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IDPMIDYEARSequenceNameLengthN-ter MODC-ter MODLinear/CyclicChiralityChem-MODOriginNatureIncubation TimeConcentrationHalf LifeUnits Half LifeProteaseAssayTest SampleVivo/VitroReferencePatent No.Activity
1183
105412991999
APPRLICDSRVLERYLLEAKEAENITTGCAEHCSLNENITVPDTKVNFYAWKRMEVGQQAVEVWQGLALLSEAVLRGQALLVNSSQPWEPLQLHVDKAVSGLRSLTTLLRALGAQKEAISPPDAASAAPLRTITADTFRKLFRVYSNFLRGKLKLYTGEACRTGDR
Epoetin166FreeFreeCyclicLThree N-linked carbohydrate chainsRecombinant human erythropoietinStimulates erythropoiesisNot mentionedNot mentioned8.5 ±2.4Human blood proteasesELISASubcutaneously injected into patients with end-stage renal failurein vivohttp://www.drugbank.ca/drugs/DB00016NoneNot reported
1184
105412991999
APPRLICDSRVLERYLLEAKEAENITTGCAEHCSLNENITVPDTKVNFYAWKRMEVGQQAVEVWQGLALLSEAVLRGQALLVNSSQPWEPLQLHVDKAVSGLRSLTTLLRALGAQKEAISPPDAASAAPLRTITADTFRKLFRVYSNFLRGKLKLYTGEACRTGDR
Novel erythropoiesis stimulating protein (NESP)166FreeFreeCyclicLFive N-linked carbohydrate chainsHyperglycosylated analogue of recombinant human erythropoietinStimulates erythropoiesisNot mentionedNot mentioned25.3 ±2.2Human blood proteasesELISASubcutaneously injected into patients with end-stage renal failurein vivohttp://www.drugbank.ca/drugs/DB00017NoneNot reported
1201
204189552010
HSQGTFTSDYSKYLDSRRAQDFVQWLMNTGGEGSGEGSEGEGSEGSGEGEGSEGSGEGEGGSEGSEGEGGSEGSEGEGGSEGSEGEGSGEGSEGEGGSEGSEGEGSGEGSEGEGSEGGSEGEGGSEGSEGEGSGEGSEGEGGEGGSEGEGSEGSGEGEGSGEGSEGEGSEGSGEGEGSGEGSEGEGSEGSGEGEGSEGSGEGEGGSEGSEGEGSEGSGEGEGGEGSGEGEGSGEGSEGEGGGEGSEGEGSGEGGEGEGSEGGSEGEGGSEGGEGEGSEGSGEGEGSEGGSEGEGSEGGSEGEGSEGSGEGEGSEGSGEG
Gcg-XTEN 288319FreeXTENLinearLNoneGlucagon derivativeRegulate blood glucoseNot mentioned12 nmol/kg9Cynomolgus monkey plasma proteasesSandwich ELISAInjected subcutaneouly into cynomolgus monkeysin vivoNoneNoneElevated blood glucose levels for 10 €“12 hours
1202
204189552010
HSQGTFTSDYSKYLDSRRAQDFVQWLMNTGGEGGSEGSEGEGSEGSGEGEGGSEGSEGEGSEGSGEGEGGSEGSEGEGGSEGSEGEGGEGSGEGEGSEGSGEGEGSGEGSEGEGGSEGGEGEGSEGGSEGEGSEGGSEGEGGEGSGEGEGGGEGSEGEGSEGSGEGEGSGEGSEG
Gcg-XTEN 144175FreeXTENLinearLNoneGlucagon derivativeRegulate blood glucoseNot mentioned12 nmol/kg8 to 10Cynomolgus monkey plasma proteasesSandwich ELISAInjected subcutaneouly into cynomolgus monkeysin vivoNoneNoneNot reported
1962
184818522008
((POG)5 (PQGPGGPPG) (POG)5)3
3A117AcetylationAmidationLinearLNoneSynthetic Collagen peptideStructural component of connective tissuesNot reportedNot mentioned580Not mentionedHPLC and MALDI-TOFNot reportedin vitroNoneNoneNot available
1963
184818522008
((POG)5 (PQGPGSPPG) (POG)5)3
3A'117AcetylationAmidationLinearLNoneSynthetic Collagen peptideStructural component of connective tissuesNot reportedNot mentioned910Not mentionedHPLC and MALDI-TOFNot reportedin vitroNoneNoneNot available
1964
184818522008
((POG)5 (PVGAAGATG) (POG)5)3
3B117AcetylationAmidationLinearLNoneSynthetic Collagen peptideStructural component of connective tissuesNot reportedNot mentioned345Not mentionedHPLC and MALDI-TOFNot reportedin vitroNoneNoneNot available
1965
184818522008
((POG)5 (PVGAASATG) (POG)5)3
3B'117AcetylationAmidationLinearLNoneSynthetic Collagen peptideStructural component of connective tissuesNot reportedNot mentioned655Not mentionedHPLC and MALDI-TOFNot reportedin vitroNoneNoneNot available
1966
184818522008
(POG)5 (PQGPGGPPG) (POG)5 (PKG)5 (PQGPGGPPG) (PKG)5 (DOG)5 (PVGAAGATG) (DOG)5
A.A.B117AcetylationAmidationLinearLNoneSynthetic Collagen peptideStructural component of connective tissuesNot reportedNot mentioned190Not mentionedHPLC and MALDI-TOFNot reportedin vitroNoneNoneNot available
1967
184818522008
(POG)5 (PQGPGGPPG) (POG)5 (PKG)5 (PQGPGGPPG) (PKG)5 (DOG)5 (PVGAAGATG) (DOG)6
A.A.B'117AcetylationAmidationLinearLNoneSynthetic Collagen peptideStructural component of connective tissuesNot reportedNot mentioned300Not mentionedHPLC and MALDI-TOFNot reportedin vitroNoneNoneNot available
1968
184818522008
(POG)5 (PQGPGSPPG) (POG)5 (PKG)5 (PQGPGSPPG) (PKG)5 (PKG)5 (PQGPGSPPG) (PKG)5
A'.A'.B117AcetylationAmidationLinearLNoneSynthetic Collagen peptideStructural component of connective tissuesNot reportedNot mentioned325Not mentionedHPLC and MALDI-TOFNot reportedin vitroNoneNoneNot available
1969
184818522008
(POG)5 (PQGPGSPPG) (POG)5 (PKG)5 (PQGPGSPPG) (PKG)5 (POG)5 (PVGAASATG) (POG)5
A'.A'.B'117AcetylationAmidationLinearLNoneSynthetic Collagen peptideStructural component of connective tissuesNot reportedNot mentioned470Not mentionedHPLC and MALDI-TOFNot reportedin vitroNoneNoneNot available
2001
119627212001
DIRCKDDEFTHLYTLIVRPDNTYEVKIDNSQVESGSLEDDWDFLPPKKIKDPDAAKPEDWDERAKIDDPTDSKPEDWDKPEHIPDPDAKKPEDWDEEMDGEWEPPVIQNPEYKGEWKPRQIDNP
CTR-S domain124FreeFreeLinearLNoneCTR (Calreticulin)It binds to C1q, prevents the formation of C1 and so inhibits activation of the classical pathwayNot reportedNot mentioned1.21 ± 0.34 in distribution phaseSerine ProteasesRadioactivity measured with a gamma counterRat plasmain vivoNoneNoneBiological activity =2 m Ci/nmol
2002
119627212001
DIRCKDDEFTHLYTLIVRPDNTYEVKIDNSQVESGSLEDDWDFLPPKKIKDPDAAKPEDWDERAKIDDPTDSKPEDWDKPEHIPDPDAKKPEDWDEEMDGEWEPPVIQNPEYKGEWKPRQIDNP
CTR-S domain124FreeFreeLinearLNoneCTR (Calreticulin)It binds to C1q, prevents the formation of C1 and so inhibits activation of the classical pathwayNot reportedNot mentioned40.5 ± 2.7 in elimination phaseSerine ProteasesRadioactivity measured with a gamma counterRat plasmain vivoNoneNoneBiological activity =2 m Ci/nmol
2216
153693942004
CDLPQTHSLGSRRTLMLLAQMRKISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE
PEG40-FMS-IFNα2146Pegylation [40kdaPEG linked to INFα2 via 2-sulfo-9-fluorenylmethoxycarbonyl (FMS)]FreeCyclic(C1-C98, C29-138)LNoneIFNα2 derivativeAntiviral and antiproliferative0-150 hours10 µg65 (t1/2 of rate of regeneration of native interferon)Rat blood proteasesBIAcore binding assayIntravenously administered to wistar ratsin vivohttp://www.drugbank.ca/drugs/DB00105NoneFollowing subcutaneous administration to rats and monitoring circulating antiviral activity, active IFNα2 levels peaked at 50 h, with substantial levels still being detected 200 h after administration.
2217
153693942004
CDLPQTHSLGSRRTLMLLAQMRKISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE
Interferon α2 (IFNα2)146FreeFreeCyclic(C1-C98, C29-138)LGlycosylation at Thr-105IFNα2Antiviral and antiproliferative0-25 hours10 μg/rat in 0.2 mL of PBS~1Rat blood proteasesBIAcore binding assayIntravenously administered to wistar ratsin vivohttp://www.uniprot.org/uniprot/P01563NoneFollowing administration of IFNα2 (100 μg/rat), the circulating antiviral activity declined with a t1/2 value of ˆ¼1 h, reaching a level lower than 20 pM IFNα2, 12 h after administration.
3040
14906681992
FPTIPLSRLFDNAMLRAHRLHQLAFDTYQEFEEAYIPKEQKYSFLQNPQTSLCFSESIPTPSNREETQQKSNLELLRISLLLIQSWLEPVQFLRSVFANSLVYGASDSNVYDLLKDLEEGIQTLMGRLEDGSPRTGQIFKQTYSKFDTNSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF
rhGH(Recombinant DNA derived human growth hormone)191FreeFreeLinearLNoneRecombinant DNA derived human growth hormonePromotes growth and developmentNot mentioned4 IU rhGH/m2 BSA18Proteases from Human serumRadioimmunoassay(Intravenous route of injection) human serumin vivoNoneNoneIn a GH-deficient child, hGH serum levels between 10 and 20 ng/ml were demonstrated for a period of 8 h after s.c. administration of 0.07 IU rhGH/kg body weight.
3041
14906681992
FPTIPLSRLFDNAMLRAHRLHQLAFDTYQEFEEAYIPKEQKYSFLQNPQTSLCFSESIPTPSNREETQQKSNLELLRISLLLIQSWLEPVQFLRSVFANSLVYGASDSNVYDLLKDLEEGIQTLMGRLEDGSPRTGQIFKQTYSKFDTNSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF
rhGH(Recombinant DNA derived human growth hormone)191FreeFreeLinearLNoneRecombinant DNA derived human growth hormonePromotes growth and developmentNot mentioned4 IU rhGH/m2 BSA2.59 ±1.32Proteases from Human serumRadioimmunoassay(Subcutaneous route of injection) human serumin vivoNoneNoneIn a GH-deficient child, hGH serum levels between 10 and 20 ng/ml were demonstrated for a period of 8 h after s.c. administration of 0.07 IU rhGH/kg body weight.
3042
14906681992
FPTIPLSRLFDNAMLRAHRLHQLAFDTYQEFEEAYIPKEQKYSFLQNPQTSLCFSESIPTPSNREETQQKSNLELLRISLLLIQSWLEPVQFLRSVFANSLVYGASDSNVYDLLKDLEEGIQTLMGRLEDGSPRTGQIFKQTYSKFDTNSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF
rhGH(Recombinant DNA derived human growth hormone)191FreeFreeLinearLNoneRecombinant DNA derived human growth hormonePromotes growth and developmentNot mentioned10 IU rhGH/m2 BSA4.29 ±1.89Proteases from Human serumRadioimmunoassay(Subcutaneous route of injection) human serumin vivoNoneNoneIn a GH-deficient child, hGH serum levels between 10 and 20 ng/ml were demonstrated for a period of 8 h after s.c. administration of 0.07 IU rhGH/kg body weight.
3043
14906681992
FPTIPLSRLFDNAMLRAHRLHQLAFDTYQEFEEAYIPKEQKYSFLQNPQTSLCFSESIPTPSNREETQQKSNLELLRISLLLIQSWLEPVQFLRSVFANSLVYGASDSNVYDLLKDLEEGIQTLMGRLEDGSPRTGQIFKQTYSKFDTNSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF
rhGH(Recombinant DNA derived human growth hormone)191FreeFreeLinearLNoneRecombinant DNA derived human growth hormonePromotes growth and developmentNot mentioned4 IU rhGH/m2 BSA6.06 ±2.64Proteases from Human serumRadioimmunoassay(Intramuscular route of injection)human serumin vivoNoneNoneIn a GH-deficient child, hGH serum levels between 10 and 20 ng/ml were demonstrated for a period of 8 h after s.c. administration of 0.07 IU rhGH/kg body weight.
