
S20C-PEG2000 derivative of HR241FreeFreeLinearLPegylation-PEG2000 of cysteine at 20th positionModified HR2 wild type peptideInhibitor to prevent virus ˆ’host cell membrane fusionNot mentioned20μM76.3Bovine TrypsinTrypsin degradation assay, Analytical reverse phase HPLCSolutions of bovine trypsin and the peptide or PEG ˆ’peptide conjugate in 10 mM PBS (pH 7.4)in vitrohttp://www.drugbank.ca/drugs/DB00172NoneCell ˆ’Cell Fusion Inhibition Efficacy (IC50)>401
3167
12136601975
FVNQHLCGSHLVEALYLVCGERGFFYTPKARREAQNPQAGAVELGGGLGGLNALALEGPPQKRGIVEQCCTSICSLYQLENYCN
Procine Proinsulin84FreeFreeCyclic (C7-C70,C19-C83,C69-C74)LNoneProinsulinNot mentionedNot reported5-8.6 µg/kg were injected.8.2 ±0.3Porcine blood proteasesRadioimmunoassayPorcine bloodin vivohttp://www.drugbank.ca/drugs/DB00186NoneNot reported
3178
80356441994
YRQSMNNFQGLRSFGCRFGTCTVQKLAHQIYQFTDKDKDNVAPRSKISPQGY
Adrenomedullin (ADM)52FreeFreeLinearLNoneSyntheticHormone in circulation controlNot reportedIntraarterial doses of 0.01-0.3 nmol55 to 80Cat blood proteasesHPLCHind limb vascular bed of the catin vivohttp://www.drugbank.ca/drugs/DB00197NoneNot reported
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.
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.
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.
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)
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
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.
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.
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
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
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
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)
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.
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.
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
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)
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.
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)
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.
5053
332841032020
YLGASVPSPDPLEPTREQCELNPACDELSDQYGLKTAYKRIYGITI
Mouse ucOCN46FreeFreeCyclic (C19-C25 Disulfide bond)LUncarboxylation at all glutamic acidOsteoblast Derived hormoneAntidiabetes0 to 5 hr at 37°C100 ng/mL~120Mouse plasma proteaseELISA Mouse plasmaIn VitroNoneNoneN.A.
5054
332841032020
YLGASVPSPDPLEPTREQCELNPACDELSDQYGLKTAYKRIYGITI
Mouse O-glycosylated ucOCN46FreeFreeCyclic (C19-C25 Disulfide bond)LO-glycosylation likely at Ser8 in SVPSPDP, Uncarboxylation at all glutamic acidOsteoblast Derived hormoneAntidiabetes0 to 5 hr at 37°C100 ng/mL>5Mouse plasma proteaseELISA Mouse plasmaIn VitroNoneNoneN.A.
5055
332841032020
YLGASVPSPDPLEPTREQCELNPACDELSDQYGLKTAYKRIYGITI
Mouse O-glycosylated ucOCN46FreeFreeCyclic (C19-C25 Disulfide bond)LO-glycosylation likely at Ser8 in SVPSPDP, Uncarboxylation at all glutamic acidOsteoblast Derived hormoneAntidiabetes2 hours at 37°C40 ng/g ~182 Mice serum proteaseOCN ELISAMice serumIn VivoNoneNoneN.A.
5056
332841032020
YLGASVPSPDPLEPTREQCELNPACDELSDQYGLKTAYKRIYGITI
Mouse ucOCN46FreeFreeCyclic (C19-C25 Disulfide bond)LUncarboxylation at all glutamic acidOsteoblast Derived hormoneAntidiabetes2 hours at 37°C40 ng/g ~108Mice serum proteaseOCN ELISAMice serumIn VivoNoneNoneN.A.
5060
331258432020
H-Aib-EGTYTNDVTEYCEEEAAKCFIEWLIKGKPSSGAPPPSYGWLDF
5a45FreeEither or nonsulfated gastrin-6 were coupled to the C-terminus of 2d and 2k through two OEG spacers, affording 5a−5d LinearLAib substiuition at position 2, Ser39 linked with fatty acidGLP-1 analogsAntidiabetesAt 0, 1, 2, 4, 8, 16, and 24 h, blood samples (~100 μL) were collected from fundus venous plexus50 nmol/kg1.7SD rats plasma proteaseLC−MS/MSSD rats plasmaIn VivoNoneNoneEC50 (nM) = 0.040 ± 0.011 (Effects of 5a on GLP-1R)
5061
331258432020
H-Aib-EGTYTNDVTEYLEEEAAKCFIEWLICGKPSSGAPPPSYGWLDF
5b45FreeEither or nonsulfated gastrin-6 were coupled to the C-terminus of 2d and 2k through two OEG spacers, affording 5a−5d LinearLAib substiuition at position 2,Ser39 linked with fatty acidGLP-1 analogsAntidiabetesAt 0, 1, 2, 4, 8, 16, and 24 h, blood samples (~100 μL) were collected from fundus venous plexus50 nmol/kg1.9SD rats plasma proteaseLC−MS/MSSD rats plasmaIn VivoNoneNoneEC50 (nM) = 0.048 ± 0.018 (Effects of 5b on GLP-1R)
5062
331258432020
H-Aib-EGTYTNDVTEY-C1-EEEAAK-C1-FIEWLIKGKPSSGAPPPSYGWLDF
6a45Free4c, 4d, 4m, and 4n were next C-terminally modified with the sequence Tyr-Gly-Trp-Leu-Asp-Phe-NH2 using two OEGs as the linker to generate 6a−6dLinearLC1 = structure given in paper, Aib substiuition at position 2,Ser39 linked with fatty acidGLP-1 analogsAntidiabetesAt 0, 1, 2, 4, 8, 16, and 24 h, blood samples (~100 μL) were collected from fundus venous plexus50 nmol/kg4.6SD rats plasma proteaseLC−MS/MSSD rats plasmaIn VivoNoneNoneEC50 (nM) = 0.022 ± 0.008 (Effects of 6a on GLP-1R)
5063
331258432020
H-Aib-EGTYTNDVTEYLEEEAAK-C1-FIEWLI-C1-GKPSSGAPPPSYGWLDF
6b45Free4c, 4d, 4m, and 4n were next C-terminally modified with the sequence Tyr-Gly-Trp-Leu-Asp-Phe-NH2 using two OEGs as the linker to generate 6a−6dLinearLC1 = structure given in paper,Aib substiuition at position 2,Ser39 linked with fatty acidGLP-1 analogsAntidiabetesAt 0, 1, 2, 4, 8, 16, and 24 h, blood samples (~100 μL) were collected from fundus venous plexus50 nmol/kg5SD rats plasma proteaseLC−MS/MSSD rats plasmaIn VivoNoneNoneEC50 (nM) = 0.041 ± 0.017 (Effects of 6b on GLP-1R)
5064
331258432020
H-Aib-EGTYTNDVTEY-C2-EEEAAK-C2-FIEWLIKGKPSSGAPPPSYGWLDF
7a45Free4c, 4d, 4m, and 4n were next C-terminally modified with the sequence Tyr-Gly-Trp-Leu-Asp-Phe-NH2 using two OEGs as the linker to generate 6a−6dLinearLModification of 6a and 6b with the introduction of C2 = structure given in paper,Aib substiuition at position 2,Ser39 linked with fatty acidGLP-1 analogsAntidiabetesAt 0, 1, 2, 4, 8, 16, and 24 h, blood samples (~100 μL) were collected from fundus venous plexus50 nmol/kg2.9SD rats plasma proteaseLC−MS/MSSD rats plasmaIn VivoNoneNoneEC50 (nM) = 0.041 ± 0.017 (Effects of 6b on GLP-1R)
5065
331258432020
H-Aib-EGTYTNDVTEYLEEEAAK-C2-FIEWLI-C2-GKPSSGAPPPSYGWLDF
7b45Free4c, 4d, 4m, and 4n were next C-terminally modified with the sequence Tyr-Gly-Trp-Leu-Asp-Phe-NH2 using two OEGs as the linker to generate 6a−6dLinearLModification of 6a and 6b with the introduction of C2 = structure given in paper,Aib substiuition at position 2,Ser39 linked with fatty acidGLP-1 analogsAntidiabetesAt 0, 1, 2, 4, 8, 16, and 24 h, blood samples (~100 μL) were collected from fundus venous plexus50 nmol/kg3.1SD rats plasma proteaseLC−MS/MSSD rats plasmaIn VivoNoneNoneEC50 (nM) = 0.041 ± 0.017 (Effects of 6b on GLP-1R)
5068
330570632020
GGGGSGGGGSGTSHLVKCAEKEKTFCVNGGECFMVKDLSNPSRYLCKCPNEFTGDRCQNYVMASFGGGGSGGGGS
ALM675FreeFreeLinearLNoneSyntheticHer4-Selective AgonismOvernight at 4 °C10 μg/mL1.4Mouse serum proteaseELISAMouse serumIn VitroNoneNoneHER4 binding KD = 440 nM
5108
328416602020
EGTFQAKQWLPQDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
XFL643FreeFreeLinearLModifcation of lysine site at position at 16 with C16 fatty acidGLP-1/GIP/Gcg receptor triagonistAntidiabetes, Antiobesity N.A.10 nmol/kg41.35 ± 1.42SD rats serum proteaseN.A.SD rats serumIn VivoNoneNoneEC50 (nM) = 0.12 (In vitro receptor activation profiles of XFL peptides for GLP-1R)
5109
328416602020
EGTFQAKQWLPQDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
XFL643FreeFreeLinearLModifcation of lysine site at position at 16 with C16 fatty acidGLP-1/GIP/Gcg receptor triagonistAntidiabetes, Antiobesity N.A.30 nmol/kg58.23 ± 2.17SD rats serum proteaseN.A.SD rats serumIn VivoNoneNoneEC50 (nM) = 0.12 (In vitro receptor activation profiles of XFL peptides for GLP-1R)
5110
328416602020
EGTFQAKQWLPQDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
XFL643FreeFreeLinearLModifcation of lysine site at position at 16 with C16 fatty acidGLP-1/GIP/Gcg receptor triagonistAntidiabetes, Antiobesity N.A.90 nmol/kg75.81 ± 3.58SD rats serum proteaseN.A.SD rats serumIn VivoNoneNoneEC50 (nM) = 0.12 (In vitro receptor activation profiles of XFL peptides for GLP-1R)
5123
327362622020
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPSLKEAKEKAIEELKKAGITSDYYFDLINKAKTVEGVNALKDEILKA
EX-AFF84FreeAFFLinearLNoneSyntheticAntiobesityBlood was withdrawn at 0, 5 min, 30 min, 1 h, 2 h, 4 h, 6 h, and 8 h post-administratio50 nmol/kg1.5ICR mice plasma proteaseELISAICR mice plasmaIn VivoNoneNoneKd(M) = 6.97 * 10-8(binding affinities of EX-ABD-AFF to glucagon-like peptide-1 receptor (GLP-1))
5124
327362622020
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPSLKEAKEKAIEELKKAGITSDYYFDLINKAKTVEGVNALKDEILKA
EX-ABD84FreeABDLinearLNoneSyntheticAntiobesityBlood was withdrawn at 0, 10 min, 1 h, 3 h, 8 h, 1 day, 2 day, 3 day, 4 day, 7 day, 10 day, and 14 day post-administratio50 nmol/kg84.02ICR mice plasma proteaseELISAICR mice plasmaIn VivoNoneNoneKd(M) = 6.97 * 10-8(binding affinities of EX-ABD-AFF to glucagon-like peptide-1 receptor (GLP-1))
5163
323874122020
HGEGTFTSDVSSYLEGQAAKEFIAWLVKGRCHGEGTFTSDVSSYLEGQAAKEFIAWLVKGRC
DIG-262FreebisMal-PEG(10KDa)LinearLRadioiodinated , A8G, G31C modification in GLP-1DIG conjugatesAntidiabetesThe collected samples at predose, 0.5, 1, 2, 4, 8, 24, 36, 48, 96, 144 and 168 h were stored at −80 °C50 nmol/kg62.6Cynomolgus monkeys plasma proteaseRP-HPLCCynomolgus monkeys plasmaIn VivoNoneNonekd (1/s) = 6.54 × 10−3 (binding results for DIG conjugates 2 with human GLP-1R ECD