3046
79948071994
ANTFLEEVRKGNLERECVEETCSYEEAFEALESSTATDVFWAKYTACETARTPRDKLAACLEGNCAEGLGTNYRGHVNITRSGIECQLWRSRYPHKPEINSTTHPGADLQENFCRNPDSSTTGPWCYTTDPTVRRQECSIPVCGQDQVTVAMTPRSEGSSVNLSPPLEQCVPDRGQQYQGRLAVTTHGLPCLAWASAQAKALSKHQDFNSAVQLVENFCRNPDGDEEGVWCYVAGKPGDFGYCDLNYCEEAVEEETGDGLDEDSDRAIEGRTA
Prothrombin fragment 1.2273FreeFreeLinearLNoneProthrombinNot mentionedNot reportedNot reported90Human blood proteases in presence of Hirudin (anti-coagulant)Radioimmunoassay ,ELISAHuman blood plasma samplein vivo3759958, 2824564NoneNot mentioned
3169
77878271994
SSSHPIFHRGEFSVCDSVSVWVGDKTTATDIKGKEVMVLGEVNINNSVFKQYFFETKCRDPNPVDSGCRGIDSKHWNSYCTTTHTFVKALTMDGKQAAWRFIRIDTACVCVLSRKAVRRA
125I-β-NGF120FreeFreeCyclic (3 disulphide bonds between C15-C80, C58-C108, C68-C110)LNoneβ-nerve growth factorNerve growth promoting peptideBlood samples (250 µl) were obtained from the catheterized carotid artery 15, 30, 45 and 60 min afte800 000 cpm of 125I-7S-NGF or 125I-β-NGF (diluted in 200 µl of saline)36.3 + 2.20Rats blood proteasesColumn chromatographyIntravenouly injected in adult male Wistar ratsin vivohttp://www.drugbank.ca/drugs/DB00188NoneNot reported
3208
83532801993
ASISGRDTHRLTRTLNCSSIVKEIIGKLPEPELKTDDEGPSLRNKSFRRVNLSKFVESQGEVDPEDRYVIKSNLQKLNCCLPTSANDSALPGVFIRDLDDFRKKLRFYMVHLNDLETVLTSRPPQPASGSVSPNRGTVEC
Interleukin-3 (IL-3)140FreeFreeCyclic (C17-C80,C79-C140)LGlycosylation at 84thand 112th positionIL3 is produced by activated T lymphocytes, activated mast cells, and eosinophils and neutrophilsHematopoietic growth factorNot mentioned1,000 biologic units2.1 (α half life)Balb/c mice blood proteasesELISAInjected intravenously in Balb/c mice bloodin vivohttp://www.uniprot.org/uniprot/P01586NoneMice treated with IL3 had megakaryocyte frequency=0.9 ±0.21 per high-power field while saline control had 1.4 ±0.33 per high-power field
3209
83532801993
ASISGRDTHRLTRTLNCSSIVKEIIGKLPEPELKTDDEGPSLRNKSFRRVNLSKFVESQGEVDPEDRYVIKSNLQKLNCCLPTSANDSALPGVFIRDLDDFRKKLRFYMVHLNDLETVLTSRPPQPASGSVSPNRGTVEC
Interleukin-3 (IL-3)140FreeFreeCyclic (C17-C80,C79-C140)LGlycosylation at 84thand 112th positionIL3 is produced by activated T lymphocytes, activated mast cells, and eosinophils and neutrophilsHematopoietic growth factorNot mentioned1,000 biologic units10.0 (β half life)Balb/c mice blood proteasesELISAInjected intravenously in Balb/c mice bloodin vivohttp://www.uniprot.org/uniprot/P01586NoneMice treated with IL3 had megakaryocyte frequency=0.9 ±0.21 per high-power field while saline control had 1.4 ±0.33 per high-power field
3210
83532801993
ASISGRDTHRLTRTLNCSSIVKEIIGKLPEPELKTDDEGPSLRNKSFRRVNLSKFVESQGEVDPEDRYVIKSNLQKLNCCLPTSANDSALPGVFIRDLDDFRKKLRFYMVHLNDLETVLTSRPPQPASGSVSPNRGTVEC
Interleukin-3 (IL-3)140FreeFreeCyclic (C17-C80,C79-C140)LGlycosylation at 84thand 112th positionIL3 is produced by activated T lymphocytes, activated mast cells, and eosinophils and neutrophilsHematopoietic growth factorNot mentioned1,000 biologic units3.6 (α half-life)Balb/c mice blood proteasesELISAInjected intravenously in Balb/c mice bloodin vivohttp://www.uniprot.org/uniprot/P01586NoneMice treated with IL3 had megakaryocyte frequency=0.9 ±0.21 per high-power field while saline control had 1.4 ±0.33 per high-power field
3211
83532801993
ASISGRDTHRLTRTLNCSSIVKEIIGKLPEPELKTDDEGPSLRNKSFRRVNLSKFVESQGEVDPEDRYVIKSNLQKLNCCLPTSANDSALPGVFIRDLDDFRKKLRFYMVHLNDLETVLTSRPPQPASGSVSPNRGTVEC
Interleukin-3 (IL-3)140FreeFreeCyclic (C17-C80,C79-C140)LGlycosylation at 84thand 112th positionIL3 is produced by activated T lymphocytes, activated mast cells, and eosinophils and neutrophilsHematopoietic growth factorNot mentioned1,000 biologic units30.8 (β half life)Balb/c mice blood proteasesELISAInjected intravenously in Balb/c mice bloodin vivohttp://www.uniprot.org/uniprot/P01586NoneMice treated with IL3 had megakaryocyte frequency=0.9 ±0.21 per high-power field while saline control had 1.4 ±0.33 per high-power field
3212
191153922009
HPAGKRPCKMQAFRIWDTNQKTFYLRNNQLIAGYLQGPNTKLEEKIDMVPIDFRNVFLGIHGGKLCLSCVKSGDDTKLQLEEVNITDLNKNKEEDKRFTFIRSETGPTTSFESLACPGWFLCTTLEADHPVSLTNTPKEPCTVTKFYFQEDQ
Interleukin-1 Receptor Antagonist (IL-1ra)152FreeFreeCyclic(66-116)LGlycosylation at 84th positionInterleukin-1 Receptor AntagonistThe natural specific receptor antagonist (IL-1ra) binds to IL-1RI but does not initiate signaling as it does not engage the IL1R accessory protein and therefore acts as a receptor antagonist.Not mentionedNot mentioned6 to 15Rats blood proteasesNot mentionedRat bloodin vivohttp://www.uniprot.org/uniprot/P25086NoneSignificant depression of LTP in the group of animals that received intracerebroventricular injection of Aβ-peptide (1 €“40) compared with control animals injected with vehicle.
4052
383407262024
IEEQAKTFLDKFNHEAEDLFYQSSLGGSKGDFRGGGGSGGGGSGGGGSGGGGSGGGGSGGGGSGGGGSDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQ
A1L35HR2m114Conjugation of angiotensin-converting enzyme 2 (ACE2)-derived peptide A1 to the N terminus of the viral HR2-derived peptide HR2m through a long flexible linker,FreeLinearLNonefusion protein of A1 and HR2mAntiviral (Inhibits Coronaviruses)Sera were collected from these mice before (0 h) and 2, 4, 8, 12, 24, 48, 72, 120, 168, 240 and 336 h after injection5 mg/kg2.64Balb/c mice serum proteaseN.A.BALB/c mice serumIn VivoNoneNoneA1L35HR2m was highly potent in inhibiting SARS-CoV-2 infection with an IC50 value of 27 nM
4053
383407262024
IEEQAKTFLDKFNHEAEDLFYQSSLGGSKGDFRGGGGSGGGGSGGGGSGGGGSGGGGSGGGGSGGGGSDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQ
A1L35HR2m-Chol114Conjugation of angiotensin-converting enzyme 2 (ACE2)-derived peptide A1 to the N terminus of the viral HR2-derived peptide HR2m through a long flexible linker,Chol conjugation at C terminalLinearLNonefusion protein of A1 and HR2mAntiviral (Inhibits Coronaviruses)Sera were collected from these mice before (0 h) and 2, 4, 8, 12, 24, 48, 72, 120, 168, 240 and 336 h after injection5 mg/kg81.83Balb/c mice serum proteaseN.A.BALB/c mice serumIn VivoNoneNoneA1L35HR2m was highly potent in inhibiting SARS-CoV-2 infection with an IC50 value of 27 nM
4054
383407262024
IEEQAKTFLDKFNHEAEDLFYQSSLGGSKGDFRGGGGSGGGGSGGGGSGGGGSGGGGSGGGGSGGGGSDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQ
A1L35HR2m-Chol114Conjugation of angiotensin-converting enzyme 2 (ACE2)-derived peptide A1 to the N terminus of the viral HR2-derived peptide HR2m through a long flexible linker,Chol conjugation at C terminalLinearLNonefusion protein of A1 and HR2mAntiviral (Inhibits Coronaviruses)N.A.5 mg/kg89.8Balb/c mice serum proteaseN.A.Balb/c mice lung tissue homogenate In VivoNoneNoneA1L35HR2m was highly potent in inhibiting SARS-CoV-2 infection with an IC50 value of 27 nM
4055
383407262024
IEEQAKTFLDKFNHEAEDLFYQSSLGGSKGDFRGGGGSGGGGSGGGGSGGGGSGGGGSGGGGSGGGGSDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQ
A1L35HR2m-Chol114Conjugation of angiotensin-converting enzyme 2 (ACE2)-derived peptide A1 to the N terminus of the viral HR2-derived peptide HR2m through a long flexible linker,Chol conjugation at C terminalLinearLNonefusion protein of A1 and HR2mAntiviral (Inhibits Coronaviruses)N.A.5 mg/kg10.6Balb/c mice serum proteaseN.A.Balb/c mice trachea tissue homogenate In VivoNoneNoneA1L35HR2m was highly potent in inhibiting SARS-CoV-2 infection with an IC50 value of 27 nM
4056
383407262024
IEEQAKTFLDKFNHEAEDLFYQSSLGGSKGDFRGGGGSGGGGSGGGGSGGGGSGGGGSGGGGSGGGGSDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQ
A1L35HR2m-Chol114Conjugation of angiotensin-converting enzyme 2 (ACE2)-derived peptide A1 to the N terminus of the viral HR2-derived peptide HR2m through a long flexible linker,Chol conjugation at C terminalLinearLNonefusion protein of A1 and HR2mAntiviral (Inhibits Coronaviruses)N.A.5 mg/kg49Balb/c mice serum proteaseN.A.Balb/c mice nose tissue homogenate In VivoNoneNoneA1L35HR2m was highly potent in inhibiting SARS-CoV-2 infection with an IC50 value of 27 nM
4058
382935402024
ENLYFQHGEGTFTSDVSSYLEGQAAKEFIAWLVKGRGGGGSGGGGSGGGGSLAEAKVLANRELDKYGVSDYYKNLINNAKTVEGVKALIDEILAALPGGGGSGGGGSGGGGSHSQGTFTSDYSKYLDSRRAQDFVQWLMNTGGEGGSEGSEGEGSEGSGEGEGGSEGSEGEGSEGSGEGEGGSEGSEGEGGSEGSEGEGGEGSGEGEGSEGSGEGEGSGEGSEGEGGSEGGEGEGSEGGSEGEGSEGGSEGEGGEGSGEGEGGGEGSEGEGSEGSGEGEGSGEGSEG
GLP-ABD-XTEN144257GLP-1 molecule was linked to the N-terminus of ABD via a (GGGGS)3 linker (GLP-ABD), His-tagABD was connected to the N-terminus of the XTEN polypeptide (144 amino acids) through a (GGGGS)3 linkerLinearLNoneFusion protein of GLP-1, ABD, XTEN (either 144 or 288)Antidiabetes, AntiobesityAt 1, 3, 7, 12, 18, 24, 30, 36 h, approximately 30 μL of blood was drawn from the tail vein5 nmol12.9C57Bl/6 mice plasma protease And DPP-4ELISAC57BL/6 mice plasmaIn VivoNoneNoneGLP-ABD-XTEN144 has a Kd value of only 5.50 nM
4059
382935402024
ENLYFQHGEGTFTSDVSSYLEGQAAKEFIAWLVKGRGGGGSGGGGSGGGGSLAEAKVLANRELDKYGVSDYYKNLINNAKTVEGVKALIDEILAALPGGGGSGGGGSGGGGSHSQGTFTSDYSKYLDSRRAQDFVQWLMNTGGEGSGEGSEGEGSEGSGEGEGSEGSGEGEGGSEGSEGEGGSEGSEGEGGSEGSEGEGSGEGSEGEGGSEGSEGEGSGEGSEGEGSEGGSEGEGGSEGSEGEGSGEGSEGEGGEGGSEGEGSEGSGEGEGSGEGSEGEGSEGSGEGEGSGEGSEGEGSEGSGEGEGSEGSGEGEGGSEGSEGEGSEGSGEGEGGEGSGEGEGSGEGSEGEGGGEGSEGEGSGEGGEGEGSEGGSEGEGGSEGGEGEGSEGSGEGEGSEGGSEGEGSEGGSEGEGSEGSGEGEGSEGSGEG
GLP-ABD-XTEN288401GLP-1 molecule was linked to the N-terminus of ABD via a (GGGGS)3 linker (GLP-ABD), His-tagABD was connected to the N-terminus of the XTEN polypeptide (288 amino acids) through a (GGGGS)3 linkerLinearLNoneFusion protein of GLP-1, ABD, XTEN (either 144 or 288)Antidiabetes, AntiobesityAt 1, 3, 7, 12, 18, 24, 30, 36 h, approximately 30 μL of blood was drawn from the tail vein5 nmol7.32C57Bl/6 mice plasma protease And DPP-4ELISAC57BL/6 mice plasmaIn VivoNoneNoneGLP-ABD-XTEN288 showed a Kd value of 27.78 nM
4062
380069442024
CGKGGGGGIEGPTLRQWLAARAGGGGGGGGIEGPTLRQWLAARA
Fatty Acid Modified TMP108FreeFreeLinearLC41H70O15N4 fatty acid modificationTMP analogueTreatment of ThrombocytopeniaN.A.100 μg/kg128.5Beagle dogs plasma proteaseELISABeagle dogs plasmaIn VivoNoneNoneThe modified TMPs, particularly the C41H70O15N4 group, showed enhanced and prolonged activity, reaching peak platelet counts of 5047 × 10⁹/L at 216 hours (enhanced platelet counts)
4125
378274962024
N.A.
TTRA81V heterozygous508N.A.N.A.LinearLAlanine (Ala) is substituted with valine (Val) at position 81Derived from missense mutation in the TTR geneCauses mild transthyretin amyloid cardiomyopathyN.A.3.6 μM21Urea between 0.5 and 9 M in phosphate buffer (1 mM of EDTA, 10 mM of sodium phosphate, and 100 mM of potassium chloride, pH = 7.4UPLCHuman serumIn VitroNoneNoneN.A.
4126
378274962024
N.A.
TTRA81V homozygous508N.A.N.A.LinearLAlanine (Ala) is substituted with valine (Val) at position 81Derived from missense mutation in the TTR geneCauses mild transthyretin amyloid cardiomyopathyN.A.3.6 μM17.5Urea between 0.5 and 9 M in phosphate buffer (1 mM of EDTA, 10 mM of sodium phosphate, and 100 mM of potassium chloride, pH = 7.4UPLCHuman serumIn VitroNoneNoneN.A.
4127
378274962024
N.A.
TTRWT (wild-type transthyretin)508N.A.N.A.LinearLNoneLiver‐secreted plasma proteinCauses mild transthyretin amyloid cardiomyopathyN.A.3.6 μM44Urea between 0.5 and 9 M in phosphate buffer (1 mM of EDTA, 10 mM of sodium phosphate, and 100 mM of potassium chloride, pH = 7.4UPLCHuman serumIn VitroNoneNoneN.A.
4128
378274962024
N.A.
TTRL55P mutation508N.A.N.A.LinearLleucine (Leu) is substituted with proline (Pro) at position 55Derived from missense mutation in the TTR gene (L55P)Causes mild transthyretin amyloid cardiomyopathyN.A.3.6 μM4.4Urea between 0.5 and 9 M in phosphate buffer (1 mM of EDTA, 10 mM of sodium phosphate, and 100 mM of potassium chloride, pH = 7.4UPLCHuman serumIn VitroNoneNoneN.A.
4165
381165632023
MKIILWLCVFGLFLATLFPISWQMPVESGLSSEDSASSESFASKIKRHGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPSGGGGGSGGGGSGGGGS-(DARP)-GGGGSGGGGSGGGGSMDSDETGFEHSGLWVSVLAGLLLGACQAHPIPDSSPLLQFGGQVRQRYLYTDDAQQTEAHLEIREDGTVGGAADQSPESLLQLKALKPGVIQILGVKTSRFLCQRPDGALYGSLHFDPEACSFRELLLEDGYNVYQSEAHGLPLHLPGNKSPHRDPAPRGPARFLPLPGLPPALPEPPGILAPQPPDVGSSDPLSMVGPSQGRSPSYAS
Ex-DARP-FGF21327Exendin-4 peptide (Ex) fused to the N-terminus of the DARPin (DARP) protein via (GGGGS)3, His-tag and TEV protease site introduced at position 1FGF21 fused to the C-terminus of the DARPin (DARP) protein via (GGGGS)3 linkerLinearLL98R and P171A amino acid substitutions in FBGF21Exendin-4, DARPin, FGF21 fusion proteinAntidiabetes, AntiobesityApproximately 40 µL of blood was collected from the orbital venous plexus at different time points (1, 3, 8, 12, 24, 36, 48, and 72 h)10 nmol/kg27.6 ± 3.2C57BL/6 mice plasma proteaseELISAC57BL/6 mice plasmaIn VivoNoneNoneEx-DARP-FGF21 and Ex-DARP were efficaciously bound to HSA with half-maximal binding concentrations of 4.5 nM and 1.9 nM, respectively
4170
380928942023
MPRPRLLAALCGALLCAPSLLVALDICSKNPCHNGGLCEEISQEVRGDVFPSYTCTCLKGYAGNHCETKCVEPLGLENGNIANSQIAASSVRVTFLGLQHWVPELARLNRAGMVNAWTPSSNDDNPWIQVNLLRRMWVTGVVTQGASRLASHEYLKAFKVAYSLNGHEFDFIHDVNKKHKEFVGNWNKNAVHVNLFETPVEAQYVRLYPTSCHTACTLRFELLGCELNGCANPLGLKNNSIPDKQITASSSYKTWGLHLFSWNPSYARLDKQGNFNAWVAGSYGNDQWLQVDLGSSKEVTGIITQGARNFGSVQFVASYKVAYSNDSANWTEYQDPRTGSSKIFPGNWDNHSHKKNLFETPILARYVRILPVAWHNRIALRLELLGC
Tag-free rhMFG-E838723 amino acid leader sequence of cystatin S introduced at N terminal FreeLinearLNoneExpressed in Expi293F cellsAntiinflammatory (Including Radiation Injury)Blood samples (100 μl per time point) were collected starting from 2 to 6 hours50 µg1.45 (Terminal Elimination Half Life)SD rats plasma proteaseELISASD rats plasmaIn VivoNoneNoneThe tag-free rhMFG-E8 demonstrated markedly higher cell adhesion binding activity (to SVEC4-10 cells) compared to E. coli-expressed His-tagged rhMFG-E8, which binds to αVβ3 integrin on the membrane of phagocytes
4171
380928942023
MPRPRLLAALCGALLCAPSLLVALDICSKNPCHNGGLCEEISQEVRGDVFPSYTCTCLKGYAGNHCETKCVEPLGLENGNIANSQIAASSVRVTFLGLQHWVPELARLNRAGMVNAWTPSSNDDNPWIQVNLLRRMWVTGVVTQGASRLASHEYLKAFKVAYSLNGHEFDFIHDVNKKHKEFVGNWNKNAVHVNLFETPVEAQYVRLYPTSCHTACTLRFELLGCELNGCANPLGLKNNSIPDKQITASSSYKTWGLHLFSWNPSYARLDKQGNFNAWVAGSYGNDQWLQVDLGSSKEVTGIITQGARNFGSVQFVASYKVAYSNDSANWTEYQDPRTGSSKIFPGNWDNHSHKKNLFETPILARYVRILPVAWHNRIALRLELLGC
Tag-free rhMFG-E838723 amino acid leader sequence of cystatin S introduced at N terminal FreeLinearLNoneExpressed in Expi293F cellsAntiinflammatory (Including Radiation Injury)Blood samples (100 μl per time point) were collected starting from 2 to 12 hours50 µg2.33 (Terminal Elimination Half Life)SD rats plasma proteaseELISASD rats plasmaIn VivoNoneNoneThe tag-free rhMFG-E8 demonstrated markedly higher cell adhesion binding activity (to SVEC4-10 cells) compared to E. coli-expressed His-tagged rhMFG-E8, which binds to αVβ3 integrin on the membrane of phagocytes
4172
380270632023
QVTLKESGPGILQPSQTLSLTCSFSGFSLNTFGMGVSWIRQPSGKGLEWLAHIFWDDDKHYNPSLKSRLTISKDTSNNQVFLKITTVDTADTATYYCVRYGFDGFPYWGQGTGGGGSGGGGSGGGGSDVVMTQTPLSLPVSLGDQASISCRSNQSLVHSNGNTYLHWYLQKPGQSPKLLIYKVSNRFSGVPDRPSGSGSGTDFTLKISRVEAEDLGFYFCSQSTRVPWTFGGGTKLEIKR -METDTLLLWVLLLWVPGSTGDEFMGYQGPPGPPGPPGIPGNHGNNGNNGATGHEGAKGEKGDKGDLGPRGERGQHGPKGEKGYPGIPGYCGPPGPPGPPGIPGNHGNNGNNGATGHEGAKGEKGDKGDLGPRGERGQHGPKGEKGYPGIPDYKDDDDKLQGGRHHHHHH
ScFv9-CD466FreeFusion of CDLinearLBiotinylationCD sequence originates from the C1qTNF3 protein and scFv9 sequence is derived from an antibody fragment to target amyloid beta (Aβ)Treatment of AD and Parkinson diseasePlasma was collected at 0, 2, 4, 8, and 24 h after injection250 μg1.82TgCRND8 mice plasma proteaseDirect ELISATgCRND8 mice plasmaIn VivoNoneNoneN.A.
4173
380270632023
QVTLKESGPGILQPSQTLSLTCSFSGFSLNTFGMGVSWIRQPSGKGLEWLAHIFWDDDKHYNPSLKSRLTISKDTSNNQVFLKITTVDTADTATYYCVRYGFDGFPYWGQGTGGGGSGGGGSGGGGSDVVMTQTPLSLPVSLGDQASISCRSNQSLVHSNGNTYLHWYLQKPGQSPKLLIYKVSNRFSGVPDRPSGSGSGTDFTLKISRVEAEDLGFYFCSQSTRVPWTFGGGTKLEIKR 
ScFv9304FreeFreeLinearLBiotinylationThe scFv9 sequence is derived from an antibody fragment to target amyloid beta (Aβ)Treatment of AD and Parkinson diseasePlasma was collected at 0, 2, 4, 8, and 24 h after injection250 μg0.74TgCRND8 mice plasma proteaseDirect ELISATgCRND8 mice plasmaIn VivoNoneNoneN.A.
4182
378748232023
GSGSGSGSGSGSGSGSGSGSGWGIPWCTLDPGSLQCAWLGKHGGGGSGGVVCQDWEGVELCWQGGGWGIPWCTLDPGSLQCAWLGKHGGGGSGGVVCQDWEGVELCWQGG
MDK-703 110Fused with IgG2 Fc chain via (Gly-Ser)10 linker, Fc-fragments consisting of the CH2 and CH3 domains of the heavy chain and hinge regions of human IgG2 Fc modified as follows: The first and second cysteines of the hinge region were replaced with serine to prevent detrimental disulfide bridge formation; the last amino acid (lysine) of the Fc region was replaced with an alanineFreeLinearLNoneSyntheticIL-7R agonist peptideBlood samples were collected at pre-Dose (day 1), 0.5, 1 h, 2 h, 4 h, 8 h, 24 h, 48 h, 72 h, 96 h, 120 h, 144 h, 168 h, 192 h, and 216 h post-dose1 mg/kg46 (Terminal Half Life)Cynomolgus monkeys serum proteaseSandwich ELISACynomolgus monkeys serumIn VivoNoneNoneIC50(nM) = 190 (IC50 values in a competition ELISA for compound binding to Cyno IL-7Rα)
4186
374497812023
pSar200-b-pCys(SO2Et)30
NCL30230Polysarcosine = poly(N-methyl glycine)FreeLinearLfluorescently labeled with Atto647N, polysarcosine-block-poly(S-ethylsulfonyl-l-cysteine)syntheticImprove the therapeutic profile of hydrophobic drugs, reduce or completely avoid protein corona formationBlood samples of 50 μL were collected from the tail vein at the defined time points after systemic administration: 10 min, 1 h, 6 h, 24 h, 72 h5 μg/μL11.4C57BL/6 mice plasma proteaseFluorescence spectrophotometryC57BL/6 mice plasma In VivoNoneNoneNot mentioned
4187
374497812023
pSar200-b-pCys(SO2Et)30
2F-CL30230Polysarcosine = poly(N-methyl glycine)FreeLinearLfluorescently labeled with Atto647N, polysarcosine-block-poly(S-ethylsulfonyl-l-cysteine)syntheticImprove the therapeutic profile of hydrophobic drugs, reduce or completely avoid protein corona formationBlood samples of 50 μL were collected from the tail vein at the defined time points after systemic administration: 10 min, 1 h, 6 h, 24 h, 72 h5 μg/μL11.3C57BL/6 mice plasma proteaseFluorescence spectrophotometryC57BL/6 mice plasma In VivoNoneNoneNot mentioned
4188
374497812023
pSar200-b-pCys(SO2Et)30
3F-CL30230Polysarcosine = poly(N-methyl glycine)FreeLinearLfluorescently labeled with Atto647N, polysarcosine-block-poly(S-ethylsulfonyl-l-cysteine)syntheticImprove the therapeutic profile of hydrophobic drugs, reduce or completely avoid protein corona formationBlood samples of 50 μL were collected from the tail vein at the defined time points after systemic administration: 10 min, 1 h, 6 h, 24 h, 72 h5 μg/μL19.1C57BL/6 mice plasma proteaseFluorescence spectrophotometryC57BL/6 mice plasma In VivoNoneNoneNot mentioned
4350
N.A.2023
EVQLLESGGGLVQPGGSLRLSCAASGFTFRSFGMSWVRQAPGKGPEWVSSISGSGSDTLYADSVKGRFTISRDNSKNTLYLQMNSLRPEDTAVYYCTIGGSLSRSSQGTLVTVSSDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLYITREPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALKFHYTQKSLSLSPG
TA-Alb23-Fc-ABDEG341Alb23 fused at the N-termini of both Fc domains of efgartigimodFreeLinearLNoneSyntheticFcRN AntagonistBlood sample were collected for Pk Measurement Ar : Test Day 1 (Td1)(Pre-Dosing), Td1(Prior To Dosing), Td1(5 Min), Td2(24 Hrs Post Dosing), Td3, Td4, Td6, Td8, Td11, Td15, Td18, Td22, Td29, Td36 And Td4320 mg/kg27Cynomolgus monkeys serum proteaseSandwich ELISACynomolgus monkeys serumIn VivoNoneEP 2023066180 WN.A.
4351
N.A.2023
EVQLLESGGGLVQPGGSLRLSCAASGFTFRSFGMSWVRQAPGKGPEWVSSISGSGSDTLYADSVKGRFTISRDNSKNTLYLQMNSLRPEDTAVYYCTIGGSLSRSSQGTLVTVSSDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLYITREPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALKFHYTQKSLSLSPG
TA-Alb23-Fc-ABDEG341Alb23 fused at the N-termini of both Fc domains of efgartigimodFreeLinearLNoneSyntheticFcRN AntagonistBlood sample were collected for PK measurement Ar : Test Day 1 (Td1)(Pre-Dosing), Td1(Prior To Dosing), Td1(5 Min), Td2(24 Hrs Post Dosing), Td3, Td4, Td6, Td8, Td11, Td15, Td18, Td22, Td29, Td36 And Td435 mg/kg28 ± 23Cynomolgus monkeys serum proteaseSandwich ELISACynomolgus monkeys serumIn VivoNoneEP 2023066180 WN.A.