5164
323874122020
HGEGTFTSDVSSYLEGQAAKEFIAWLVKGRCHGEGTFTSDVSSYLEGQAAKEFIAWLVKGRC
DIG-262FreebisMal-PEG(10KDa)LinearLRadioiodinated , A8G, G31C modification in GLP-1DIG conjugatesAntidiabetesThe collected samples at predose, 0.5, 1, 2, 4, 8, 24, 36, 48, 96, 144 and 168 h were stored at −80 °C100 nmol/kg97.2Cynomolgus monkeys plasma proteaseRP-HPLCCynomolgus monkeys plasmaIn VivoNoneNonekd (1/s) = 6.54 × 10−3 (binding results for DIG conjugates 2 with human GLP-1R ECD
5165
323874122020
HGEGTFTSDVSSYLEGQAAKEFIAWLVKGRCHGEGTFTSDVSSYLEGQAAKEFIAWLVKGRC
DIG-262FreebisMal-PEG(10KDa)LinearLRadioiodinated , A8G, G31C modification in GLP-1DIG conjugatesAntidiabetesThe collected samples at predose, 0.5, 1, 2, 4, 8, 24, 36, 48, 96, 144 and 168 h were stored at −80 °C150 nmol/kg120.4Cynomolgus monkeys plasma proteaseRP-HPLCCynomolgus monkeys plasmaIn VivoNoneNonekd (1/s) = 6.54 × 10−3 (binding results for DIG conjugates 2 with human GLP-1R ECD
5188
354966222020
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPSKKKKKK
Lixisenatide 44FreeAmidationLinearLNoneExendin-4 analogsAntidiabetesincubated at 37 °C for 6, 12, 24, and 48 h1000 ng/mL7.1Rats blood plasma proteaseLC-MS/MSRats blood plasma In VitroNoneNoneEC50(nM) = 0.076 ± 0.013 for Lixisenatide (in vitro GLP-1 receptor activation potency)
5189
354966222020
HGEGTFTSDLSQMEEEAVRLFIEWLKNGGPSSGAPPSKKKKKK
Lixisenatide 1a 44FreeAmidationLinearL(X1) MPAs modification on Lys12 lixisenatide analoguesAntidiabetesincubated at 37 °C for 6, 12, 24, and 48 h1000 ng/mL13.2Rats blood plasma proteaseLC-MS/MSRats blood plasma In VitroNoneNoneEC50(nM) = 0.19 ± 0.02 for Lixisenatide 1a (in vitro GLP-1 receptor activation potency)
5190
354966222020
HGEGTFTSDLSQMEEEAVRLFIEWLKNGGPSSGAPPSKKKKKK
Lixisenatide 1b44FreeAmidationLinearL(X2) MPAs modification on Lys12lixisenatide analoguesAntidiabetesincubated at 37 °C for 6, 12, 24, and 48 h1000 ng/mL19.1Rats blood plasma proteaseLC-MS/MSRats blood plasma In VitroNoneNoneEC50(nM) = 0.49 ± 0.11 for Lixisenatide 1b (in vitro GLP-1 receptor activation potency)
5191
354966222020
HGEGTFTSDLSQMEEEAVRLFIEWLKNGGPSSGAPPSKKKKKK
Lixisenatide 1c44FreeAmidationLinearL(X3) MPAs modification on Lys12lixisenatide analoguesAntidiabetesincubated at 37 °C for 6, 12, 24, and 48 h1000 ng/mL30Rats blood plasma proteaseLC-MS/MSRats blood plasma In VitroNoneNoneEC50(nM) = 0.98 ± 0.24 for Lixisenatide 1c (in vitro GLP-1 receptor activation potency)
5192
354966222020
HGEGTFTSDLSKQMEEEAVRLFIEWLNGGPSSGAPPSKKKKKK
Lixisenatide 1d44FreeAmidationLinearL(X1) MPAs modification on Lys12 lixisenatide analoguesAntidiabetesincubated at 37 °C for 6, 12, 24, and 48 h1000 ng/mL13.1Rats blood plasma proteaseLC-MS/MSRats blood plasma In VitroNoneNoneEC50(nM) = 0.085 ± 0.021 for Lixisenatide 1d (in vitro GLP-1 receptor activation potency)
5193
354966222020
HGEGTFTSDLSKQMEEEAVRLFIEWLNGGPSSGAPPSKKKKKK
Lixisenatide 1e44FreeAmidationLinearL(X2) MPAs modification on Lys12lixisenatide analoguesAntidiabetesincubated at 37 °C for 6, 12, 24, and 48 h1000 ng/mL21.2Rats blood plasma proteaseLC-MS/MSRats blood plasma In VitroNoneNoneEC50(nM) = 0.13 ± 0.03 for Lixisenatide 1e (in vitro GLP-1 receptor activation potency)
5194
354966222020
HGEGTFTSDLSKQMEEEAVRLFIEWLNGGPSSGAPPSKKKKKK
Lixisenatide 1f44FreeAmidationLinearL(X3) MPAs modification on Lys12lixisenatide analoguesAntidiabetesincubated at 37 °C for 6, 12, 24, and 48 h1000 ng/mL33.4Rats blood plasma proteaseLC-MS/MSRats blood plasma In VitroNoneNoneEC50(nM) = 0.32 ± 0.13 for Lixisenatide 1f (in vitro GLP-1 receptor activation potency)
5195
354966222020
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPSKKKKK
Lixisenatide 1g44FreeAmidationLinearL(X1) MPAs modification on Lys12 lixisenatide analoguesAntidiabetesincubated at 37 °C for 6, 12, 24, and 48 h1000 ng/mL11.9Rats blood plasma proteaseLC-MS/MSRats blood plasma In VitroNoneNoneEC50(nM) = 0.59 ± 0.16 for Lixisenatide 1g (in vitro GLP-1 receptor activation potency)
5196
354966222020
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPSKKKKK
Lixisenatide 1h44FreeAmidationLinearL(X2) MPAs modification on Lys12lixisenatide analoguesAntidiabetesincubated at 37 °C for 6, 12, 24, and 48 h1000 ng/mL17.8Rats blood plasma proteaseLC-MS/MSRats blood plasma In VitroNoneNoneEC50(nM) = 1.97 ± 0.53 for Lixisenatide 1h (in vitro GLP-1 receptor activation potency)
5197
354966222020
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPSKKKKK
Lixisenatide 1i44FreeAmidationLinearL(X3) MPAs modification on Lys12lixisenatide analoguesAntidiabetesincubated at 37 °C for 6, 12, 24, and 48 h1000 ng/mL31.6Rats blood plasma proteaseLC-MS/MSRats blood plasma In VitroNoneNoneEC50(nM) = 4.68 ± 0.85 for Lixisenatide 1i (in vitro GLP-1 receptor activation potency)
5309
316546852019
HGEGTFTSDVSSYLEGQAAKEFIAWLVKGRAEAAAAKEAAAAKEAAAAKA
Off-target repebody-fused GLP-150RepebodyGLP-1(7-36) (A8G) fused to the off-target repebody through linker (A(EAAAAK)3A) at C terminusLinearLNoneSyntheticAntidiabetesMice were euthanized at predetermined time points (n = 5 mice each at 0.05, 0.5, 1, 3, 6, 12 and 24 h post-injection) to collect whole blood from the aorta abdominalis25 nmol/kg1.3 (Initial Half Life)Mice plasma proteaseSandwich ELISAMice plasmaIn VivoPDB id: 5VAINoneC57BLKS/J lar- Leprdb/Leprdb mice (n = 5 per group, 6 weeks) were intravenously injected with the repebody-fused GLP-1 in complex with HSA, an off-target repebody-fused GLP-1, native GLP-1, and PBS. The blood glucose levels were analyzed at each time point for 24 h. The HSA-specific repebody-fused GLP-1 showed a significant decrease (**p < 0.005) in blood glucose level compared to other cases
5310
316546852019
HGEGTFTSDVSSYLEGQAAKEFIAWLVKGRAEAAAAKEAAAAKEAAAAKA
Repebody-fused GLP-1 in complex with HSA50RepebodyGLP-1(7-36) (A8G) fused to the repebody in complex with HSA through linker (A(EAAAAK)3A) at C terminusLinearLNoneSyntheticAntidiabetesMice were euthanized at predetermined time points (n = 5 mice each at 0.05, 0.5, 1, 3, 6, 12 and 24 h post-injection) to collect whole blood from the aorta abdominalis25 nmol/kg4.2 (Initial Half Life)Mice plasma proteaseSandwich ELISAMice plasmaIn VivoPDB id: 5VAINoneC57BLKS/J lar- Leprdb/Leprdb mice (n = 5 per group, 6 weeks) were intravenously injected with the repebody-fused GLP-1 in complex with HSA, an off-target repebody-fused GLP-1, native GLP-1, and PBS. The blood glucose levels were analyzed at each time point for 24 h. The HSA-specific repebody-fused GLP-1 showed a significant decrease (**p < 0.005) in blood glucose level compared to other cases
5311
316546852019
HGEGTFTSDVSSYLEGQAAKEFIAWLVKGRAEAAAAKEAAAAKEAAAAKA
Repebody-fused GLP-1 in complex with HSA50RepebodyGLP-1(7-36) (A8G) fused to the repebody in complex with HSA through linker (A(EAAAAK)3A) at C terminusLinearLNoneSyntheticAntidiabetesMice were euthanized at predetermined time points (n = 5 mice each at 0.05, 0.5, 1, 3, 6, 12 and 24 h post-injection) to collect whole blood from the aorta abdominalis25 nmol/kg10.7 (Terminal Half Life) Mice plasma proteaseSandwich ELISAMice plasmaIn VivoPDB id: 5VAINoneC57BLKS/J lar- Leprdb/Leprdb mice (n = 5 per group, 6 weeks) were intravenously injected with the repebody-fused GLP-1 in complex with HSA, an off-target repebody-fused GLP-1, native GLP-1, and PBS. The blood glucose levels were analyzed at each time point for 24 h. The HSA-specific repebody-fused GLP-1 showed a significant decrease (**p < 0.005) in blood glucose level compared to other cases
5313
316156712019
NSEIQNAVEVEEVVLPSIESPTENLPNNGSVVQPPSRSSPAGRPAIWIKDFVWGHIRPRRLTNDRLADMPLERRESWARMQRREWEEIEEEKGETQEEGG
Free-ADI100FreeFreeLinearLNonePurified from the mycelia of A. nidulanAnticancer20 days100 μl50.14Mice serum proteaseHPLCMice serumIn VivoNoneNoneIC50 = 6.3 ± 0.6(μmol/mg/min) in HepG-2 cells
5314
316156712019
NSEIQNAVEVEEVVLPSIESPTENLPNNGSVVQPPSRSSPAGRPAIWIKDFVWGHIRPRRLTNDRLADMPLERRESWARMQRREWEEIEEEKGETQEEGG
Dextran-ADI100FreeFreeLinearLADI was conjugated to dextran- reactive aldehyde groups via the formation of aldimine linkage Purified from the mycelia of A. nidulanAnticancer20 days100 μl66.8Mice serum proteaseHPLCMice serumIn VivoNoneNoneIC50 = 4.7 ± 0.9 (μmol/mg/min) in HepG-2 cells
5330
313894632019
ACAELVDNAVAIGGQGTFTSDYSYLDSRRAQDFVQWLMNTARNRNNIA
PP1849FreeFreeLinearLSer23 linked with X3 = Structure givven in paperOXM analogsAntidiabetes, Antiobesityblood was sampled pre-dose and at 0.5, 1, 2, 4, 8, 24, 48, 72, and 96 h post-dose30 nmoL/kg38.5 ± 5.9SD rats plasma proteaseLC-MS, ELISASD rats plasmaIn VivoNoneNoneEC50(nM) = 0.487 for Human GLP-1R
5348
312789572019
HGEGTFTSDLSKQMEEEQVRLFIEWLKNGGPSSGAPPPSVPGVGVPGVGVPGVGVPGVGVPGVGVPGVGVPGVGVPGVGVPGVGVPGVGHHHHHH
Ex-(EBP)10-6xHis96FreeTen repeats of EBP without a linker sequence, (EBP)10 fused at the C-terminus of the exenatide for Ex-(EBP)10, 6xHis tagLinearLInserting valine to the X amino acid position in the EBP (VPGXG) sequence, labeled with Flamma® 675 vinylsulfoneFusion protein of exenatide and elastin-based polypeptide from recombinant Saccharomyces cerevisiaeAntidiabetesThe fluorescence images of the mice were measured at 0, 1, 2, 4, 8, 12, 24, 48, 72, 96, and 147 h after injection20 μg7.7Mouse body proteaseIn vivo imaging systemMouse bodyIn VivoNoneNoneN.A.