4352
N.A.2023
EVQLLESGGGLVQPGGSLRLSCAASGFTFRSFGMSWVRQAPGKGPEWVSSISGSGSDTLYADSVKGRFTISRDNSKNTLYLQMNSLRPEDTAVYYCTIGGSLSRSSQGTLVTVSSDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLYITREPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALKFHYTQKSLSLSPG
TA-Alb23-Fc-ABDEG341Alb23 fused at the N-termini of both Fc domains of efgartigimodFreeLinearLNoneSyntheticFcRN AntagonistBlood sample were collected for PK measurement Ar : Test Day 1 (Td1)(Pre-Dosing), Td1(Prior To Dosing), Td1(5 Min), Td2(24 Hrs Post Dosing), Td3, Td4, Td6, Td8, Td11, Td15, Td18, Td22, Td29, Td36 And Td4320 mg/kg26.5C2 Cynomolgus monkeys serum proteaseSandwich ELISAC2 Cynomolgus monkeys serumIn VivoNoneEP 2023066180 WN.A.
4353
N.A.2023
EVQLLESGGGLVQPGGSLRLSCAASGFTFRSFGMSWVRQAPGKGPEWVSSISGSGSDTLYADSVKGRFTISRDNSKNTLYLQMNSLRPEDTAVYYCTIGGSLSRSSQGTLVTVSSDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLYITREPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALKFHYTQKSLSLSPG
TA-Alb23-Fc-ABDEG341Alb23 fused at the N-termini of both Fc domains of efgartigimodFreeLinearLNoneSyntheticFcRN AntagonistBlood sample were collected for PK Measurement Ar : Test Day 1 (Td1)(Pre-Dosing), Td1(Prior To Dosing), Td1(5 Min), Td2(24 Hrs Post Dosing), Td3, Td4, Td6, Td8, Td11, Td15, Td18, Td22, Td29, Td36 And Td435 mg/kg13.4C4 Cynomolgus monkeys serum proteaseSandwich ELISAC4 Cynomolgus monkeys serumIn VivoNoneEP 2023066180 WN.A.
4354
N.A.2023
EVQLLESGGGLVQPGGSLRLSCAASGFTFRSFGMSWVRQAPGKGPEWVSSISGSGSDTLYADSVKGRFTISRDNSKNTLYLQMNSLRPEDTAVYYCTIGGSLSRSSQGTLVTVSSDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLYITREPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALKFHYTQKSLSLSPG
TA-Alb23-Fc-ABDEG341Alb23 fused at the N-termini of both Fc domains of efgartigimodFreeLinearLNoneSyntheticFcRN AntagonistBlood sample were collected for PK measurement Ar : Test Day 1 (Td1)(Pre-Dosing), Td1(Prior To Dosing), Td1(5 Min), Td2(24 Hrs Post Dosing), Td3, Td4, Td6, Td8, Td11, Td15, Td18, Td22, Td29, Td36 And Td435 mg/kg54.4C5 Cynomolgus monkeys serum proteaseSandwich ELISAC5 Cynomolgus monkeys serumIn VivoNoneEP 2023066180 WN.A.
4355
N.A.2023
EVQLLESGGGLVQPGGSLRLSCAASGFTFRSFGMSWVRQAPGKGPEWVSSISGSGSDTLYADSVKGRFTISRDNSKNTLYLQMNSLRPEDTAVYYCTIGGSLSRSSQGTLVTVSSDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLYITREPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALKFHYTQKSLSLSPG
TA-Alb23-Fc-ABDEG341Alb23 fused at the N-termini of both Fc domains of efgartigimodFreeLinearLNoneSyntheticFcRN AntagonistBlood sample were collected for PK Measurement Ar : Test Day 1 (Td1)(Pre-Dosing), Td1(Prior To Dosing), Td1(5 Min), Td2(24 Hrs Post Dosing), Td3, Td4, Td6, Td8, Td11, Td15, Td18, Td22, Td29, Td36 And Td435 mg/kg16.9C6 Cynomolgus monkeys serum proteaseSandwich ELISAC6 Cynomolgus monkeys serumIn VivoNoneEP 2023066180 WN.A.
4356
N.A.2023
DKTHTCPPCPAPELLGGPSVFLFPPKPKDTLYITREPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALKFHYTQKSLSLSPGGGGGSGGGGSGGGGSGGGGSEVQLLESGGGLVQPGGSLRLSCAASGFTFRSFGMSWVRQAPGKGPEWVSSISGSGSDTLYADSVKGRFTISRDNSKNTLYLQMNSLRPEDTAVYYCTIGGSLSRSSQGTLVTVSS
TA-Fc-ABDEG-Alb23361FreeAlb23 fused at the C-termini of both Fc domains of ABDEG via a 20GS linkerLinearLNoneSyntheticFcRN AntagonistN.A.30 mg/kg15G1-1 Cynomolgus monkeys serum proteaseSandwich ELISAG1-1 Cynomolgus monkeys serumIn VivoNoneEP 2023066180 WN.A.
4357
N.A.2023
DKTHTCPPCPAPELLGGPSVFLFPPKPKDTLYITREPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALKFHYTQKSLSLSPGGGGGSGGGGSGGGGSGGGGSEVQLLESGGGLVQPGGSLRLSCAASGFTFRSFGMSWVRQAPGKGPEWVSSISGSGSDTLYADSVKGRFTISRDNSKNTLYLQMNSLRPEDTAVYYCTIGGSLSRSSQGTLVTVSS
TA-Fc-ABDEG-Alb23361FreeAlb23 fused at the C-termini of both Fc domains of ABDEG via a 20GS linkerLinearLNoneSyntheticFcRN AntagonistN.A.30 mg/kg9.3G1-2 Cynomolgus monkeys serum proteaseSandwich ELISAG1-2 Cynomolgus monkeys serumIn VivoNoneEP 2023066180 WN.A.
4358
N.A.2023
DKTHTCPPCPAPELLGGPSVFLFPPKPKDTLYITREPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALKFHYTQKSLSLSPGGGGGSGGGGSGGGGSGGGGSEVQLLESGGGLVQPGGSLRLSCAASGFTFRSFGMSWVRQAPGKGPEWVSSISGSGSDTLYADSVKGRFTISRDNSKNTLYLQMNSLRPEDTAVYYCTIGGSLSRSSQGTLVTVSS
TA-Fc-ABDEG-Alb23361FreeAlb23 fused at the C-termini of both Fc domains of ABDEG via a 20GS linkerLinearLNoneSyntheticFcRN AntagonistN.A.30 mg/kg4.5G1-3 Cynomolgus monkeys serum proteaseSandwich ELISAG1-3 Cynomolgus monkeys serumIn VivoNoneEP 2023066180 WN.A.
4359
N.A.2023
DKTHTCPPCPAPELLGGPSVFLFPPKPKDTLYITREPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALKFHYTQKSLSLSPGGGGGSGGGGSGGGGSGGGGSEVQLLESGGGLVQPGGSLRLSCAASGFTFRSFGMSWVRQAPGKGPEWVSSISGSGSDTLYADSVKGRFTISRDNSKNTLYLQMNSLRPEDTAVYYCTIGGSLSRSSQGTLVTVSS
TA-Fc-ABDEG-Alb23361FreeAlb23 fused at the C-termini of both Fc domains of ABDEG via a 20GS linkerLinearLNoneSyntheticFcRN AntagonistN.A.75 mg/kg13G2-1 Cynomolgus monkeys serum proteaseSandwich ELISAG2-1 Cynomolgus monkeys serumIn VivoNoneEP 2023066180 WN.A.
4360
N.A.2023
DKTHTCPPCPAPELLGGPSVFLFPPKPKDTLYITREPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALKFHYTQKSLSLSPGGGGGSGGGGSGGGGSGGGGSEVQLLESGGGLVQPGGSLRLSCAASGFTFRSFGMSWVRQAPGKGPEWVSSISGSGSDTLYADSVKGRFTISRDNSKNTLYLQMNSLRPEDTAVYYCTIGGSLSRSSQGTLVTVSS
TA-Fc-ABDEG-Alb23361FreeAlb23 fused at the C-termini of both Fc domains of ABDEG via a 20GS linkerLinearLNoneSyntheticFcrn AntagonistN.A.75 mg/kg6.1G2-2 Cynomolgus monkeys serum proteaseSandwich ELISAG2-2 Cynomolgus monkeys serumIn VivoNoneEP 2023066180 WN.A.
4361
N.A.2023
DKTHTCPPCPAPELLGGPSVFLFPPKPKDTLYITREPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALKFHYTQKSLSLSPGGGGGSGGGGSGGGGSGGGGSEVQLLESGGGLVQPGGSLRLSCAASGFTFRSFGMSWVRQAPGKGPEWVSSISGSGSDTLYADSVKGRFTISRDNSKNTLYLQMNSLRPEDTAVYYCTIGGSLSRSSQGTLVTVSS
TA-Fc-ABDEG-Alb23361FreeAlb23 fused at the C-termini of both Fc domains of ABDEG via a 20GS linkerLinearLNoneSyntheticFcrn AntagonistN.A.75 mg/kg12G2-3 Cynomolgus monkeys serum proteaseSandwich ELISAG2-3 Cynomolgus monkeys serumIn VivoNoneEP 2023066180 WN.A.
4362
N.A.2023
AEAKYAKEAVEALVEIWTLPNLTREQWQAFIYKLRDDPSQSSELLSEAKKLNDSQAPKASGSLAEAKEAANAELDSYGVSDFYKRLIDKAKTVEGVEALKDAILAALP
ZTPA001108FreeABD (albumin Binding Domain)LinearLNoneTslp Binding Z VariantsAntiinflammatoryBlood samples (0.5 mL) were collected at the following time points: Predose, At 10 And 30 Min And 1 , 6, 10, 26, 50, 72, And 96 H Postdose And At Days 6, 7, 8, 11 , 13, 15, 18, And 221.33 mg/kg3-4 (Terminal Half Life)Cynomolgus monkeys serum proteaseSandwich PK-ELISACynomolgus monkeys serumIn VivoNoneEP 2023053030 WIC50(nM) = 0.5
4363
N.A.2023
GSLAEAKEAANAELDSYGVSDFYKRLIDKAKTVEGVEALKDAILAALPGGGGSAEAKYAKEAVEALVEIWTLPNLTREQWQAFIYKLRDDPSQSSELLSEAKKLNDSQAPK
ZTPA104111ABD (albumin Binding Domain)FreeLinearLNoneTslp Binding Z VariantsAntiinflammatoryBlood sampling time points were divided into two cohorts as follows: Cohort A (N=3 Per Test Item) Were Bled Predose, At 5 Min And 1 , 8, 72, 168, 264, 408 And 504 H Postdose; And Cohort B (N=3 Per Test Item) Were Bled Predose, At 30 Min And 3, 24, 120, 216, 336 And 456 H Postdose1.2 mg/kg36 (Terminal Half Life)SD rats serum proteaseELISASD rats serumIn VivoNoneEP 2023053030 WIC50(nM) = 0.03
4364
N.A.2023
AEAKYAKEAVEALVEIWTLPNLTREQWQAFIYKLRDDPSQSSELLSEAKKLNDSQAPKASGSLAEAKEAANAELDSYGVSDFYKRLIDKAKTVEGVEALKDAILAALP
ZTPA001108FreeABD (albumin Binding Domain)LinearLNoneTslp Binding Z VariantsAntiinflammatoryBlood sampling time points were divided into two cohorts as follows: Cohort A (N=3 Per Test Item) Were Bled Predose, At 5 Min And 1 , 8, 72, 168, 264, 408 And 504 H Postdose; And Cohort B (N=3 Per Test Item) Were Bled Predose, At 30 Min And 3, 24, 120, 216, 336 And 456 H Postdose1.2 mg/kg29 (Terminal Half Life)SD rats serum proteaseELISASD rats serumIn VivoNoneEP 2023053030 WIC50(nM) = 0.5
4377
380928942023
N.A.