5389
310837402019
HSEGTFTSDVSSYLEGQAAKEFIAWLVKGGVKALIDEILAA
SKL-1828741FreeAmidationLinearL3H labeling at Tyr, Ser8 modificationGLP-1 analogsAntidiabetesBlood samples were collected via the jugular vein for rats, the cephalic vein for monkeys, and the jugular venous or femoral venous catheter for mini-pigs, using a heparinized syringe at 0.083, 0.25, 0.5, 1, 2, 4, 6, 8, 10, 12, 24, 48, and 72h for intravenous10 µg/kg5.4 ± 0.3 (Elimination Half Life)SD rats plasma proteaseLC-MS/MS SD rats plasmaIn VivoNoneNoneN.A.
5390
310837402019
HSEGTFTSDVSSYLEGQAAKEFIAWLVKGGVKALIDEILAA
SKL-1828741FreeAmidationLinearL3H labeling at Tyr, Ser8 modificationGLP-1 analogsAntidiabetesBlood samples were collected via the jugular vein for rats, the cephalic vein for monkeys, and the jugular venous or femoral venous catheter for mini-pigs, using a heparinized syringe at 0.25, 0.5, 1, 2, 4, 6, 8, 10, 12, 24, 48, and 72 h for subcutaneous administration10 µg/kg5.8 ± 0.4 (Elimination Half Life)SD rats plasma proteaseLC-MS/MS SD rats plasmaIn VivoNoneNoneN.A.
5391
310837402019
HSEGTFTSDVSSYLEGQAAKEFIAWLVKGGVKALIDEILAA
SKL-1828741FreeAmidationLinearL3H labeling at Tyr, Ser8 modificationGLP-1 analogsAntidiabetesBlood samples were collected via the jugular vein for rats, the cephalic vein for monkeys, and the jugular venous or femoral venous catheter for mini-pigs, using a heparinized syringe at 0.25, 0.5, 1, 2, 4, 6, 8, 10, 12, 24, 48, and 72 h for subcutaneous administration30 µg/kg5.4 ± 0.3 (Elimination Half Life)SD rats plasma proteaseLC-MS/MS SD rats plasmaIn VivoNoneNoneN.A.
5392
310837402019
HSEGTFTSDVSSYLEGQAAKEFIAWLVKGGVKALIDEILAA
SKL-1828741FreeAmidationLinearL3H labeling at Tyr, Ser8 modificationGLP-1 analogsAntidiabetesBlood samples were collected via the jugular vein for rats, the cephalic vein for monkeys, and the jugular venous or femoral venous catheter for mini-pigs, using a heparinized syringe at 0.25, 0.5, 1, 2, 4, 6, 8, 10, 12, 24, 48, and 72 h for subcutaneous administration100 µg/kg5.2 ± 0.2 (Elimination Half Life)SD rats plasma proteaseLC-MS/MS SD rats plasmaIn VivoNoneNoneN.A.
5393
310837402019
HSEGTFTSDVSSYLEGQAAKEFIAWLVKGGVKALIDEILAA
SKL-1828741FreeAmidationLinearL3H labeling at Tyr, Ser8 modificationGLP-1 analogsAntidiabetesBlood samples were collected via the jugular vein for rats, the cephalic vein for monkeys, and the jugular venous or femoral venous catheter for mini-pigs, using a heparinized syringe at 0.083, 0.25, 0.5, 1, 2, 4, 6, 8, 10, 12, 24, 48, and 72h for intravenous17.4 µ/kg9.0 ± 1.8 (Elimination Half Life)Cynomolgus monkeys plasma proteaseLC-MS/MS Cynomolgus monkeys plasmaIn VivoNoneNoneN.A.
5394
310837402019
HSEGTFTSDVSSYLEGQAAKEFIAWLVKGGVKALIDEILAA
SKL-1828741FreeAmidationLinearL3H labeling at Tyr, Ser8 modificationGLP-1 analogsAntidiabetesBlood samples were collected via the jugular vein for rats, the cephalic vein for monkeys, and the jugular venous or femoral venous catheter for mini-pigs, using a heparinized syringe at 0.25, 0.5, 1, 2, 4, 6, 8, 10, 12, 24, 48, and 72 h for subcutaneous administration17.4 µ/kg11.4 ± 1.0 (Elimination Half Life)Cynomolgus monkeys plasma proteaseLC-MS/MS Cynomolgus monkeys plasmaIn VivoNoneNoneN.A.
5395
310837402019
HSEGTFTSDVSSYLEGQAAKEFIAWLVKGGVKALIDEILAA
SKL-1828741FreeAmidationLinearL3H labeling at Tyr, Ser8 modificationGLP-1 analogsAntidiabetesBlood samples were collected via the jugular vein for rats, the cephalic vein for monkeys, and the jugular venous or femoral venous catheter for mini-pigs, using a heparinized syringe at 0.083, 0.25, 0.5, 1, 2, 4, 6, 8, 10, 12, 24, 48, and 72h for intravenous17.4 µ/kg12.9 ± 1.0 (Elimination Half Life)Göttingen minipigs plasma proteaseLC-MS/MS Göttingen minipigs plasmaIn VivoNoneNoneN.A.
5396
310837402019
HSEGTFTSDVSSYLEGQAAKEFIAWLVKGGVKALIDEILAA
SKL-1828741FreeAmidationLinearL3H labeling at Tyr, Ser8 modificationGLP-1 analogsAntidiabetesBlood samples were collected via the jugular vein for rats, the cephalic vein for monkeys, and the jugular venous or femoral venous catheter for mini-pigs, using a heparinized syringe at 0.25, 0.5, 1, 2, 4, 6, 8, 10, 12, 24, 48, and 72 h for subcutaneous administration17.4 µ/kg15.4 ± 0.3 (Elimination Half Life)Göttingen minipigs plasma proteaseLC-MS/MS Göttingen minipigs plasmaIn VivoNoneNoneN.A.
5427
355207042019
HGEGTFTSDVSSYLEGQAAKEFIAWLVKGRCHGEGTFTSDVSSYLEGQAAKEFIAWLVKGRC
Di-GLP-162FreeBis-maleimide-NH2LinearLNoneGLP-1 analogsAntidiabetesAt each predetermined times (1, 2, 3, 4, 6, 12, 24 and 36 h), there mice were sacrificed and ∼200 μL of blood samples were collected50 nmol/kg 1.8 ± 0.2Kunming mice plasma proteaseLC-MS/MSKunming mice plasmaIn VivoPDB id: 5VAINoneEC50 = 0.039 ± 0.007 nM
5428
355207042019
HGEGTFTSDVSSYLEGQAAKEFIAWLVKGRCHGEGTFTSDVSSYLEGQAAKEFIAWLVKGRC
Lip-Di-GLP-1 62FreeBis-maleimide-C16 conjugation at C terminalLinearLNoneGLP-1 analogsAntidiabetesAt each predetermined times (1, 2, 3, 4, 6, 12, 24 and 36 h), there mice were sacrificed and ∼200 μL of blood samples were collected50 nmol/kg 7.0 ± 0.7 Kunming mice plasma proteaseLC-MS/MSKunming mice plasmaIn VivoPDB id: 5VAINoneEC50 = 0.056 ± 0.018 nM
5450
307564832019
GLAEAKVLANRELDKYGVSDYYKNLINNAKTVEGVKALIDEILAALP
ABD–Dox47FreeDox conjugationLinearLNoneDerived from streptococcal protein GAnticancerBlood samples were collected at 40 s, 15 and 30 min, and 2, 4, 8, 24, 48, 72, and 96 h post injection 5 mg/kg29.4 ± 0.8 (Elimination Half Life)Mice plasma proteaseFlurorescence assayMice plasmaIn VivoNoneNone(IC50) of ABD–Dox was 6.4 × 10−6 for C26 cell
5520
305434202019
(QLYSALANKCCHVGVOKRSLARFC)-DSWMEEVIKLCGRELVRAQIAICGMSTWS
R253FreeFreeLinearLB-D1A Cys mutationR3 based relaxin analogsRole in Hemodynamics and Renal function and has shown preclinical efficacy in multiple disease models, including Acute Heart Failure, Fibrosis, Preeclampsia, and Corneal Wound HealingN.A.0.3 mg/kg0.3Mouse plasma proteaseLC-MSMouse plasmaIn VivoNoneNoneEC50(nM) = 0.025 ± 0.004 
5521
305434202019
(QLYSALANKCCHVGVOKRSLARFC)-(DSWMEEVIKLCGRELVRAQIAICGMSTWS)
R253FreeFreeLinearLB-D1A Cys mutationR3 based relaxin analogsRole in Hemodynamics and Renal function and has shown preclinical efficacy in multiple disease models, including Acute Heart Failure, Fibrosis, Preeclampsia, and Corneal Wound HealingN.A.0.3 mg/kg7Mouse plasma proteaseLC-MSMouse plasmaIn VivoNoneNoneEC50(nM) = 0.025 ± 0.55
5522
305434202019
(QLYSALANKCCHVGVOKRSLARFC)-(ASWMEEVIKLCGRELVRAQIAICGMSTWC)
R3-0153FreeFA-01LinearLB-S29C,D1A Cys mutationR3 based relaxin analogsRole in Hemodynamics and Renal function and has shown preclinical efficacy in multiple disease models, including Acute Heart Failure, Fibrosis, Preeclampsia, and Corneal Wound HealingN.A.0.3 mg/kgN.A.Mouse plasma proteaseLC-MSMouse plasmaIn VivoNoneNoneEC50(nM) = 4.3 ± 0.005
5523
305434202019
(QLYSALANKCCHVGVOKRSLARFC)-(ASWMEEVIKLCGRELVRAQIAICGMSTWC)
R3-0253FreeFA-02LinearLB-S29C,D1A Cys mutationR3 based relaxin analogsRole in Hemodynamics and Renal function and has shown preclinical efficacy in multiple disease models, including Acute Heart Failure, Fibrosis, Preeclampsia, and Corneal Wound HealingN.A.0.3 mg/kg1Mouse plasma proteaseLC-MSMouse plasmaIn VivoNoneNoneEC50(nM) = 0.028 ± 0.18
5524
305434202019
(QLYSALANKCCHVGVOKRSLARFC)-(ASWMEEVIKLCGRELVRAQIAICGMSTWC)
R3-0253FreeFA-02LinearLB-S29C,D1A Cys mutationR3 based relaxin analogsRole In Hemodynamics And Renal Function And Has Shown Preclinical Efficacy In Multiple Disease Models, Including Acute Heart Failure, Fibrosis, Preeclampsia, And Corneal Wound HealingN.A.0.3 mg/kg1Mouse plasma proteaseLC-MSmouse plasmaIn VivoNoneNoneEC50(nM) = 0.028 ± 0.10
5525
305434202019
(QLYSALANKCCHVGVOKRSLARFC)-(ASWMEEVIKLCGRELVRAQIAICGMSTWC)
R3-0853FreeFA-08LinearLB-S29C,D1A Cys mutationR3 based relaxin analogsRole In Hemodynamics And Renal Function And Has Shown Preclinical Efficacy In Multiple Disease Models, Including Acute Heart Failure, Fibrosis, Preeclampsia, And Corneal Wound HealingN.A.0.3 mg/kgN.A.Mouse plasma proteaseLC-MSmouse plasmaIn VivoNoneNoneEC50(nM) = 1.5
5526
305434202019
(QLYSALANKCCHVGVOKRSLARFC)-(ASWMEEVIKLCGRELVRAQIAICGMSTWC)
R3-0953FreeFA-09LinearLB-S29C,D1A Cys mutationR3 based relaxin analogsRole In Hemodynamics And Renal Function And Has Shown Preclinical Efficacy In Multiple Disease Models, Including Acute Heart Failure, Fibrosis, Preeclampsia, And Corneal Wound HealingN.A.0.3 mg/kgN.A.Mouse plasma proteaseLC-MSmouse plasmaIn VivoNoneNoneEC50(nM) = 0.8
5555
316156712019
NSEIQNAVEVEEVVLPSIESPTENLPNNGSVVQPPSRSSPAGRPAIWIKDFVWGHIRPRRLTNDRLADMPLERRESWARTQEEGG
Free-ADI85FreeFreeLinearLNoneIsolated from Thermophilic Aspergillus nidulansAnticancer4°CN.A.1445 (Activity Half Life)Mice plasma proteaseStandard assayMice plasmaIn VivoNoneNoneIC50 = 6.3 ± 0.6(μmol/mg/min) in HepG-2 cells
5556
316156712019
NSEIQNAVEVEEVVLPSIESPTENLPNNGSVVQPPSRSSPAGRPAIWIKDFVWGHIRPRRLTNDRLADMPLERRESWARTQEEGG
Dextran-ADI85FreeFreeLinearLADI was conjugated to dextran- reactive aldehyde groups via the formation of aldimine linkage SyntheticAnticancer4°CN.A.2440 (Activity Half Life)Mice plasma proteaseStandard assayMice plasmaIn VivoNoneNoneIC50 = 4.7 ± 0.9 (μmol/mg/min) in HepG-2 cells
5557
316156712019
NSEIQNAVEVEEVVLPSIESPTENLPNNGSVVQPPSRSSPAGRPAIWIKDFVWGHIRPRRLTNDRLADMPLERRESWARTQEEGG
Free-ADI85FreeFreeLinearLNoneIsolated from Thermophilic Aspergillus nidulansAnticancer30 °CN.A.23.5 (Activity Half Life)Mice plasma proteaseStandard assayMice plasmaIn VivoNoneNoneIC50 = 6.3 ± 0.6(μmol/mg/min) in HepG-2 cells
5558
316156712019
NSEIQNAVEVEEVVLPSIESPTENLPNNGSVVQPPSRSSPAGRPAIWIKDFVWGHIRPRRLTNDRLADMPLERRESWARTQEEGG
Dextran-ADI85FreeFreeLinearLADI was conjugated to dextran- reactive aldehyde groups via the formation of aldimine linkage SyntheticAnticancer30 °CN.A.40.2 (Activity Half Life)Mice plasma proteaseStandard assayMice plasmaIn VivoNoneNoneIC50 = 4.7 ± 0.9 (μmol/mg/min) in HepG-2 cells
5559
316156712019
NSEIQNAVEVEEVVLPSIESPTENLPNNGSVVQPPSRSSPAGRPAIWIKDFVWGHIRPRRLTNDRLADMPLERRESWARTQEEGG
Free-ADI85FreeFreeLinearLNoneIsolated from Thermophilic Aspergillus nidulansAnticancer37°CN.A.17.3 (Activity Half Life) Mice plasma proteaseStandard assayMice plasmaIn VivoNoneNoneIC50 = 6.3 ± 0.6(μmol/mg/min) in HepG-2 cells
5560
316156712019
NSEIQNAVEVEEVVLPSIESPTENLPNNGSVVQPPSRSSPAGRPAIWIKDFVWGHIRPRRLTNDRLADMPLERRESWARTQEEGG
Dextran-ADI85FreeFreeLinearLADI was conjugated to dextran- reactive aldehyde groups via the formation of aldimine linkage SyntheticAnticancer37°CN.A.34.2 (Activity Half Life)Mice plasma proteaseStandard assayMice plasmaIn VivoNoneNoneIC50 = 4.7 ± 0.9 (μmol/mg/min) in HepG-2 cells
5561
316156712019
NSEIQNAVEVEEVVLPSIESPTENLPNNGSVVQPPSRSSPAGRPAIWIKDFVWGHIRPRRLTNDRLADMPLERRESWARTQEEGG
Free-ADI85FreeFreeLinearLNoneIsolated from Thermophilic Aspergillus nidulansAnticancer45°CN.A.3.4 (Activity Half Life)Mice plasma proteaseStandard assayMice plasmaIn VivoNoneNoneIC50 = 6.3 ± 0.6(μmol/mg/min) in HepG-2 cells
5562
316156712019
NSEIQNAVEVEEVVLPSIESPTENLPNNGSVVQPPSRSSPAGRPAIWIKDFVWGHIRPRRLTNDRLADMPLERRESWARTQEEGG
Dextran-ADI85FreeFreeLinearLADI was conjugated to dextran- reactive aldehyde groups via the formation of aldimine linkage SyntheticAnticancer45°CN.A.8.4 (Activity Half Life)Mice plasma proteaseStandard assayMice plasmaIn VivoNoneNoneIC50 = 4.7 ± 0.9 (μmol/mg/min) in HepG-2 cells
5566
312819492019
KDQSPLAGESGETEYITEVYGNQQNPVDIDKKLPNETGFSGNMVETEDT
FUD49FreeFreeLinearLSulfo-Cy5 fluorophoreSyntheticTherapeutic candidate for disorders linked with hyperdeposition of fibronectin-modulated ECM proteinsAt time points of 30 min and 1, 3, 6, 12, 24, 36, and 48 h12.5 mg/kg 0.81 (Abosrption Half Life)N.A.Fluorescence in vivo imagingMiceIn Vivohttps://pmc.ncbi.nlm.nih.gov/articles/PMC5705399/NoneN.A.
5567
312819492019
KDQSPLAGESGETEYITEVYGNQQNPVDIDKKLPNETGFSGNMVETEDT
10K PEG-FUD 4910K PEGFreeLinearLSulfo-Cy5 fluorophoreSyntheticTherapeutic candidate for disorders linked with hyperdeposition of fibronectin-modulated ECM proteinsAt time points of 30 min and 1, 3, 6, 12, 24, 36, and 48 h12.5 mg/kg 3.28 (Abosrption Half Life)N.A.Fluorescence in vivo imagingMiceIn Vivohttps://pmc.ncbi.nlm.nih.gov/articles/PMC5705399/NoneN.A.
5568
312819492019
KDQSPLAGESGETEYITEVYGNQQNPVDIDKKLPNETGFSGNMVETEDT
20K PEG-FUD 4920K PEGFreeLinearLSulfo-Cy5 fluorophoreSyntheticTherapeutic candidate for disorders linked with hyperdeposition of fibronectin-modulated ECM proteinsAt time points of 30 min and 1, 3, 6, 12, 24, 36, and 48 h12.5 mg/kg 6.77 (Abosrption Half Life)N.A.Fluorescence in vivo imagingMiceIn Vivohttps://pmc.ncbi.nlm.nih.gov/articles/PMC5705399/NoneN.A.
5569
312819492019
KDQSPLAGESGETEYITEVYGNQQNPVDIDKKLPNETGFSGNMVETEDT
40K PEG-FUD 4940K PEGFreeLinearLSulfo-Cy5 fluorophoreSyntheticTherapeutic candidate for disorders linked with hyperdeposition of fibronectin-modulated ECM proteinsAt time points of 30 min and 1, 3, 6, 12, 24, 36, and 48 h12.5 mg/kg 10.09 (Abosrption Half Life)N.A.Fluorescence in vivo imagingMiceIn Vivohttps://pmc.ncbi.nlm.nih.gov/articles/PMC5705399/NoneN.A.
5570
312819492019
KDQSPLAGESGETEYITEVYGNQYNSVDPDKKLINEGGFSTNMVEPEDT
mFUD49FreeFreeLinearLSulfo-Cy5 fluorophoreSyntheticTherapeutic candidate for disorders linked with hyperdeposition of fibronectin-modulated ECM proteinsAt time points of 30 min and 1, 3, 6, 12, 24, 36, and 48 h12.5 mg/kg 0.86 (Abosrption Half Life)N.A.Fluorescence in vivo imagingMiceIn Vivohttps://pmc.ncbi.nlm.nih.gov/articles/PMC5705399/NoneN.A.