tag-free rhMFG-E8387Cystatin SFreeLinearLGlycosylationDerived from Expi293F Human cellsantiinflammatoryBlood samples (100 μl per time point) were collected at 0, 3, 6, 9, 12 and 15 min, then every 15 min for the first 60 min till 2 hours50 µg11.55 (Distribution Half Life)SD rats plasma proteaseELISASD rats plasmaIn VivoNoneNoneLD50/30 (lethal dose, 50% at 30 days) falls between 14.5 Gy and 15 Gy after partial body irradiation (PBI) in mice treated with vehicle (normal saline),
4389
369970032023
Y-Aib-QGTFTSDYSKYLDERRAKEFVQWLMNTCLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSQEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKGLPSSIEKTISKAKGQPREPQVYTFPPSQEEMTKNQVSLRCLVKGFYPSDIAVEWESNGQPENNYKTTKPVLDSDGSFRLESRLTVDKSRWQEGNVFSCSVMHEALHNHYTQKSLSLS
HM15136240FreeHMC001Cyclic (E36-K40 lactam bridge in GCG analog)LAib, GC15136 and HMC001 are linked via a 10-kDa, bifunctional maleimide-polyethylene glycol-aldehyde (MAL-PEG-ALD) linkerGlucagon analogTreatment of Congenital HyperinsulinismBlood (0.3 mL) was collected from the retro-orbital plexus at 0.25, 0.5, 1, 4, 8, 24, 48, 72, 96, 120, 144, 168, 192, 216, 240, 264, 288, 312, and 336 h after IV administration and at 1, 4, 8, 24, 48, 72, 96, 120, 144, 168, 192, 216, 240, 264, 288, 312, and 336 h after SC administration of HM15136260 μg/kg54.5Mouse serum proteaseELISAMouse serumIn VivoPDB id: 5HVW, https://pubmed.ncbi.nlm.nih.gov/36202918/NoneKD (HM15136) = No binding for FcγRIA, FcγRIIA, FcγRIIB/C, FcγRIIIA, FcγRIIIB, C1q
4390
369970032023
Y-Aib-QGTFTSDYSKYLDERRAKEFVQWLMNTCLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSQEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKGLPSSIEKTISKAKGQPREPQVYTFPPSQEEMTKNQVSLRCLVKGFYPSDIAVEWESNGQPENNYKTTKPVLDSDGSFRLESRLTVDKSRWQEGNVFSCSVMHEALHNHYTQKSLSLS
HM15136240FreeHMC001Cyclic (E36-K40 lactam bridge in GCG analog)LAib, GC15136 and HMC001 are linked via a 10-kDa, bifunctional maleimide-polyethylene glycol-aldehyde (MAL-PEG-ALD) linkerGlucagon analogTreatment of Congenital HyperinsulinismBlood (0.3 mL) was collected from the retro-orbital plexus at 0.25, 0.5, 1, 4, 8, 24, 48, 72, 96, 120, 144, 168, 192, 216, 240, 264, 288, 312, and 336 h after IV administration and at 1, 4, 8, 24, 48, 72, 96, 120, 144, 168, 192, 216, 240, 264, 288, 312, and 336 h after SC administration of HM15136260 μg/kg32.3Mouse serum proteaseELISAMouse serumIn VivoPDB id: 5HVW, https://pubmed.ncbi.nlm.nih.gov/36202918/NoneKD (HM15136) = No binding for FcγRIA, FcγRIIA, FcγRIIB/C, FcγRIIIA, FcγRIIIB, C1q
4391
369970032023
Y-Aib-QGTFTSDYSKYLDERRAKEFVQWLMNTCLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSQEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKGLPSSIEKTISKAKGQPREPQVYTFPPSQEEMTKNQVSLRCLVKGFYPSDIAVEWESNGQPENNYKTTKPVLDSDGSFRLESRLTVDKSRWQEGNVFSCSVMHEALHNHYTQKSLSLS
HM15136240FreeHMC001Cyclic (E36-K40 lactam bridge in GCG analog)LAib, GC15136 and HMC001 are linked via a 10-kDa, bifunctional maleimide-polyethylene glycol-aldehyde (MAL-PEG-ALD) linkerGlucagon analogTreatment of Congenital HyperinsulinismBlood (0.3 mL) was collected from the retro-orbital plexus at 0.25, 0.5, 1, 4, 8, 24, 48, 72, 96, 120, 144, 168, 192, 216, 240, 264, 288, 312, and 336 h after IV administration and at 1, 4, 8, 24, 48, 72, 96, 120, 144, 168, 192, 216, 240, 264, 288, 312, and 336 h after SC administration of HM15136260 μg/kg66.4 ± 33.0Rats serum proteaseELISARats serumIn VivoPDB id: 5HVW, https://pubmed.ncbi.nlm.nih.gov/36202918/NoneKD (HM15136) = No binding for FcγRIA, FcγRIIA, FcγRIIB/C, FcγRIIIA, FcγRIIIB, C1q
4392
369970032023
Y-Aib-QGTFTSDYSKYLDERRAKEFVQWLMNTCLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSQEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKGLPSSIEKTISKAKGQPREPQVYTFPPSQEEMTKNQVSLRCLVKGFYPSDIAVEWESNGQPENNYKTTKPVLDSDGSFRLESRLTVDKSRWQEGNVFSCSVMHEALHNHYTQKSLSLS
HM15136240FreeHMC001Cyclic (E36-K40 lactam bridge in GCG analog)LAib, GC15136 and HMC001 are linked via a 10-kDa, bifunctional maleimide-polyethylene glycol-aldehyde (MAL-PEG-ALD) linkerGlucagon analogTreatment of Congenital HyperinsulinismBlood (0.3 mL) was collected from the retro-orbital plexus at 0.25, 0.5, 1, 4, 8, 24, 48, 72, 96, 120, 144, 168, 192, 216, 240, 264, 288, 312, and 336 h after IV administration and at 1, 4, 8, 24, 48, 72, 96, 120, 144, 168, 192, 216, 240, 264, 288, 312, and 336 h after SC administration of HM15136260 μg/kg40.9 ± 17.7Rats serum proteaseELISARats serumIn VivoPDB id: 5HVW, https://pubmed.ncbi.nlm.nih.gov/36202918/NoneKD (HM15136) = No binding for FcγRIA, FcγRIIA, FcγRIIB/C, FcγRIIIA, FcγRIIIB, C1q
4393
369970032023
Y-Aib-QGTFTSDYSKYLDERRAKEFVQWLMNTCLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSQEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKGLPSSIEKTISKAKGQPREPQVYTFPPSQEEMTKNQVSLRCLVKGFYPSDIAVEWESNGQPENNYKTTKPVLDSDGSFRLESRLTVDKSRWQEGNVFSCSVMHEALHNHYTQKSLSLS
HM15136240FreeHMC001Cyclic (E36-K40 lactam bridge in GCG analog)LAib, GC15136 and HMC001 are linked via a 10-kDa, bifunctional maleimide-polyethylene glycol-aldehyde (MAL-PEG-ALD) linkerGlucagon analogTreatment of Congenital HyperinsulinismBlood (0.3 mL) was collected from the retro-orbital plexus at 0.25, 0.5, 1, 4, 8, 24, 48, 72, 96, 120, 144, 168, 192, 216, 240, 264, 288, 312, and 336 h after IV administration and at 1, 4, 8, 24, 48, 72, 96, 120, 144, 168, 192, 216, 240, 264, 288, 312, and 336 h after SC administration of HM1513652 μg/kg24.9 ± 2.2Dogs serum proteaseELISADogs serumIn VivoPDB id: 5HVW, https://pubmed.ncbi.nlm.nih.gov/36202918/NoneKD (HM15136) = No binding for FcγRIA, FcγRIIA, FcγRIIB/C, FcγRIIIA, FcγRIIIB, C1q
4394
369970032023
Y-Aib-QGTFTSDYSKYLDERRAKEFVQWLMNTCLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSQEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKGLPSSIEKTISKAKGQPREPQVYTFPPSQEEMTKNQVSLRCLVKGFYPSDIAVEWESNGQPENNYKTTKPVLDSDGSFRLESRLTVDKSRWQEGNVFSCSVMHEALHNHYTQKSLSLS
HM15136240FreeHMC001Cyclic (E36-K40 lactam bridge in GCG analog)LAib, GC15136 and HMC001 are linked via a 10-kDa, bifunctional maleimide-polyethylene glycol-aldehyde (MAL-PEG-ALD) linkerGlucagon analogTreatment of Congenital HyperinsulinismBlood (0.3 mL) was collected from the retro-orbital plexus at 0.25, 0.5, 1, 4, 8, 24, 48, 72, 96, 120, 144, 168, 192, 216, 240, 264, 288, 312, and 336 h after IV administration and at 1, 4, 8, 24, 48, 72, 96, 120, 144, 168, 192, 216, 240, 264, 288, 312, and 336 h after SC administration of HM1513652 μg/kg26.6 ± 1.5Dogs serum proteaseELISADogs serumIn VivoPDB id: 5HVW, https://pubmed.ncbi.nlm.nih.gov/36202918/NoneKD (HM15136) = No binding for FcγRIA, FcγRIIA, FcγRIIB/C, FcγRIIIA, FcγRIIIB, C1q
4433
364714332022
EVQLVESGGGLYQPGNSLTLSCVASGFTFSNYGMHWIRQAPKKGLEWIAMITYDSSKMNYADTVKGRFTISRDNSKNTLYEMNSLRSEDTAMYYCAYPTSHYVVDVWGQGYSVTVSSGSTSGGGSGGGSGGGGSSDIQMTQSPASLSASLEEIVTITCQASQDIGNWLAWTQQKPGKSPQLLIYGATSLADGVPSRFSQSRSGTQFSLKISRYQVEDIGIYYCLQAYNTPWTFGGGTKLELKRASAPGSGGGSAPGEPRYPITQNPSPPLKECPPCAAPDLLGGPSYFIFPPKIKDVLMISLSPMYTCVVVDVSEDDPDYQISWFVNNYEVHTAQTQTHREDYNSTLRVVSALPIQHQDWMSGKEFKCKYNNRALPSPIEKTISKPRGPVRAPQVYVLPPPAEEMTKKEFSLTCMITGFLPAEIAVDWTSNGRTEQNYKNTATYLDSDGSYFMYSKLRVQKSTWERGSLFACSVVHEGLHNHLTTKTISRSLGPGGGGSGGGGSGGGGSEPRYPITQNPSPPLKECPPCAAPDLLGGPSVFIFPPKIKDVLMISLSPMVTCVVVDVSEDDPDYQISWFVNNVEVHTAQTQTHREDYNSTLRYVSALPIQHQDWMSGKEFKCKVNNRALPSPIEKTISKPRGPYRAPQVYVLPPPAEEMTKKEFSLTCMITGFLPAEIAVDWTSNGRTEQNYKNTATVLDSDGSYFMYSKLRVQKSTWERGSLFACSVVHEGLHNHLTTKTISRSLG-APGSGGGSAPG-YDDGICKSSDCIKSAARLIQNMDASVEPCTDFFKYACGGWLKRNVIPETSSRYSNFDILRDELEVILKDVLQEPKTEDIVAVQKAKTLYRSCINESAIDSRGGQPLLKLLPDIYGWPVASDNWDQTYGTSWTAEKSIAQLNSKYGKKVLINFFVGTDDKNSTQHIIHFDQPRLGLPSRDYYECTGIYKEACTAYVDFMISVARLIRQEQSLPIDENQLSLEMNKVMELEKEIANATTKPEDRNDPMLLYNKMTLAKLQNNFSLEYNGKSFSWSNFTNEIMSTVNINIQNEEEVVVYAPEYLTKLKPILTKYSPRDLQNLMSWRFIMDLVSSLSRNYKESRNAFRKALYGTTSETATWRRCANYVNGNMENAVGRLYVEAAFAGESKHVVEDLIAQIREVFIQTLDDLTWMDAETKKKAEEKALAIKERIGYPDDIISNENKLNNEYLELNYREDEYFENIIQNLKFSQSKQLKKLREKVDKDEWISGAAVVNAFYSSGRNQIVFPAGILQPPFFSAQQSNSLNYGGIGMVIGHEITHGFDDNGRNFNKDGDLVDWWTQQSANNFKDQSQCMVYQYGNFSWDLAGGQHLNGINTLGENIADNGGIGQAYRAYQNYVKKNGEEKLLPGLDLNHKQLFFLNFAQVWCGTYRPEYAYNSIKTDVHSPGNFRIIGTLQNSAEFADAFHCRKNSYMNPERKCRVW
[125I]sNEP-scFv8D3-scFc 1456sNEP (amino acid 52–749 of NEP) recombinantly linked to a single-chain fragment constant (scFc) of mouse IgG2c antibody at N terminus using linkerScFc then attached to the BBB transporter (scFv8D3) at C terminus using linkerLinearL125I labeledFusion protein of sNEP-scFc-scFv8D3 Treatment of Alzheimer's diseasesBlood samples collected from the tail vein at 1, 4, 6, 24, 48 and 72 h post-administration5 mg/kg16Tg-Arcswe Mice Plasma Proteaseinstant thin layer chromatography (iTLC)Tg-ArcSwe mice plasma In VivoNoneNoneN.A.
4434
364714332022
EVQLVESGGGLYQPGNSLTLSCVASGFTFSNYGMHWIRQAPKKGLEWIAMITYDSSKMNYADTVKGRFTISRDNSKNTLYEMNSLRSEDTAMYYCAYPTSHYVVDVWGQGYSVTVSSGSTSGGGSGGGSGGGGSSDIQMTQSPASLSASLEEIVTITCQASQDIGNWLAWTQQKPGKSPQLLIYGATSLADGVPSRFSQSRSGTQFSLKISRYQVEDIGIYYCLQAYNTPWTFGGGTKLELKRASAPGSGGGSAPGEPRYPITQNPSPPLKECPPCAAPDLLGGPSYFIFPPKIKDVLMISLSPMYTCVVVDVSEDDPDYQISWFVNNYEVHTAQTQTHREDYNSTLRVVSALPIQHQDWMSGKEFKCKYNNRALPSPIEKTISKPRGPVRAPQVYVLPPPAEEMTKKEFSLTCMITGFLPAEIAVDWTSNGRTEQNYKNTATYLDSDGSYFMYSKLRVQKSTWERGSLFACSVVHEGLHNHLTTKTISRSLGPG-GGGSGGGGSGGGGS-EPRYPITQNPSPPLKECPPCAAPDLLGGPSVFIFPPKIKDVLMISLSPMVTCVVVDVSEDDPDYQISWFVNNVEVHTAQTQTHREDYNSTLRYVSALPIQHQDWMSGKEFKCKVNNRALPSPIEKTISKPRGPYRAPQVYVLPPPAEEMTKKEFSLTCMITGFLPAEIAVDWTSNGRTEQNYKNTATVLDSDGSYFMYSKLRVQKSTWERGSLFACSVVHEGLHNHLTTKTISRSLG-APGSGGGSAPG-YDDGICKSSDCIKSAARLIQNMDASVEPCTDFFKYACGGWLKRNVIPETSSRYSNFDILRDELEVILKDVLQEPKTEDIVAVQKAKTLVRSCINESAIDSRGGQPLLKLLPDIYGWPVASDNWDQTYGTSWTAEKSIAQLNSKYGKKVLINFFVGTDDKNSTQHIIHFDQPRLGLPSRDYYECTGIYKEACTAYVDFMISVARLIRQEQSLPIDENQLSLEMNKVMELEKEIANATTKPEDRNDPMLLYNKMTLAKLQNNFSLEYNGKSFSWSNFTNEIMSTVNINIQNEEEVVVYAPEYLTKLKPILTKYSPRDLQNLMSWRFIMDLVSSLSRNYKESRNAFRKALYVTTSETATWRRCANYVNGNMENAVGRLYVEAAFAGESKHVVEDLIAQIREVFIQTLDDLTWMDAETKKKAEEKALAIKERIGYPDDIISNENKLNNEYLELNYREDEYFENIIQNLKFSQSKQLKKLREKVDKDEWISGAAVVNAFYSSGRNQIVFPAGILQPPFFSAQQSNSLNYGGIGMVIGHEITHGFDDNGRNFNKDGDLVDWWTQQSANNFKDQSQCMVYQYGNFSWDLAGGQHLNGINTLGENIADNGGIGQAYRAYQNYVKKNGEEKLLPGLDLNHKQLFFLNFAQVWCGTYRPEYAYNSIKTDVHSPKNFRIIGTLQNSAEFADAFHCRKNSYMNPERKCRVW
[125I]muNEP-scFv8D3-scFc1456sNEP (amino acid 52–749 of NEP) recombinantly linked to a single-chain fragment constant (scFc) of mouse IgG2c antibody at N terminus using linkerScFc then attached to the BBB transporter (scFv8D3) at C terminus using linkerLinearL125I labeledFusion protein of sNEP-scFc-scFv8D3 Treatment of Alzheimer's diseasesBlood samples collected from the tail vein at 1, 4, 6, 24, 48 and 72 h post-administration2.5 mg/kg 18Tg-Arcswe Mice Plasma Proteaseinstant thin layer chromatography (iTLC)Tg-ArcSwe mice plasma In VivoNoneNoneN.A.