5571
312819492019
KDQSPLAGESGETEYITEVYGNQQNPVDIDKKLPNETGFSGNMVETEDT
10K PEG-mFUD 4910K PEGFreeLinearLSulfo-Cy5 fluorophoreSyntheticTherapeutic candidate for disorders linked with hyperdeposition of fibronectin-modulated ECM proteinsAt time points of 30 min and 1, 3, 6, 12, 24, 36, and 48 h12.5 mg/kg 3.06 (Abosrption Half Life)N.A.Fluorescence in vivo imagingMiceIn Vivohttps://pmc.ncbi.nlm.nih.gov/articles/PMC5705399/NoneN.A.
5572
312819492019
KDQSPLAGESGETEYITEVYGNQQNPVDIDKKLPNETGFSGNMVETEDT
20K PEG-mFUD 4920K PEGFreeLinearLSulfo-Cy5 fluorophoreSyntheticTherapeutic candidate for disorders linked with hyperdeposition of fibronectin-modulated ECM proteinsAt time points of 30 min and 1, 3, 6, 12, 24, 36, and 48 h12.5 mg/kg 5.25 (Abosrption Half Life)N.A.Fluorescence in vivo imagingMiceIn Vivohttps://pmc.ncbi.nlm.nih.gov/articles/PMC5705399/NoneN.A.
5573
312819492019
KDQSPLAGESGETEYITEVYGNQQNPVDIDKKLPNETGFSGNMVETEDT
40K PEG-mFUD4940K PEGFreeLinearLSulfo-Cy5 fluorophoreSyntheticTherapeutic candidate for disorders linked with hyperdeposition of fibronectin-modulated ECM proteinsAt time points of 30 min and 1, 3, 6, 12, 24, 36, and 48 h12.5 mg/kg 8.36 (Abosrption Half Life)N.A.Fluorescence in vivo imagingMiceIn Vivohttps://pmc.ncbi.nlm.nih.gov/articles/PMC5705399/NoneN.A.
5662
300966512018
HGEGTYTNDVTEYLEEEAAKEFIEWLIKGKPSSGAPPPSCHGEGTYTNDVTEYLEEEAAKEFIEWLIKGKPSSGAPPPSC
Analogue 680FreeC terminal Cys extension for bis-maleimide linkageLinearLConjugation of Palmitic acid at Lys20 (single monomer) , dimerizationDimeric lipidated Xenopus GLP-1 analoguesAntidiabetesAt 1, 2, 3, 4, 6, 12, 24 and 48 h after injection, three Kunming mice were sacrificed at each time point and blood samples (~200 mL) were collected through extracting eyeball50 nmol/kg10.8 ± 0.8Kunming mice plasma proteaseLC-MS/MSKunming mice plasmaIn VivoNoneNoneEC50 = 1.4 ± 0.5 nM in HEK293 cells
5663
300966512018
HGEGTYTNDVTEYLEEEAAKEFIEWLIKGKPSSGAPPPSCHGEGTYTNDVTEYLEEEAAKEFIEWLIKGKPSSGAPPPSC
Analogue 680FreeC terminal Cys extension for bis-maleimide linkageLinearLConjugation of Palmitic acid at Lys20 (single monomer) , dimerizationDimeric lipidated Xenopus GLP-1 analoguesAntidiabetesBlood samples (100e150 mL) were obtained from fundus venous plexus and stored in polyethylene tubes containing heparin50 nmol/kg12.9 ± 3.6SD rats plasma proteaseLC-MS/MSSD rats plasmaIn VivoNoneNoneEC50 = 1.4 ± 0.5 nM in HEK293 cells
5664
300411532018
GIVEQCCTSICSLYQLENYCN/FVNQHLCGSHLVEALYLVCGERGFFYTPKT
HI51FreeFreeCyclic (3 S-S Bond)LNoneSyntheticAntidiabetesAt each time point (0, 0.5, 1, 2, 4 h), 50 µL of SCts were collected from the incubation mixture1 µM<0.5Rats SCT proteaseLC-HRMS1 mg/ml rats SCT protein In Vitrohttps://sci-hub.st/10.1016/j.jpba.2018.07.009, PDB id: 1SF1NoneN.A.
5665
300411532018
GIVEQCCTSICSLYQLENYCN/FVNQHLCGSHLVEALYLVCGERGFFYTPKT
HI51FreeFreeCyclic (3 S-S Bond)LNoneSyntheticAntidiabetesAt each time point (0, 0.5, 1, 2, 4 h), 50 µL of SCts were collected from the incubation mixture1 µM<0.5Rats SCT proteaseLC-HRMS2 mg/ml rats SCT protein In Vitrohttps://sci-hub.st/10.1016/j.jpba.2018.07.009, PDB id: 1SF1NoneN.A.
5666
300411532018
GIVEQCCTSICSLYQLENYCN/FVNQHLCGSHLVEALYLVCGERGFFYTPKT
HI51FreeFreeCyclic (3 S-S Bond)LNoneSyntheticAntidiabetesAt each time point (0, 0.5, 1, 2, 4 h), 50 µL of SCts were collected from the incubation mixture1 µM<0.5Rats SCT proteaseLC-HRMS4 mg/ml rats SCT protein In Vitrohttps://sci-hub.st/10.1016/j.jpba.2018.07.009, PDB id: 1SF1NoneN.A.
5667
300411532018
GIVEQCCTSICSLYQLENYCN/FVNQHLCGSHLVEALYLVCGERGFFYTPKT
HI51FreeFreeCyclic (3 S-S Bond)LNoneSyntheticAntidiabetesAt each time point (0, 0.5, 1, 2, 4 h), 50 µL of SCts were collected from the incubation mixture10 µM> 4 Rats SCT proteaseLC-HRMS1 mg/ml rats SCT protein In Vitrohttps://sci-hub.st/10.1016/j.jpba.2018.07.009, PDB id: 1SF1NoneN.A.
5668
300411532018
GIVEQCCTSICSLYQLENYCN/FVNQHLCGSHLVEALYLVCGERGFFYTPKT
HI51FreeFreeCyclic (3 S-S Bond)LNoneSyntheticAntidiabetesAt each time point (0, 0.5, 1, 2, 4 h), 50 µL of SCts were collected from the incubation mixture10 µM3.43Rats SCT proteaseLC-HRMS2 mg/ml rats SCT protein In Vitrohttps://sci-hub.st/10.1016/j.jpba.2018.07.009, PDB id: 1SF1NoneN.A.
5669
300411532018
GIVEQCCTSICSLYQLENYCN/FVNQHLCGSHLVEALYLVCGERGFFYTPKT
HI51FreeFreeCyclic (3 S-S Bond)LNoneSyntheticAntidiabetesAt each time point (0, 0.5, 1, 2, 4 h), 50 µL of SCts were collected from the incubation mixture10 µM0.56Rats SCT proteaseLC-HRMS4 mg/ml rats SCT protein In Vitrohttps://sci-hub.st/10.1016/j.jpba.2018.07.009, PDB id: 1SF1NoneN.A.
5670
300411532018
GIVEQCCTSICSLYQLENYCN/FVNQHLCGSHLVEALYLVCGERGFFYTPKT
HI51FreeFreeCyclic (3 S-S Bond)LNoneSyntheticAntidiabetesAt each time point (0, 0.5, 1, 2, 4 h), 50 µL of SCts were collected from the incubation mixture50 µM> 4Rats SCT proteaseLC-HRMS1 mg/ml rats SCT protein In Vitrohttps://sci-hub.st/10.1016/j.jpba.2018.07.009, PDB id: 1SF1NoneN.A.
5671
300411532018
GIVEQCCTSICSLYQLENYCN/FVNQHLCGSHLVEALYLVCGERGFFYTPKT
HI51FreeFreeCyclic (3 S-S Bond)LNoneSyntheticAntidiabetesAt each time point (0, 0.5, 1, 2, 4 h), 50 µL of SCts were collected from the incubation mixture50 µM> 4Rats SCT proteaseLC-HRMS2 mg/ml rats SCT protein In Vitrohttps://sci-hub.st/10.1016/j.jpba.2018.07.009, PDB id: 1SF1NoneN.A.
5672
300411532018
GIVEQCCTSICSLYQLENYCN/FVNQHLCGSHLVEALYLVCGERGFFYTPKT
HI51FreeFreeCyclic (3 S-S Bond)LNoneSyntheticAntidiabetesAt each time point (0, 0.5, 1, 2, 4 h), 50 µL of SCts were collected from the incubation mixture50 µM> 4Rats SCT proteaseLC-HRMS4 mg/ml rats SCT protein In Vitrohttps://sci-hub.st/10.1016/j.jpba.2018.07.009, PDB id: 1SF1NoneN.A.
5674
300411532018
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPSKKKKKK
Lixisenatide 44FreeAmidationLinearLNoneGLP-1 analogsAntidiabetesAt each time point (0, 0.5, 1, 2, 4 h), 50 µL of SCts were collected from the incubation mixture10 µM<0.5Human SCT proteaseLC-HRMS1 mg/ml human SCT proteinIn VitroNoneNoneN.A.
5678
300411532018
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPSKKKKKK
Lixisenatide 44FreeAmidationLinearLNoneGLP-1 analogsAntidiabetesAt each time point (0, 0.5, 1, 2, 4 h), 50 µL of SCts were collected from the incubation mixture10 µM<0.5SD rats SCT proteaseLC-HRMS1 mg/ml SD rats SCT proteinIn VitroNoneNoneN.A.
5682
300411532018
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPSKKKKKK
Lixisenatide 44FreeAmidationLinearLNoneGLP-1 analogsAntidiabetesAt each time point (0, 0.5, 1, 2, 4 h), 50 µL of SCts were collected from the incubation mixture10 µM<0.5Göttingen minipigs SCT proteaseLC-HRMS1 mg/ml göttingen minipigs SCT proteinIn VitroNoneNoneN.A.
5719
297992052018
HGEGTYTNDVTEYLEEEAA-X1-EFIEWLIKGKPSSGAPPSKKKKKK
4m43FreeFreeLinearLX1 = structure given in paperXenopus GLP-1 analogsAntidiabetes37°C over 72 h1000 ng/mL 18.8Rats plasma proteaseLC-MS/MS.Rats plasmaIn VitroNoneNoneEC50(nM) = 0.18 ± 0.06
5720
297992052018
HGEGTYTNDVTEYLEEEAA-X2-EFIEWLIKGKPSSGAPPSKKKKKK
4n43FreeFreeLinearLX2 = structure given in paperXenopus GLP-1 analogsAntidiabetes37°C over 72 h1000 ng/mL 26.6Rats plasma proteaseLC-MS/MS.Rats plasmaIn VitroNoneNoneEC50(nM) = 0.44 ± 0.11
5721
297992052018
HGEGTYTNDVTEYLEEEAA-X3-EFIEWLIKGKPSSGAPPSKKKKKK
4o43FreeFreeLinearLX3 = structure given in paperXenopus GLP-1 analogsAntidiabetes37°C over 72 h1000 ng/mL 36.4Rats plasma proteaseLC-MS/MS.Rats plasmaIn VitroNoneNoneEC50(nM) = 0.98 ± 0.18
5722
297992052018
HGEGTYTNDVTEYLEEEAAKEFIEWLI-X1-GKPSSGAPPSKKKKKK
4p43FreeFreeLinearLX1 = structure given in paperXenopus GLP-1 analogsAntidiabetes37°C over 72 h1000 ng/mL 16.9Rats plasma proteaseLC-MS/MS.Rats plasmaIn VitroNoneNoneEC50(nM) = 0.14 ± 0.02
5723
297992052018
HGEGTYTNDVTEYLEEEAAKEFIEWLI-X2-GKPSSGAPPSKKKKKK
4q43FreeFreeLinearLX2 = structure given in paperXenopus GLP-1 analogsAntidiabetes37°C over 72 h1000 ng/mL 27.2Rats plasma proteaseLC-MS/MS.Rats plasmaIn VitroNoneNoneEC50(nM) = 0.48 ± 0.08 
5724
297992052018
HGEGTYTNDVTEYLEEEAAKEFIEWLI-X3-GKPSSGAPPSKKKKKK
4r43FreeFreeLinearLX3 = structure given in paperXenopus GLP-1 analogsAntidiabetes37°C over 72 h1000 ng/mL 38.7Rats plasma proteaseLC-MS/MS.Rats plasmaIn VitroNoneNoneEC50(nM) = 0.61 ± 0.24
5786
295500182018
MSDKPDMAEIEKFDKSKLKKTETQEKNPLPSKETIEQEKQAGESGSMSDKPDMAEIEKFDKSKLKKTETQEKNPLPSKETIEQEKQAGES
DTβ4 88FreeFreeLinearLDimerization using GS linkerDimeric Tβ4Protects post-ischemic cardiac functionN.A.50 μg59.1Mouse serum proteaseHPLCMouse serumIn VivoUniprot id: P62328NoneIn scratch wound and Boyden chamber assays, the migration of HUVECs induced by DTβ4 was significantly higher than that induced by wild-type Tβ4 at each applied concentration 
5787
295500182018
MSDKPDMAEIEKFDKSKLKKTETQEKNPLPSKETIEQEKQAGES
Tβ443FreeFreeLinearLNoneSyntheticProtects post-ischemic cardiac functionN.A.50 μg53.3Mouse serum proteaseHPLCMouse serumIn VivoUniprot id: P62328NoneIn scratch wound and Boyden chamber assays, the migration of HUVECs induced by DTβ4 was significantly higher than that induced by wild-type Tβ4 at each applied concentration 
5799
295286342018
HGDGSFSDEMNTILDNCAARDFICWLIQTKITDPSSGAPPPS
GLP-2 analog 842FreeAmidationCyclic (C17-C24 Stapled Using Linker L3)LNoneGLP-2 analoguesEfficacy in Dextran Sodium Sulfate induced Mouse Colitis ModelsPlasma levels of the peptides at various time points (5 min, 30 min, 1 h, 3 h, 7 h, and 24 h)10 nmol/kg2.7Mice plasma proteaseIn vitro cell based activity assayMice plasmaIn VivoNoneNoneEC50(nM) = 0.068 ± 0.003
5800
295286342018
HGDGSFSDCMNTILDCLAARDFINWLIQTKITDPSSGAPPPS
GLP-2 analog 942FreeAmidationCyclic (C9-C16 Stapled Using Linker L3)LNoneGLP-2 analoguesEfficacy in Dextran Sodium Sulfate induced Mouse Colitis ModelsPlasma levels of the peptides at various time points (5 min, 30 min, 1 h, 3 h, 7 h, and 24 h)10 nmol/kg3.1Mice plasma proteaseIn vitro cell based activity assayMice plasmaIn VivoNoneNoneEC50(nM) = 0.041 ± 0.005
5801
295286342018
HGDGSFSDEMCTILDNLCARDFINWLIQTKITDPSSGAPPPS
GLP-2 analog 1042FreeAmidationCyclic (C11-C18 Stapled Using Linker L3)LNoneGLP-2 analoguesEfficacy in Dextran Sodium Sulfate induced Mouse Colitis ModelsPlasma levels of the peptides at various time points (5 min, 30 min, 1 h, 3 h, 7 h, and 24 h)10 nmol/kg4.7Mice plasma proteaseIn vitro cell based activity assayMice plasmaIn VivoNoneNoneEC50(nM) = 0.028 ± 0.002
5836
294368352018
(hpcdypewqwlcelGk)3
PIE 12-trimer48Maleimide joined by linker PEG24FreeLinearMixAll D-amino acids except GlySyntheticAntiviral (HIV Entry Inhibitor)5 min to 24 h1 mg/kg0.6Rats plasma proteaseLC-MS/MS using an Agilent HPLCRats plasmaIn VivoNoneNoneJRFL(nM) = 2.1 ± 0.28 (antiviral potency)
5837
294368352018
(hpcdypewqwlcelGk)3
PIE 12-trimer48Maleimide joined by linker PEG24FreeLinearMixAll D-amino acids except GlySyntheticAntiviral (HIV Entry Inhibitor)15 min to 48 h1 mg/kg0.8Rats plasma proteaseLC-MS/MS using an Agilent HPLCRats plasmaIn VivoNoneNoneJRFL(nM) = 2.1 ± 0.28 (antiviral potency)
5838
294368352018
(hpcdypewqwlcelGk)3
Palm-PIE12-trimer48Palm-Maleimide joined by linker PEG24FreeLinearMixAll D-amino acids except GlySyntheticAntiviral (HIV Entry Inhibitor)5 min to 24 h1.2 mg/kg1.8Rats plasma proteaseLC-MS/MS using an Agilent HPLCRats plasmaIn VivoNoneNoneJRFL(nM) = 0.54 ± 0.029 (antiviral potency)
5839
294368352018
(hpcdypewqwlcelGk)3
Palm-PIE12-trimer48Palm-Maleimide joined by linker PEG24FreeLinearMixAll D-amino acids except GlySyntheticAntiviral (HIV Entry Inhibitor)15 min to 48 h1.2 mg/kg2.2Rats plasma proteaseLC-MS/MS using an Agilent HPLCRats plasmaIn VivoNoneNoneJRFL(nM) = 0.54 ± 0.029 (antiviral potency)
5840
294368352018
(hpcdypewqwlcelGk)3
C16-PIE12-trimer48C16-Maleimide joined by linker PEG24FreeLinearMixAll D-amino acids except GlySyntheticAntiviral (HIV Entry Inhibitor)5 min to 24 h1 mg/kg0.9Rats plasma proteaseLC-MS/MS using an Agilent HPLCRats plasmaIn VivoNoneNoneJRFL(nM) = 0.11 ± 0.012 (antiviral potency)
5841
294368352018
(hpcdypewqwlcelGk)3
C16-PIE12-trimer48C16-Maleimide joined by linker PEG24FreeLinearMixAll D-amino acids except GlySyntheticAntiviral (HIV Entry Inhibitor)15 min to 48 h1 mg/kg1.2Rats plasma proteaseLC-MS/MS using an Agilent HPLCRats plasmaIn VivoNoneNoneJRFL(nM) = 0.11 ± 0.012 (antiviral potency)
5842
294368352018
(hpcdypewqwlcelGk)3
C18-PIE12-trimer48C18-Maleimide joined by linker PEG24FreeLinearMixAll D-amino acids except GlySyntheticAntiviral (HIV Entry Inhibitor)5 min to 24 h1 mg/kg1.1Rats plasma proteaseLC-MS/MS using an Agilent HPLCRats plasmaIn VivoNoneNoneJRFL(nM) = 0.087 ± 0.012(antiviral potency)
5843
294368352018
(hpcdypewqwlcelGk)3
C18-PIE12-trimer48C18-Maleimide joined by linker PEG24FreeLinearMixAll D-amino acids except GlySyntheticAntiviral (HIV Entry Inhibitor)15 min to 48 h1 mg/kg1.4Rats plasma proteaseLC-MS/MS using an Agilent HPLCRats plasmaIn VivoNoneNoneJRFL(nM) = 0.087 ± 0.012(antiviral potency)
5844
294368352018
(hpcdypewqwlcelGk)3
Chol-PIE12-trimer 48Chol-Maleimide joined by linker PEG24FreeLinearMixAll D-amino acids except GlySyntheticAntiviral (HIV Entry Inhibitor)5 min to 24 h1 mg/kg1.8Rats plasma proteaseUHPLC coupled with Quadrupole Time-of-Flight (Q-TOF) Mass SpectrometryRats plasmaIn VivoNoneNoneJRFL(nM) = 0.022 ± 0.0018 (antiviral potency)
5845
294368352018
(hpcdypewqwlcelGk)3
Chol-PIE12-trimer 48Chol-Maleimide joined by linker PEG24FreeLinearMixAll D-amino acids except GlySyntheticAntiviral (HIV Entry Inhibitor)15 min to 48 h1 mg/kg2.7Rats plasma proteaseUHPLC coupled with Quadrupole Time-of-Flight (Q-TOF) Mass SpectrometryRats plasmaIn VivoNoneNoneJRFL(nM) = 0.022 ± 0.0018 (antiviral potency)
5846
294368352018
(hpcdypewqwlcelGk)3
Chol-PIE12-trimer48Chol-Maleimide joined by linker PEG24FreeLinearMixAll D-amino acids except GlySyntheticAntiviral (HIV Entry Inhibitor)5 min to 24 h1 mg/kg1.6Rats plasma proteaseUHPLC coupled with Quadrupole Time-of-Flight (Q-TOF) Mass SpectrometryRats plasmaIn VivoNoneNoneJRFL(nM) = 0.022 ± 0.0018 (antiviral potency)
5847
294368352018
(hpcdypewqwlcelGk)3
Chol-PIE12-trimer48Chol-Maleimide joined by linker PEG24FreeLinearMixAll D-amino acids except GlySyntheticAntiviral (HIV Entry Inhibitor)15 min to 48 h1 mg/kg3.9Rats plasma proteaseUHPLC coupled with Quadrupole Time-of-Flight (Q-TOF) Mass SpectrometryRats plasmaIn VivoNoneNoneJRFL(nM) = 0.022 ± 0.0018 (antiviral potency)
5848
294368352018
(hpcdypewqwlcelGk)3
Chol-PEG5k-PIE12-trimer48Chol-PEG5K-Maleimide joined by linker PEG24FreeLinearMixAll D-amino acids except GlySyntheticAntiviral (HIV Entry Inhibitor)5 min to 24 h1 mg/kg5.6Rats plasma proteaseUHPLCRats plasmaIn VivoNoneNoneJRFL(nM) = 0.030 ± 0.0010 (antiviral potency)
5849
294368352018
(hpcdypewqwlcelGk)3
Chol-PEG5k-PIE12-trimer48Chol-PEG5K-Maleimide joined by linker PEG24FreeLinearMixAll D-amino acids except GlySyntheticAntiviral (HIV Entry Inhibitor)15 min to 48 h1 mg/kg7.2Rats plasma proteaseUHPLCRats plasmaIn VivoNoneNoneJRFL(nM) = 0.030 ± 0.0010 (antiviral potency)
5850
294368352018