4524
360348082022
MGHPPLLPLLLLLHTCVPASWGLRCMQCKTNGDCRVEECALGQDLCRTTIVRLWEEGEELELVEKSCTHSEKTNRTLSYRTGLKITSLTEVVCGLDLCNQGNSGRAVTYSRSRYLECISCGSSDMSCERGRHQSLQCRSPEEQCLDVVTHWIQEGEEGRPKDDRHLRGCGYLPGCPGSNGFHNNDTFHFLKCCNTTKCNEGPILELENLPQNGRQCYSCKGNSTHGCSSEETFLIDCRGPMNQCLVATGTHEPKNQSYMVRGCATASMCQHAHLGDAFSMNHIDVSCCTKSGCNHPDLDVQYRSGAAPQPGPAHLSLTITLLMTARLWGGTLLWT
uPAR335FreeFreeLinearLNoneDerived from PLAUR genePlays role in thrombosisN.A.N.A.209.6 ± 0.2 BEAS-2B cells lysate proteaseDensitometry analysis using NIH Image JBEAS-2B cells lysate with UK treatment +H/R (Hypoxia/Reoxygenation) + CycloheximideIn VivoNoneNoneN.A.
4525
360348082022
MGHPPLLPLLLLLHTCVPASWGLRCMQCKTNGDCRVEECALGQDLCRTTIVRLWEEGEELELVEKSCTHSEKTNRTLSYRTGLKITSLTEVVCGLDLCNQGNSGRAVTYSRSRYLECISCGSSDMSCERGRHQSLQCRSPEEQCLDVVTHWIQEGEEGRPKDDRHLRGCGYLPGCPGSNGFHNNDTFHFLKCCNTTKCNEGPILELENLPQNGRQCYSCKGNSTHGCSSEETFLIDCRGPMNQCLVATGTHEPKNQSYMVRGCATASMCQHAHLGDAFSMNHIDVSCCTKSGCNHPDLDVQYRSGAAPQPGPAHLSLTITLLMTARLWGGTLLWT
uPAR335FreeFreeLinearLNoneDerived from PLAUR genePlays role in thrombosisN.A.N.A.48.2 ± 2.3 BEAS-2B cells lysate proteaseDensitometry analysis using NIH Image JBEAS-2B cells lysate with UK treatment +H/R (Hypoxia/Reoxygenation) + CycloheximideIn VivoNoneNoneN.A.
4560
358492142022
DAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLVAASQAALGL
HSA585FreeFreeCyclic (17 Disulfide Bond)LNoneHuman derivedCarrier Protein30 minutes3 mL/kg of 20% albumin 8Human intravascular sample proteaseN.A.Human intravascular sampleIn VivoNoneNoneN.A.
4561
358492142022
DAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLVAASQAALGL
HSA585FreeFreeCyclic (17 Disulfide Bond)LNoneHuman derivedCarrier Protein120 minutes3 mL/kg of 20% albumin 6.3Human intravascular sample proteaseN.A.Human intravascular sampleIn VivoNoneNoneN.A.
4562
358403382022
FVNQHLCGSHLVEALELVCGERGFHYGGGGGGSGGGGGIVEQCCTSTCSLDQLENYCGGGGGQGGGGQGGGGQGGGGGECPPCPAPPVAGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTFRVVSVLTVVHQDWLNGKEYKCKVSNKGLPAPIEKTISKTKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPMLDSDGSFFLYSVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPG
BIF296Single-chain variant of insulin has modifications:TyrB16Glu,PheB25His,ThrB27Gly,ProB28Gly,LysB29Gly,ThrB30Gly,IleA10Thr,TyrA14Asp,AsnA21Gly, single-chain variant of insulin with B-chain linked to A-chain by a short linker (Linker 1)Interdomain linker (Linker 2) connecting the A-chain of insulin to the Fc and the Fc domain from IgG2LinearLNoneFc-fusion proteinAntidiabetesBlood samples for glucose measurements were collected by tail bleed conducted under brief restraint. Blood glucose was measured preinjection, 1, 2, 4, 6, 8, 10, 12, 24, 48, 72, 96, 120,144, 168, 240, and 336 hours postdose3 nmol/kg128 ± 10Streptozotocin STZ-treated diabetic SD rats blood proteaseInsulin receptor ELISAStreptozotocin STZ-treated diabetic SD rats blood sampleIn VivoNoneNoneReceptor Phosphorylation EC50, nM = 4241 (Functional activity of BIF as determined by phosphorylation of hIR-A expressed in 293 cells)
4563
358403382022
FVNQHLCGSHLVEALELVCGERGFHYGGGGGGSGGGGGIVEQCCTSTCSLDQLENYCGGGGGQGGGGQGGGGQGGGGGECPPCPAPPVAGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTFRVVSVLTVVHQDWLNGKEYKCKVSNKGLPAPIEKTISKTKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPMLDSDGSFFLYSVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPG
BIF296Single-chain variant of insulin has modifications:TyrB16Glu,PheB25His,ThrB27Gly,ProB28Gly,LysB29Gly,ThrB30Gly,IleA10Thr,TyrA14Asp,AsnA21Gly, single-chain variant of insulin with B-chain linked to A-chain by a short linker (Linker 1)Interdomain linker (Linker 2) connecting the A-chain of insulin to the Fc and the Fc domain from IgG2LinearLNoneFc-fusion proteinAntidiabetesBlood samples for glucose measurements were collected by tail bleed conducted under brief restraint. Blood glucose was measured preinjection, 1, 2, 4, 6, 8, 10, 12, 24, 48, 72, 96, 120,144, 168, 240, and 336 hours postdose10 nmol/kg104 ± 4 Streptozotocin STZ-treated diabetic SD rats blood proteaseInsulin receptor ELISAStreptozotocin STZ-treated diabetic SD rats blood sampleIn VivoNoneNoneReceptor Phosphorylation EC50, nM = 391 (Functional activity of BIF as determined by phosphorylation of hIR-B expressed in 293 cells)
4564
358403382022
FVNQHLCGSHLVEALELVCGERGFHYGGGGGGSGGGGGIVEQCCTSTCSLDQLENYCGGGGGQGGGGQGGGGQGGGGGECPPCPAPPVAGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTFRVVSVLTVVHQDWLNGKEYKCKVSNKGLPAPIEKTISKTKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPMLDSDGSFFLYSVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPG
BIF296single-chain variant of insulin has modifications:TyrB16Glu,PheB25His,ThrB27Gly,ProB28Gly,LysB29Gly,ThrB30Gly,IleA10Thr,TyrA14Asp,AsnA21Gly, single-chain variant of insulin with B-chain linked to A-chain by a short linker (Linker 1)interdomain linker (Linker 2) connecting the A-chain of insulin to the Fc and the Fc domain from IgG2LinearLNoneFc-fusion proteinAntidiabetesBlood samples for glucose measurements were collected by tail bleed conducted under brief restraint. Blood glucose was measured preinjection, 1, 2, 4, 6, 8, 10, 12, 24, 48, 72, 96, 120,144, 168, 240, and 336 hours postdose30 nmol/kg120 ± 21Streptozotocin STZ-treated diabetic SD rats blood proteaseInsulin receptor ELISAStreptozotocin STZ-treated diabetic SD rats blood sampleIn VivoNoneNoneReceptor Phosphorylation EC50, nM > 10,000 (Functional activity of BIF as determined by phosphorylation of hIGF-1R expressed in 293 cells)
4565
358403382022
FVNQHLCGSHLVEALELVCGERGFHYGGGGGGSGGGGGIVEQCCTSTCSLDQLENYCGGGGGQGGGGQGGGGQGGGGGECPPCPAPPVAGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTFRVVSVLTVVHQDWLNGKEYKCKVSNKGLPAPIEKTISKTKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPMLDSDGSFFLYSVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPG
BIF296single-chain variant of insulin has modifications:TyrB16Glu,PheB25His,ThrB27Gly,ProB28Gly,LysB29Gly,ThrB30Gly,IleA10Thr,TyrA14Asp,AsnA21Gly, single-chain variant of insulin with B-chain linked to A-chain by a short linker (Linker 1)interdomain linker (Linker 2) connecting the A-chain of insulin to the Fc and the Fc domain from IgG2LinearLNoneFc-fusion proteinAntidiabetesBlood samples for glucose measurements were collected by tail bleed conducted under brief restraint. Blood glucose was measured preinjection, 1, 2, 4, 6, 8, 10, 12, 24, 48, 72, 96, 120,144, 168, 240, and 336 hours postdose30 nmol/kg120 ± 21Streptozotocin STZ-treated diabetic SD rats blood proteaseInsulin receptor ELISAStreptozotocin STZ-treated diabetic SD rats blood sampleIn VivoNoneNoneLipogenesis in 3T3-L1 Adipocytes, EC50 nM = 19 (Functional activity of BIF as assessed by lipogenesis and cellular proliferation)
4566
358403382022
FVNQHLCGSHLVEALELVCGERGFHYGGGGGGSGGGGGIVEQCCTSTCSLDQLENYCGGGGGQGGGGQGGGGQGGGGGECPPCPAPPVAGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTFRVVSVLTVVHQDWLNGKEYKCKVSNKGLPAPIEKTISKTKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPMLDSDGSFFLYSVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPG
BIF296single-chain variant of insulin has modifications:TyrB16Glu,PheB25His,ThrB27Gly,ProB28Gly,LysB29Gly,ThrB30Gly,IleA10Thr,TyrA14Asp,AsnA21Gly, single-chain variant of insulin with B-chain linked to A-chain by a short linker (Linker 1)interdomain linker (Linker 2) connecting the A-chain of insulin to the Fc and the Fc domain from IgG2LinearLNoneFc-fusion proteinAntidiabetesBlood samples for glucose measurements were collected by tail bleed conducted under brief restraint. Blood glucose was measured preinjection, 1, 2, 4, 6, 8, 10, 12, 24, 48, 72, 96, 120,144, 168, 240, and 336 hours postdose30 nmol/kg120 ± 21Streptozotocin STZ-treated diabetic SD rats blood proteaseInsulin receptor ELISAStreptozotocin STZ-treated diabetic SD rats blood sampleIn VivoNoneNoneProliferation in Saos-2 Cells,EC50 nM = 134 (Functional activity of BIF as assessed by cellular proliferation)
4567
358403382022
FVNQHLCGSHLVEALELVCGERGFHYGGGGGGSGGGGGIVEQCCTSTCSLDQLENYCGGGGGQGGGGQGGGGQGGGGGECPPCPAPPVAGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTFRVVSVLTVVHQDWLNGKEYKCKVSNKGLPAPIEKTISKTKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPMLDSDGSFFLYSVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPG
BIF296single-chain variant of insulin has modifications:TyrB16Glu,PheB25His,ThrB27Gly,ProB28Gly,LysB29Gly,ThrB30Gly,IleA10Thr,TyrA14Asp,AsnA21Gly, single-chain variant of insulin with B-chain linked to A-chain by a short linker (Linker 1)interdomain linker (Linker 2) connecting the A-chain of insulin to the Fc and the Fc domain from IgG2LinearLNoneFc-fusion proteinAntidiabetesBlood samples for glucose measurements were collected by tail bleed conducted under brief restraint. Blood glucose was measured preinjection, 1, 2, 4, 6, 8, 10, 12, 24, 48, 72, 96, 120,144, 168, 240, and 336 hours postdose30 nmol/kg120 ± 21Streptozotocin STZ-treated diabetic SD rats blood proteaseInsulin receptor ELISAStreptozotocin STZ-treated diabetic SD rats blood sampleIn VivoNoneNoneProliferation in H4IIE Cells,EC50 nM = 20 (Functional activity of BIF as assessed by cellular proliferation)
4595
356773072022
MTPLGPASSLPQSFLLKCLEQVRKIQADGAALLANQVRQVGDGAALQEKLVSELGNALENALPDTLDTLQLDVKDYFSLRAALLAALPTRLRYLQEADAFQRRAGGVLVASHLGTSLQRLALADSGVLRQLLYYIESGPHQAPLGTGGADQGAMNVTCSKELQAYREQILHDCWLPKDLKDLQLLIEMNVTVLVDIDKLVEVLRLRQGVLHGVHVC
rhG-CSF175FreeFreeLinearLNoneRecombinant human methionyl-granulocyte colonystimulating factorN.A.Sampling time - 0, 0.083, 0.25, 0.5, 1, 2, 4, 8, 12, 24 h1.0 mg/kg2.74 ± 0.33Mice Serum ProteaseELISAMice serum In VivoNoneNoneN.A.
4596
356773072022
MTPLGPASSLPQSFLLKCLEQVRKIQADGAALLANQVRQVGDGAALQEKLVSELGNALENALPDTLDTLQLDVKDYFSLRAALLAALPTRLRYLQEADAFQRRAGGVLVASHLGTSLQRLALADSGVLRQLLYYIESGPHQAPLGTGGADQGAMNVTCSKELQAYREQILHDCWLPKDLKDLQLLIEMNVTVLVDIDKLVEVLRLRQGVLHGVHVC
PEG10k-rhG-CSF175FreeFreeLinearLPEG10K-MAL fatty chain-modification of rhG-CSF at Cys18 positionrhG-CSF derivativeN.A.sampling time - 0, 0.5, 2, 4, 8, 12, 24, 48, 72, 96, 120, 144, 168h1.0 mg/kg13.05 ± 0.45Mice Serum ProteaseELISAMice serum In VivoNoneNoneN.A.
4597
356773072022
MTPLGPASSLPQSFLLKCLEQVRKIQADGAALLANQVRQVGDGAALQEKLVSELGNALENALPDTLDTLQLDVKDYFSLRAALLAALPTRLRYLQEADAFQRRAGGVLVASHLGTSLQRLALADSGVLRQLLYYIESGPHQAPLGTGGADQGAMNVTCSKELQAYREQILHDCWLPKDLKDLQLLIEMNVTVLVDIDKLVEVLRLRQGVLHGVHVC
C15-rhG-CSF175FreeFreeLinearLC15-MAL fatty chain-modification of rhG-CSF at Cys18 positionrhG-CSF derivativeN.A.sampling time - 0, 0.5, 2, 4, 8, 12, 24, 48, 72, 96, 120, 144, 168 h1.0 mg/kg5.72 ± 0.43Mice Serum ProteaseELISAMice serum In VivoNoneNoneN.A.
4615
354583852022
RDLEVVAATPTSLLISWDAPAVTVRYYRITYGETGGNSPVQEFTVPGSKSTATISGLKPGVDYTITVYAVTGRGDSPASSKPISINYRTEIGGGGSGGGGSGGGGSGGGGSGGGGSGGGGSGGGGSSLDQINVTFLDLEYEMKKLEEAIKKLEESYIDLKEL
FL-EK1162Flexible 35-mer linker (L35) connects the FN3 domain to the EK1 peptide at N terminusFreeLinearLNoneEK1 and 10th FN3 unit conjugatePan-cov fusion inhibitorSerum samples were collected before (0 h) and after injection of EK1 (0.5 h, 1 h, 3 h, 7 h, and 12 h) or FL-EK1 (0.5 h, 1 h, 3 h, 7 h, 24 h, 48 h, 72 h, and 96 h)40 mg/kg 30.0 ± 12.8Mice serum proteaseSandwich ELISAMice serumIn VivoNoneNoneIC50(nM) = 114.5 ± 33.4 against B.1.1.7 (Alpha), IC50(nM) = 201.2 ± 16.8 against B.1.351 (Beta), IC50(nM) = 373.1 ± 16.9 against P.1 (Gamma), IC50(nM) = 133.0 ± 16.5 against B.1.617.2 (Delta), IC50(nM) = 179.2 ± 38.3 against B.1.525 (Eta), IC50(nM) = 230.9 ± 49.3 against B.1.617.1 (Kappa), IC50(nM) = 88.5 ± 58.2 against C.37 (Lambda), IC50(nM) = 297.5 ± 188.2 against B.1.1.529 (Omicron)
4617
354554212022
RDLEVVAATPTSLLISWDAPAVTVRYYRITYGETGGNSPVQEFTVPGSKSTATISGLKPGVDYTITVYAVTGRGDSPASSKPISINYRTEIGGGGSGGGGSGGGGSGGGGSGGGGSGGGGSGGGGSTTWEAWDRAIAEYAARIEALLRALQEQQEKNEAALRE
FLT163FN3 domainFreeLinearLNoneFN3 ,T1144 fusion proteinAntiviral (HIV fusion inhibitor)Blood samples were collected from the orbital sinus at 0, 0.5, 1.5, 3, 6, 9, 12, 24, 48, 72, 96 and 120 h after injection of the inhibitors tested5.94 mg/kg27.09 ± 6.9Rats serum proteaseSandwich ELISARats serum In VivoNoneNoneIC50(nM)= 65.3 ± 2.6 against HIV-1 96USSN20 (X4/R5, A), IC50(nM) = 9.8 ± 0.9 against HIV-1 96USNG17 (X4, A), IC50(nM) = 6.5 ± 0.2 against HIV-1 90US_873 (R5, B), IC50(nM) = 8.8 ± 0.3 against HIV-1 BZ167 (X4, B), IC50(nM) = 12.5 ± 0.5 against HIV-1 SE364 (R5, C), IC50(nM) = 9.3 ± 0.5 against HIV-1 PBL288 (R5, C), IC50(nM) = 11.7 ± 0.8 against HIV-1 92UG001 (X4/R5, D), IC50(nM) = 6.4 ± 0.3 against HIV-1 J32228M4 (R5, D), IC50(nM) = 7.5 ± 0.3 against HIV-1 DJ263 (R5, CRF02_AG), IC50(nM) = 10.2 ± 0.6 against HIV-1 CAM1475MV (R5, CRF02_AG) (Infection on MT-4 cells) 
4631
354148772022
MVATKTFALLLLSLFLAVGLGEKKEGHFSALPSLPVGSHAKVSSPQPRGPRYAEGTFISDYSIAMDKIHQQDFVNWLLAQKGKKNDWKHNITQREARALELASQANRKEEEAVEPQSSPAKNPSDEDLLRDLLIQELLACLLDQTNLCRLRSR
Native GIP153FreeFreeLinearLNoneGlucagonGlucose dependent insulinotropic At selected time points samples were taken: 5, 15, 30, 60, 120, 210, 300 mins1 μM45Human plasma protease LC-MS80% pooled human Li-heparin plasma In VitroNoneNoneN.A.
4648
351746982022
MVSKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTLVTTLTYGVQCFSRYPDHMKQHDFFKSAMPEGYVQERTIFFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNYNSHNVYIMADKQKNGIKVNFKIRHNIEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSALSKDPNEKRDHMVLLEFVTAAGITLGMDELYK
eGFP239FreeFreeLinearLNoneEnhanced GFPTaggingN.A.N.A.565E. Coli Bl21(De3) cells lysate proteaseFluorescence assayE. coli BL21(DE3) cells lysate after 5 h removed the inducerIn VivoPDB id: 4EULNoneN.A.
4649
351746982022
MVSKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTLVTTLTYGVQCFSRYPDHMKQHDFFKSAMPEGYVQERTIFFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNYNSHNVYIMADKQKNGIKVNFKIRHNIEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSALSKDPNEKRDHMVLLEFVTAAGITLGMDELYK-AANDENYALAA
GFP-Ec250GFPEc (E.coli) SsrA tag sequences conjugationLinearLNoneeGFP derivativeIncreases Half LifeN.A.N.A.6E. Coli Bl21(De3) cells lysate proteaseFluorescence assayE. coli BL21(DE3) cells lysate after 5 h removed the inducerIn VivoPDB id: 4EULNoneN.A.
4650
351746982022
MVSKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTLVTTLTYGVQCFSRYPDHMKQHDFFKSAMPEGYVQERTIFFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNYNSHNVYIMADKQKNGIKVNFKIRHNIEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSALSKDPNEKRDHMVLLEFVTAAGITLGMDELYK-AANKNEENTNEVPTFMLNAGQANYAFA
GFP-Mf266GFPMf (M.fluorum) SsrA tag sequencesLinearLNoneeGFP derivativeIncreases Half LifeN.A.N.A.56E. Coli Bl21(De3) cells lysate proteaseFluorescence assayE. coli BL21(DE3) cells lysate after 5 h removed the inducerIn VivoPDB id: 4EULNoneN.A.
4651
351746982022
MVSKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTLVTTLTYGVQCFSRYPDHMKQHDFFKSAMPEGYVQERTIFFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNYNSHNVYIMADKQKNGIKVNFKIRHNIEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSALSKDPNEKRDHMVLLEFVTAAGITLGMDELYK
eGFP239FreeFreeLinearLNoneEnhanced GFPTaggingN.A.N.A.No DegradationE. Coli Bl21(De3) star strain lysate proteaseFluorescence assayE. coli BL21 (DE3) star strain lysate in which RNase E has been knocked out In VivoPDB id: 4EULNoneN.A.
4652
351746982022
MVSKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTLVTTLTYGVQCFSRYPDHMKQHDFFKSAMPEGYVQERTIFFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNYNSHNVYIMADKQKNGIKVNFKIRHNIEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSALSKDPNEKRDHMVLLEFVTAAGITLGMDELYK-AANDENYALAA
GFP-Ec250GFPEc (E.coli) SsrA tag sequencesLinearLNoneeGFP derivativeIncreases Half LifeN.A.N.A.14E. Coli Bl21(De3) star strain lysate proteaseFluorescence assayE. coli BL21 (DE3) star strain lysate in which RNase E has been knocked out In VivoPDB id: 4EULNoneN.A.
4653
351746982022
MVSKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTLVTTLTYGVQCFSRYPDHMKQHDFFKSAMPEGYVQERTIFFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNYNSHNVYIMADKQKNGIKVNFKIRHNIEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSALSKDPNEKRDHMVLLEFVTAAGITLGMDELYK-AANKNEENTNEVPTFMLNAGQANYAFA
GFP-Mf266GFPMf (M.fluorum) SsrA tag sequencesLinearLNoneeGFP derivativeIncreases Half LifeN.A.N.A.424E. Coli Bl21(De3) star strain lysate proteaseFluorescence assayE. coli BL21 (DE3) star strain lysate in which RNase E has been knocked out In VivoPDB id: 4EULNoneN.A.
4664
350460192022
MSKGPG-(VPGGGVPGAGVPGYG)10-PGGGG-SKGEELFTGVVPILVELDGDVNGHKFSVRGEGEGDATNGKLTLKFICTTGKLPVPWPTLVTTLTYGVQCFSRYPDHMKRHDFFKSAMPEGYVQERTISFKDDGTYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNFNSHNVYITADKQKNGIKANFKIRHNVEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSVLSKDPNEKRDHMVLLEFVTAAGITHGMDELYKGS
ELP(0FA)GFP400FreeGFPLinearLNoneELP-GFP conjugateIncreases Half Life1 week10 μM1.6C57Bl/6J mice blood plasma proteaseGFP-specific ELISAC57BL/6J mice blood plasmaIn VivoNoneNoneKD MSA - Mouse serum albumin (μM) = n.d. (Binding affinity of ELP-GFP constructs for serum albumin), KD HSA - Human serum albumin (μM) = n.d
4665
350460192022
MSKGPG-(VPGGGVPGAGVPG(pAzF-FA)G)1(VPGGGVPGAGVPGYG)9-PGGGG-SKGEELFTGVVPILVELDGDVNGHKFSVRGEGEGDATNGKLTLKFICTTGKLPVPWPTLVTTLTYGVQCFSRYPDHMKRHDFFKSAMPEGYVQERTISFKDDGTYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNFNSHNVYITADKQKNGIKANFKIRHNVEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSVLSKDPNEKRDHMVLLEFVTAAGITHGMDELYKGS
ELP(1FA)GFP400FreeGFPLinearL1 Fatty acid conjugation through pAzF (para-azidophenylalanine)ELP-GFP conjugateIncreases Half Life1 week10 μM1.9C57Bl/6J mice blood plasma proteaseGFP-specific ELISAC57BL/6J mice blood plasmaIn VivoNoneNoneKD MSA (μM) = 126 ± 32.2, KD HSA - Human serum albumin (μM) = n.d
4666
350460192022
MSKGPG-(VPGGGVPGAGVPG(pAzF-FA)GVPGGGVPGAGVPGYG)5-PGGGG-SKGEELFTGVVPILVELDGDVNGHKFSVRGEGEGDATNGKLTLKFICTTGKLPVPWPTLVTTLTYGVQCFSRYPDHMKRHDFFKSAMPEGYVQERTISFKDDGTYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNFNSHNVYITADKQKNGIKANFKIRHNVEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSVLSKDPNEKRDHMVLLEFVTAAGITHGMDELYKGS
ELP(5FA)GFP400FreeGFPLinearL5 Fatty acid conjugation through pAzF (para-azidophenylalanine)ELP-GFP conjugateIncreases Half Life1 week10 μM19.6C57Bl/6J mice blood plasma proteaseGFP-specific ELISAC57BL/6J mice blood plasmaIn VivoNoneNoneKD MSA (μM) = 10.3 ± 4.0, KD HSA - Human serum albumin (μM) = n.d
4667
350460192022
MSKGPG-(VPGGGVPGAGVPG(pAzF)G)10-PGGGG–SKGEELFTGVVPILVELDGDVNGHKFSVRGEGEGDATNGKLTLKFICTTGKLPVPWPTLVTTLTYGVQCFSRYPDHMKRHDFFKSAMPEGYVQERTISFKDDGTYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNFNSHNVYITADKQKNGIKANFKIRHNVEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSVLSKDPNEKRDHMVLLEFVTAAGITHGMDELYKGS