(hpcdypewqwlcelGk)3
CPT3148Chol-Maleimide joined by linker PEG31FreeLinearMixAll D-amino acids except GlySyntheticAntiviral (HIV Entry Inhibitor)5 min to 24 h1 mg/kg3.3Rats plasma proteaseUltra-High Performance Liquid Chromatography (UHPLC)Rats plasmaIn VivoNoneNoneJRFL(nM) = 0.015 ± 0.0062 (antiviral potency)
5851
294368352018
(hpcdypewqwlcelGk)3
CPT3148Chol-Maleimide joined by linker PEG31FreeLinearMixAll D-amino acids except GlySyntheticAntiviral (HIV Entry Inhibitor)15 min to 48 h1 mg/kg5.4Rats plasma proteaseUltra-High Performance Liquid Chromatography (UHPLC)Rats plasmaIn VivoNoneNoneJRFL(nM) = 0.015 ± 0.0062 (antiviral potency)
5852
294368352018
(hpcdypewqwlcelGk)3
CPT31 48Chol-Maleimide joined by linker PEG31FreeLinearMixAll D-amino acids except GlySyntheticAntiviral (HIV Entry Inhibitor)One ml blood samples were collected by venipuncture of a femoral vein at 0.083, 0.167, 0.25, 0.5, 1, 2, 4, 8, 16 and 24 h1 mg/kg7.4Male cynomolgus monkeys plasma proteaseLC-MSMale cynomolgus monkeys plasmaIn VivoNoneNoneJRFL(nM) = 0.015 ± 0.0062 (antiviral potency)
5853
294368352018
(hpcdypewqwlcelGk)3
CPT31 48Chol-Maleimide joined by linker PEG31FreeLinearMixAll D-amino acids except GlySyntheticAntiviral (HIV Entry Inhibitor)Plasma samples were collected pre-dose and 0.25, 0.5, 1, 2, 4, 8, 16, 24, 48 and 72 h post-dose3 mg/kg18.8Male cynomolgus monkeys plasma proteaseLC-MSMale cynomolgus monkeys plasmaIn VivoNoneNoneJRFL(nM) = 0.015 ± 0.0062 (antiviral potency)
5873
293911872018
HSEGTFTSDVSSYLEGQAAKEFIAWLVKGGVKALIDEILAA
Peptide 641FreeABD domain from Streptococcal G strain , AmidationLinearLNone[Ser8]-GLP-1 analogsAntidiabetesBlood samples were collected via the jugular vein using a heparinised syringe at 0.083, 0.25, 0.5, 1, 2, 4, 6, 8, 10, 12 and 24 h postdose0.01 mg/kg5.8 ± 0.4Rats plasma proteaseLC-MSRats plasmaIn VivoNoneNoneEC50(nM) = 1.7
5874
293911872018
HSEGTFTSDVSSYLEGQAAKEFIAWLVKGGVKALIDEILAA
Peptide 641FreeABD domain from Streptococcal G strain , AmidationLinearLNone[Ser8]-GLP-1 analogsAntidiabetesBlood samples were collected via the jugular vein using a heparinised syringe at 0.083, 0.25, 0.5, 1, 2, 4, 6, 8, 10, 12 and 24 h postdose0.01 mg/kg5.4 ± 0.3Rats plasma proteaseLC-MSRats plasmaIn VivoNoneNoneEC50(nM) = 1.7
5901
N.A.2018
(GIVEQCCHSICSLYQLENYCN-OH)-(FVEQHLCGDHLVEALYLVCGERGFFYPK)
Example 749FreeB29K(N(Eps)Tetradecanedioyl-4×gGlu), desB30 modificationsCyclic (C7-C12 disulfide bond in A chain)LA and B chain linked with disulfide bond, B3E, desB27, modifications Insulin DerivativeTreatment of HypoglycaemiaBlood sample was collected at 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/kg44Pig plasma proteaseELISAPig plasmaIn VivoNoneUS 201615754342 ALipogenesis 1% HSA (%rel to HI) = 10.5
5902
N.A.2018
(GIVEQCCTSICSLYQLENYCA-OH)-(FVEQHLCGDHLVEALYLVCGERGFFYPK)
Example 849FreeB29K(N(Eps)Tetradecanedioyl-4×gGlu), desB30 modificationsCyclic (C7-C12 disulfide bond in A chain)LA and B chain linked with disulfide bond,A21A, B3E, desB27 modificationsInsulin DerivativeTreatment of HypoglycaemiaBlood sample was collected at 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/kg45Pig plasma proteaseELISAPig plasmaIn VivoNoneUS 201615754342 ALipogenesis 1% HSA (%rel to HI) = 11.8
5903
N.A.2018
(GIVEQCCTSICSLYQLENYCA-OH)-(FVEQHLCGDHLVEALYLVCGERGFFYPK)
Example 849FreeB29K(N(Eps)Tetradecanedioyl-4×gGlu), desB30 modificationsCyclic (C7-C12 disulfide bond in A chain)LA and B chain linked with disulfide bond,A21A, B3E, desB27 modificationsInsulin DerivativeTreatment of HypoglycaemiaBlood sample was collected at 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/kg52Pig plasma proteaseELISAPig plasmaIn VivoNoneUS 201615754342 ALipogenesis 1% HSA (%rel to HI) = 11.8
5904
N.A.2018
(GIVEQCCTSICSLYQLENYCN-OH)-(FVNQHLCGSHLVEALYLVCGERGFFYTDK-OH)
Prior Art analogue 250FreeB29K(N(Eps)Tetradecanedioyl-gGlu-2xOEG), desB30 modificationsCyclic (C7-C12 disulfide bond in A chain)LA and B chain linked with disulfide bond,B28D,modificationsInsulin DerivativeTreatment of HypoglycaemiaBlood sample was collected at 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/kg121Pig plasma proteaseELISAPig plasmaIn VivoNoneUS 201615754342 AN.A.
5905
N.A.2018
(GIVEQCCTSICSLYQLENYCN-OH)-(FVNQHLCGSHLVEALYLVCGERGFFYTDK)
Prior Art analogue 250FreeB29K(N(Eps)Tetradecanedioyl-gGlu-2xOEG), desB30 modificationsCyclic (C7-C12 disulfide bond in A chain)LA and B chain linked with disulfide bond,B28D, modifcationsInsulin DerivativeTreatment of HypoglycaemiaBlood sample was collected at 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/kg159Pig plasma proteaseELISAPig plasmaIn VivoNoneUS 201615754342 AN.A.
5906
N.A.2018
(GIVEQCCTSICSLYQLENYCA-OH)-(FVEQHLCGDHLVEALYLVCGERGFFYPK)
Example 849FreeB29K(N(Eps)Tetradecanedioyl-4×gGlu), desB30 modificationsCyclic (C7-C12 disulfide bond in A chain)LA and B chain linked with disulfide bond,A21A, B3E, desB27,modificationsInsulin DerivativeTreatment of HypoglycaemiaPlasma was collected at the time points 0, 3,7,15,30,60,120,180 minutes after dosing25 nmol/kg29SD rats plasma proteaseELISASD rats plasma with zinc ionIn VivoNoneUS 201615754342 ALipogenesis 1% HSA (%rel to HI) = 11.8
5907
N.A.2018
(GIVEQCCHSICSLYQLENYCA-OH)-(FVEQHLCGSHLVEALYLVCGERGFFYPK)
Example 549FreeB29K(N(Eps)Tetradecanedioyl-gGlu-2×OEG), desB30 modificationsCyclic (C7-C12 disulfide bond in A chain)LA and B chain linked with disulfide bond,A21A, B3E, desB27, modifcationsInsulin DerivativeTreatment of HypoglycaemiaPlasma was collected at the time points 0, 3,7,15,30,60,120,180 minutes after dosing25 nmol/kg35SD rats plasma proteaseELISASD rats plasma with zinc ionIn VivoNoneUS 201615754342 ALipogenesis 1% HSA (%rel to HI) = 7.6
5908
N.A.2018
(GIVEQCCTSICSLYQLENYCA-OH)-(FVQQHLCGSHLVEALYLVCGERGFFYPK)
Example 949FreeB29K(N(Eps)Tetradecanedioyl-4×gGlu), desB30 modificationsCyclic (C7-C12 disulfide bond in A chain)LA and B chain linked with disulfide bond, A21A, B3Q, desB27, modificationsInsulin DerivativeTreatment of HypoglycaemiaPlasma was collected at the time points 0, 3,7,15,30,60,120,180 minutes after dosing25 nmol/kg30SD rats plasma proteaseELISASD rats plasma with zinc ionIn VivoNoneUS 201615754342 ALipogenesis 1% HSA (%rel to HI) = 16.7
5909
N.A.2018
(GIVEQCCHSICSLYQLENYCN-OH)-(FVEQHLCGDHLVEALYLVCGERGFFYPK)
Example 749FreeB29K(N(Eps)Tetradecanedioyl-4×gGlu), desB30 modifications Cyclic (C7-C12 disulfide bond in A chain)LA and B chain linked with disulfide bond, B3E, desB27, modififcationsInsulin DerivativeTreatment of HypoglycaemiaPlasma was collected at the time points 0, 3,7,15,30,60,120,180 minutes after dosing25 nmol/kg30SD rats plasma proteaseELISASD rats plasma with zinc ionIn VivoNoneUS 201615754342 ALipogenesis 1% HSA (%rel to HI) = 10.5
5910
N.A.2018
(GIVEQCCTSICSLYQLENYCN-OH)-(FVEQHLCGDHLVEALYLVCGERGFFYPK)
Example 449FreeB29K(N(Eps)Tetradecanedioyl-gGlu-2×OEG), desB30 modificationsCyclic (C7-C12 disulfide bond in A chain)LA and B chain linked with disulfide bond,B3E, desB27,modificaitonsInsulin DerivativeTreatment of HypoglycaemiaPlasma was collected at the time points 0, 3,7,15,30,60,120,180 minutes after dosing25 nmol/kg31SD rats plasma proteaseELISASD rats plasma with zinc ionIn VivoNoneUS 201615754342 ALipogenesis 1% HSA (%rel to HI) = 9.3
5911
N.A.2018
(GIVEQCCTSICSLYQLENYCN-OH)-(FVNQHLCGSHLVEALYLVCGERGFFYTDK)
Prior Art analogue 250FreeB29K(N(Eps)Tetradecanedioyl-gGlu-2xOEG), desB30 modificationsCyclic (C7-C12 disulfide bond in A chain)LA and B chain linked with disulfide bond,B28D, modifcationsInsulin DerivativeTreatment of HypoglycaemiaPlasma was collected at the time points 0, 3,7,15,30,60,120,180 minutes after dosing25 nmol/kg45SD rats plasma proteaseELISASD rats plasma with 3 Zinc Ion Per HexamerIn VivoNoneUS 201615754342 AN.A.
5912
N.A.2018
(GIVEQCCTSICSLYQLENYCN-OH)-(FVNQHLCGSHLVEALYLVCGERGFFYTPK)
Prior Art analogue 350FreeB29K(N(Eps)Tetradecanedioyl), desB30 modificationsCyclic (C7-C12 disulfide bond in A chain)LA and B chain linked with disulfide bond, modificationsInsulin DerivativeTreatment of HypoglycaemiaPlasma was collected at the time points 0, 3,7,15,30,60,120,180 minutes after dosing25 nmol/kg50SD rats plasma proteaseELISASD rats plasma with 3 Zinc Ion Per HexamerIn VivoNoneUS 201615754342 AN.A.
5913
N.A.2018
(GIVEQCCTSICSLYQLENYCA-OH)-(FVEQHLCGSHLVEALYLVCGERGFFYPK)
Example 1549FreeB29K(N(Eps)Hexadecanedioyl-gGlu-2×OEG), desB30 modificationscyclic (C7-C12 disulfide bond in A chain)LA and B chain linked with disulfide bond,A21A, B3E, desB27, modificaitonsInsulin DerivativeTreatment Of HypoglycaemiaPlasma was collected at the time points 0, 3,7,15,30,60,120,180 minutes after dosing25 nmol/kg67SD rats plasma proteaseELISASD rats plasma with Zinc IonIn VivoNoneUS 201615754342 ALipogenesis 1% HSA (%rel to HI) = 1.8
5914
N.A.2018
(GIVEQCCTSICSLYQLENYCA-OH)-(FVQQHLCGSHLVEALYLVCGERGFFYPK)
Example 2349FreeB29K(N(Eps)Hexadecanedioyl-4×gGlu), desB30 modificationscyclic (C7-C12 disulfide bond in A chain)LA and B chain linked with disulfide bond,A21A, B3Q, desB27, modificationsInsulin DerivativeTreatment Of HypoglycaemiaPlasma was collected at the time points 0, 3,7,15,30,60,120,180 minutes after dosing25 nmol/kg55SD rats plasma proteaseELISASD rats plasma with Zinc IonIn VivoNoneUS 201615754342 ALipogenesis 1% HSA (%rel to HI) = 1.54
5915
N.A.2018
(GIVEQCCTSICSLYQLENYCN-OH)-(FVNQHLCGSHLVEALYLVCGERGFFYTPK)
Prior Art analogue 750FreeB29K(N(Eps)Hexadecanedioyl-gGlu), desB30 modificationscyclic (C7-C12 disulfide bond in A chain)LA and B chain linked with disulfide bond,modificationsInsulin DerivativeTreatment Of HypoglycaemiaPlasma was collected at the time points 0, 3,7,15,30,60,120,180 minutes after dosing25 nmol/kg200SD rats plasma proteaseELISASD rats plasma with 3 Zinc Ion Per HexamerIn VivoNoneUS 201615754342 AN.A.
5925
294640072018
((99mTc-HHEDEG-DEG-QWECPYGLCWIQ)-PEG2000)4
99mTc-F4A72FreeFreeCyclic (PEG2000 Linkage)LTetramerization using PEG2000Fibrin-specific natural peptide analogue99mTc-F4A is a high-avidity prototype probe for characterizing thrombus in LVADsserial blood samples were obtained at 0, 2, 5, 10, 15, 20, 30, 60, 120, and 180 min via an indwelling jugular catheterN.A.5.0 ± 1.9 (T1/2A Distribution Half Life)Mice plasma proteaseRadioactivity assayMice plasmaIn VivoNoneNoneN.A.
5949
288998382017
VQQRKESKKPPAKLQPRCFGLKLDRIGSMSGLGCVQQRKESKKPPAKLQPR
Ghrelin(12-28)CNP(6-22)ghrelin(12-28)51FreeGhrelin(12-28)Cyclic (C18-C34 Disulfide Bond)LNoneNatriuretic peptide derivativesTreatment of Growth Failure and Short Stature Disorders such as AchondroplasiaN.A.15 nmol/kg18.40 ± 2.05Rats plasma proteaseRIARats plasmaIn VivoNoneNoneAgonist activity of ghrelin(12-28)CNP(6-22)ghrelin(12-28) was also the lowest
5950
288998382017
RPQLKAPPKKSEKRQQVCFGLKLDRIGSMSGLGCVQQRKESKKPPAKLQPR
Ghrelin(28-12)CNP(6-22)ghrelin(12-28) 51Reversed sequence ghrelin(28-12) fused to the N-terminal side of CNP(6-22)FreeCyclic (C18-C34 Disulfide Bond)LNoneNatriuretic peptide derivativesTreatment of Growth Failure and Short Stature Disorders such as AchondroplasiaN.A.16 nmol/kg17.38 ± 1.00Rats plasma proteaseRIARats plasmaIn VivoNoneNoneGhrelin(28-12)CNP(6-22)ghrelin(12-28) exhibited lower potency than that of ghrelin(28-12)CNP(6-22) and CNP(6-22)ghrelin(12-28)
6017
284640432017
GTSLSPPPESSGSPQQPGLSAPHSRQIPAPQGAVLVQREKDLPNYNWNSFGLRF
KP-5454FreeAmidationLinearLNonekisspeptin analogueTreatment of Specific Human Reproductive Disorders100 μl of blood was collected from the lateral tail vein from groups of mice (n = 4) for each time point (0, 1min, 2 min, 5 min, 10 min, 30 min, 60 min and 120 min)1 nmol32Mouse plasma proteaseRIAMouse plasmaIn Vivohttps://www.jbc.org/article/S0021-9258(19)77047-1/fulltextNoneN.A.
6019
284578952017
HGEGTFTSDLSKQMEEEAVRLFIEWLKQGGPSSGAPPPSGSEGSEGEGGSEGSEGEGHAHFNFGSWTWENGKWTWKGIWLPAR
Exenatide-APTHSA83FreeC-terminal part of exenatide was connected to the N-terminal part of APTHSA using a long (18-mer) linkerLinearLNoneExendin-4 analogsAntihyperglycemic1 hour25 nmol/kg~1.3ICR mice retro-orbital sinus proteaseExenatide ELISAICR mice retro-orbital sinusIn VivoPDB id: 7MLLNoneboth exenatide and exenatide-APTHSA groups at an equal dose effectively cleared glucose from the bloodstream, showing similar anti-hyperglycemic activity
6142
271157552016
MKWVTFISLLFLFSSAYSRGVFRRHHHHHH-IEGPTLRQWLAARAGGGGSIEGPTLRQWLAARA
HSA-dTMP63HSA joined using a linkerFreeLinearLNoneFusion protein of dTMP and HSATreatment of ThrombocytopeniaSerum was sampled from mice eyes at 5 min, 30 min, 1 h,1.5 h, 2 h, 4 h, 12 h, 24 h, and 48 h after dosing300 μg/kg17.1Mice serum proteaseImmunoenzymetric assayMice serumIn VivoNoneNoneboth HSA-dTMP and dTMP-HSA could significantly increase peripheral platelet counts in a dose-dependent manner in normal mice
6143
271157552016
IEGPTLRQWLAARA-GGGGS-IEGPTLRQWLAARA-MKWVTFISLLFLFSSAYSRGVFRRHHHHHH
dTMP-HSA63FreeHSA joined using a linkerLinearLNoneFusion protein of dTMP and HSATreatment of ThrombocytopeniaSerum was sampled from mice eyes at 5 min, 30 min, 1 h,1.5 h, 2 h, 4 h, 12 h, 24 h, and 48 h after dosing300 μg/kg16.1Mice serum proteaseImmunoenzymetric assayMice serumIn VivoNoneNoneboth HSA-dTMP and dTMP-HSA could significantly increase peripheral platelet counts in a dose-dependent manner in normal mice
6196
289898132016
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPSLPET
54.6 kDa EG943FreeAEBMP: N-(2-(2-(2-(2-aminoacetamido)acet-amido)acetamido) ethyl)-2-bromo-2-methylpropanamide, OEGMA(54.6KDa)LinearLFluorescently labeled with Alexa FluorExendin-4 analogsAntidiabetes10 μL of blood samples were collected from the tail vein into 100 μL of a heparin solution (1kU/ml in PBS, Sigma Aldrich) at 40 s, 40 min, 2.5 h, 4.5 h, 8 h, 24 h, 48 h, 72 h, 96 h and 120 h after injection75 nmol/kg42.4 ± 2.9 (T1/2 Elimination Half Life)Mice plasma proteaseFluorescence assayMice plasmaIn VivoNoneNoneEC50(nM) = 1.91 ± 0.35
6197
289898132016
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPSLPET
55.6 kDa EG343FreeAEBMP: N-(2-(2-(2-(2-aminoacetamido)acet-amido)acetamido) ethyl)-2-bromo-2-methylpropanamide, OEGMA(55.6KDa)LinearLFluorescently labeled with Alexa FluorExendin-4 analogsAntidiabetes10 μL of blood samples were collected from the tail vein into 100 μL of a heparin solution (1kU/ml in PBS, Sigma Aldrich) at 40 s, 40 min, 2.5 h, 4.5 h, 8 h, 24 h, 48 h, 72 h, 96 h and 120 h after injection75 nmol/kg61.2 ± 5.0 (T1/2 Elimination Half Life)Mice plasma proteaseFluorescence assayMice plasmaIn VivoNoneNoneEC50(nM) = 4.17 ± 0.13
6198
289898132016
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPSLPET
71.6 kDa EG343FreeAEBMP: N-(2-(2-(2-(2-aminoacetamido)acet-amido)acetamido) ethyl)-2-bromo-2-methylpropanamide, OEGMA(71.6KDa)LinearLFluorescently labeled with Alexa FluorExendin-4 analogsAntidiabetes10 μL of blood samples were collected from the tail vein into 100 μL of a heparin solution (1kU/ml in PBS, Sigma Aldrich) at 40 s, 40 min, 2.5 h, 4.5 h, 8 h, 24 h, 48 h, 72 h, 96 h and 120 h after injection75 nmol/kg61.5 ± 3.2 (T1/2 Elimination Half Life)Mice plasma proteaseFluorescence assayMice plasmaIn VivoNoneNoneEC50(nM) = 5.11 ± 0.23
6284
138-792-131-275-4112017
MAERAALEELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQLGPDESKQKFVLKTPKHHHHHH
HRS (1-60)67FreeFreeLinearLNoneSyntheticTherapeutic1.5 hr8 mg/kg0.5NAELISAmicein vivohttps://lens.org/138-792-131-275-411US 9587235 B2NA
6287
138-792-131-275-4112017
MAERAALEELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQLGPDESKQKFVLKTPKHHHHHH
HRS (1-60)67FreeFreeLinearLNoneSyntheticTherapeutic1.5 hr8 mg/kg0.7NAELISAmicein vivohttps://lens.org/138-792-131-275-411US 9587235 B2NA
6290
159-909-893-044-9682017
K(mod)GCRFGTCTVQKLAHQIYQFTDKDKDNVAPRSKISPQGY
adrenomedullin44lipidfreeLinearDNonehuman adrenomedullin peptideagonisticNANA1.5NAELISASHR ratin vivohttps://lens.org/159-909-893-044-968US 9694051 B2NA
6294
034-343-155-162-3022017
MKIILWLCVFGLFLATLFPISWQMPVESGLSSEDSASSESFASKIKRHGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPSG
Ex487FreeFreeLinearLNoneNANANANA38chymotrypsinELISANAin vitrohttps://lens.org/034-343-155-162-302US 9695224 B2NA
6298
034-343-155-162-3022017
MKIILWLCVFGLFLATLFPISWQMPVESGLSSEDSASSESFASKIKRHGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPSG
exenatide87FreeFreeLinearLNoneNANANANA13pepsinELISANAin vitrohttps://lens.org/034-343-155-162-302US 9695224 B2NA