ELP(10FA)GFP400FreeGFPLinearL10 Fatty acid conjugation through pAzF (para-azidophenylalanine)ELP-GFP conjugateIncreases Half Life1 week10 μM33.3C57Bl/6J mice blood plasma proteaseGFP-specific ELISAC57BL/6J mice blood plasmaIn VivoNoneNoneKD MSA (μM) =2.76 ± 0.19, KD HSA - Human serum albumin (μM) = n.d
4668
350460192022
MSKGPG-(VPGGGVPGAGVPG(pAzF-FA)G)1(VPGGGVPGAGVPGYG)9-PGGGG-SKGEELFTGVVPILVELDGDVNGHKFSVRGEGEGDATNGKLTLKFICTTGKLPVPWPTLVTTLTYGVQCFSRYPDHMKRHDFFKSAMPEGYVQERTISFKDDGTYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNFNSHNVYITADKQKNGIKANFKIRHNVEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSVLSKDPNEKRDHMVLLEFVTAAGITHGMDELYKGS
ELP(1FA)GFP400FreeGFPLinearL1 Fatty acid conjugation through pAzF (para-azidophenylalanine)ELP-GFP conjugateIncreases Half Life1 week10 μM18.5C57Bl/6J mice blood plasma proteaseGFP-specific ELISAC57BL/6J mice blood plasmaIn VivoNoneNoneKD MSA (μM) =25.9 ± 7.1, KD HSA - Human serum albumin (μM) = 19.3 ± 3.9
4669
350460192022
MSKGPG-(VPGGGVPGAGVPG(pAzF-FA)GVPGGGVPGAGVPGYG)5-PGGGG-SKGEELFTGVVPILVELDGDVNGHKFSVRGEGEGDATNGKLTLKFICTTGKLPVPWPTLVTTLTYGVQCFSRYPDHMKRHDFFKSAMPEGYVQERTISFKDDGTYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNFNSHNVYITADKQKNGIKANFKIRHNVEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSVLSKDPNEKRDHMVLLEFVTAAGITHGMDELYKGS
ELP(5FA)GFP400FreeGFPLinearL5 Fatty acid conjugation through pAzF (para-azidophenylalanine)ELP-GFP conjugateIncreases Half Life1 week10 μM31.7C57Bl/6J mice blood plasma proteaseGFP-specific ELISAC57BL/6J mice blood plasmaIn VivoNoneNoneKD MSA (μM) =4.0 ± 1.6, KD HSA - Human serum albumin (μM) = 3.16 ± 0.60
4670
350460192022
MSKGPG-(VPGGGVPGAGVPG(pAzF)G)10-PGGGG–SKGEELFTGVVPILVELDGDVNGHKFSVRGEGEGDATNGKLTLKFICTTGKLPVPWPTLVTTLTYGVQCFSRYPDHMKRHDFFKSAMPEGYVQERTISFKDDGTYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNFNSHNVYITADKQKNGIKANFKIRHNVEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSVLSKDPNEKRDHMVLLEFVTAAGITHGMDELYKGS
ELP(10FA)GFP400FreeGFPLinearL10 Fatty acid conjugation through pAzF (para-azidophenylalanine)ELP-GFP conjugateIncreases Half Life1 week10 μM27.9C57Bl/6J mice blood plasma proteaseGFP-specific ELISAC57BL/6J mice blood plasmaIn VivoNoneNoneKD MSA (μM) = 2.22 ± 0.03, KD HSA - Human serum albumin (μM) = 1.64 ± 0.17
4724
N.A.2022
QTVVTQEPSLTVSPGGTVTLTCRSSTGAVTTSNYANWVQQKPGQAPRGLIGGTNKRAPGTPARFSGSLLGGKAALTLSGVQPEDEAEYYCALWYSNLWVFGGGTKLTVLGGGGSGGGGSGGGGSEVQLVESGGGLVQPGGSLKLSCAASGFTFNTYAMNWVRQAPGKGLEWVARIRSKYNNYATYYADSVKDRFTISRDDSKNTAYLQMNNLKTEDTAVYYCVRHGNFGNSYVSWFAYWGQGTLVTVSSGGGGSQVQLQQSGSELKKPGASVKVSCKASGYTFTNYGMNWVKQAPGQGLKWMGWINTYTGEPTYTDDFKGRFAFSLDTSVSTAYLQISSLKADDTAVYFCARGGFGSSYWYFDVWGQGSLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSC-DIQLTQSPSSLSASVGDRVSITCKASQDVSIAVAWYQQKPGKAPKLLIYSASYRYTGVPDRFSGSGSGTDFTLTISSLQPEDFAVYYCQQHYITPLTFGAGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
TROP2 TCE (PC1)692FreeFab heavy chain linked to C terminus of ScFv light chainLinearLNoneSyntheticMediates tumor cytotoxicity and T cell activationN.A.3 ug/kg1.02Cynomolgus monkeys plasma proteaseELISACynomolgus monkeys plasmaIn VivoNoneUS 2021/0062261 WEC50(nM) = 0.1477 (TROP binding)
4725
N.A.2022
EVQLVESGGGLVQPGGSLRLSCAASGSTFYTAVMGWVRQAPGKGLEWVAAIRWTALTTSYADSVKGRFTISRDGAKTTLYLQMNSLRPEDTAVYYCAARGTLGLFTTADSYDYWGQGTLVTVSSGGGGSGGGSGGVYCGPEFDESVGCMGGGGSGGGLSGRSDAGSPLGLAGSGGGSEVQLVESGGGLVQPGGSLKLSCAASGFTFNKYAMNWVRQAPGKGLEWVARIRSKYNNYATYYADSVKDRFTISRDDSKNTAYLQMNNLKTEDTAVYYCVRHGNFGNSYISYWAYWGQGTLVTVSSGGGGSGGGGSGGGGSQTVVTQEPSLTVSPGGTVTLTCGSSTGAVTSGNYPNWVQQKPGQAPRGLIGGTKFLAPGTPARFSGSLLGGKAALTLSGVQPEDEAEYYCVLWYSNRWVFGGGTKLTVLGGGGSQVQLQQSGSELKKPGASVKVSCKASGYTFTNYGMNWVKQAPGQGLKWMGWINTYTGEPTYTDDFKGRFAFSLDTSVSTAYLQISSLKADDTAVYFCARGGFGSSYWYFDVWGQGSLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSC-GGVDFCKIYSWPVCHQGGGGSGGLSGRSDAGSPLGLAGSGGSDIQLTQSPSSLSASVGDRVSITCKASQDVSIAVAWYQQKPGKAPKLLIYSASYRYTGVPDRFSGSGSGTDFTLTISSLQPEDFAVYYCQQHYITPLTFGAGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
TROP2 TRACTr PC complex (PC5)911FreeFab heavy chain linked to C terminus of ScFv light chainLinearLNoneSyntheticMediates tumor cytotoxicity and T cell activationN.A.100 ug/kg90.16Cynomolgus monkeys plasma proteaseELISACynomolgus monkeys plasmaIn VivoNoneUS 2021/0062261 WEC50(nM) = 60.25 (TROP binding)
4726
N.A.2022
EVQLVESGGGLVQPGGSLRLSCAASGSTFYTAVMGWVRQAPGKGLEWVAAIRWTALTTSYADSVKGRFTISRDGAKTTLYLQMNSLRPEDTAVYYCAARGTLGLFTTADSYDYWGQGTLVTVSSGGGGSGGGSGGVYCGPEFDESVGCMGSSGGSAAGLLAPPGGLSGRSDAGGGGSEVQLVESGGGLVQPGGSLKLSCAASGFTFNKYAMNWVRQAPGKGLEWVARIRSKYNNYATYYADSVKDRFTISRDDSKNTAYLQMNNLKTEDTAVYYCVRHGNFGNSYISYWAYWGQGTLVTVSSGGGGSGGGGSGGGGSQTVVTQEPSLTVSPGGTVTLTCGSSTGAVTSGNYPNWVQQKPGQAPRGLIGGTKFLAPGTPARFSGSLLGGKAALTLSGVQPEDEAEYYCVLWYSNRWVFGGGTKLTVLGGGGSQVQLQQSGSELKKPGASVKVSCKASGYTFTNYGMNWVKQAPGQGLKWMGWINTYTGEPTYTDDFKGRFAFSLDTSVSTAYLQISSLKADDTAVYFCARGGFGSSYWYFDVWGQGSLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSC-GGIDFCMLYNWPICAGGGGGSSGGSAAGLLAPPGGLSGRSDAGGGGSDIQLTQSPSSLSASVGDRVSITCKASQDVSIAVAWYQQKPGKAPKLLIYSASYRYTGVPDRFSGSGSGTDFTLTISSLQPEDFAVYYCQQHYITPLTFGAGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
TROP2 TRACTr PC complex (PC18)916FreeFab heavy chain linked to C terminus of ScFv light chainLinearLNoneSyntheticMediates tumor cytotoxicity and T cell activationN.A.100 μg/kg 97.31Cynomolgus monkeys plasma proteaseELISACynomolgus monkeys plasmaIn VivoNoneUS 2021/0062261 WIC50(pM) = 3,253
4727
N.A.2022
EVQLVESGGGLVQPGGSLRLSCAASGSTFYTAVMGWVRQAPGKGLEWVAAIRWTALTTSYADSVKGRFTISRDGAKTTLYLQMNSLRPEDTAVYYCAARGTLGLFTTADSYDYWGQGTLVTVSSGGGGSGGGSGGVYCGPEFDESVGCMGSSGGSAAGLLAPPGGLSGRSDAGGGGSEVQLVESGGGLVQPGGSLKLSCAASGFTFNKYAMNWVRQAPGKGLEWVARIRSKYNNYATYYADSVKDRFTISRDDSKNTAYLQMNNLKTEDTAVYYCVRHGNFGNSYISYWAYWGQGTLVTVSSGGGGSGGGGSGGGGSQTVVTQEPSLTVSPGGTVTLTCGSSTGAVTSGNYPNWVQQKPGQAPRGLIGGTKFLAPGTPARFSGSLLGGKAALTLSGVQPEDEAEYYCVLWYSNRWVFGGGTKLTVLGGGGSQVQLQQSGSELKKPGASVKVSCKASGYTFTNYGMNWVKQAPGQGLKWMGWINTYTGEPTYTDDFKGRFAFSLDTSVSTAYLQISSLKADDTAVYFCARGGFGSSYWYFDVWGQGSLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSC-GGVDFCKIYSWPVCHQGGGGSSGGSAAGLLAPPGGLSGRSDAGGGGSDIQLTQSPSSLSASVGDRVSITCKASQDVSIAVAWYQQKPGKAPKLLIYSASYRYTGVPDRFSGSGSGTDFTLTISSLQPEDFAVYYCQQHYITPLTFGAGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGECGGIDFCMLYNWPICAGGGGGSSGGSAAGLLAPPGGLSGRSDAGGGGSDIQLTQSPSSLSASVGDRVSITCKASQDVSIAVAWYQQKPGKAPKLLIYSASYRYTGVPDRFSGSGSGTDFTLTISSLQPEDFAVYYCQQHYITPLTFGAGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
TROP2 TRACTr PC complex (PC21)1177FreeFab heavy chain linked to C terminus of ScFv light chainLinearLNoneSyntheticMediates tumor cytotoxicity and T cell activationN.A.100 μg/kg 100.73Cynomolgus monkeys plasma proteaseELISACynomolgus monkeys plasmaIn VivoNoneUS 2021/0062261 WN.A.
4728
N.A.2022
EVQLVESGGGLVQPGGSLRLSCAASGSTFYTAVMGWVRQAPGKGLEWVAAIRWTALTTSYADSVKGRFTISRDGAKTTLYLQMNSLRPEDTAVYYCAARGTLGLFTTADSYDYWGQGTLVTVSSGGGGSGGGSGGVYCGPEFDESVGCMGGGGSGGGLSGRSDAGSPLGLAGSGGGSEVQLVESGGGLVQPGGSLKLSCAASGFTFNKYAMNWVRQAPGKGLEWVARIRSKYNNYATYYADSVKDRFTISRDDSKNTAYLQMNNLKTEDTAVYYCVRHGNFGNSYISYWAYWGQGTLVTVSSGGGGSGGGGSGGGGSQTVVTQEPSLTVSPGGTVTLTCGSSTGAVTSGNYPNWVQQKPGQAPRGLIGGTKFLAPGTPARFSGSLLGGKAALTLSGVQPEDEAEYYCVLWYSNRWVFGGGTKLTVLGGGGSQVQLQQSGSELKKPGASVKVSCKASGYTFTNYGMNWVKQAPGQGLKWMGWINTYTGEPTYTDDFKGRFAFSLDTSVSTAYLQISSLKADDTAVYFCARGGFGSSYWYFDVWGQGSLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSC-GGIDFCMLYNWPICAGGGGGSGGLSGRSDAGSPLGLAGSGGSDIQLTQSPSSLSASVGDRVSITCKASQDVSIAVAWYQQKPGKAPKLLIYSASYRYTGVPDRFSGSGSGTDFTLTISSLQPEDFAVYYCQQHYITPLTFGAGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
PC-22 complex911FreeFab heavy chain linked to C terminus of ScFv light chainLinearLNoneSyntheticMediates tumor cytotoxicity and T cell activationN.A.100 μg/kg 68.97Cynomolgus monkeys plasma proteaseELISACynomolgus monkeys plasmaIn VivoNoneUS 2021/0062261 WN.A.
4729
N.A.2022
MTMRHNWTPDLSPLWVLLLCAHVVTLLVRATPVSQTTTAATASVRSTKDPCPSQPPVFPAAKQCPALEVTWPEVEVPLNGTLSLSCVACSRFPNFSILYWLGNGSFIEHLPGRLWEGSTSRERGSTGTQLCKALVLEQLTPALHSTNFSCVLVDPEQVVQRHVVLAQLWAGLRATLPPTQEALPSSHSSPQQQG
hIL-18BP194FreeFreeLinearLNoneSyntheticAntagonist of IL-18Single subcutaneous administration: 0, 0.33, 1, 1.5, 3, 5, 7, 12, 24, 48, 72, 120, And 168 Hours (13 Points In Total), Single Intravenous Administration: 0, 0.083, 0.25, 0.5, 1.25, 3, 5, 10, 24, 48, And 72 Hours (11 Points In Total)3 mg/kg + 1 mg/kg6.51Rats plasma proteaseELISARats plasmaIn VivoNoneIB 2021058964 WIC50 of IL-18BP-His was 0.0240 nM
4730
N.A.2022
MTMRHNWTPDLSPLWVLLLCAHVVTLLVRATPVSQTTTAATASVRSTKDPCPSQPPVFPAAKQCPALEVTWPEVEVPLNGTLSLSCVACSRFPNFSILYWLGNGSFIEHLPGRLWEGSTSRERGSTGTQLCKALVLEQLTPALHSTNFSCVLVDPEQVVQRHVVLAQLWAGLRATLPPTQEALPSSHSSPQQQG
hIL-18BP194FreeFreeLinearLNoneSyntheticAntagonist of IL-18Single intravenous administration: 0, 0.083, 0.25, 0.5, 1.25, 3, 5, 10, 24, 48, And 72 Hours (11 Points In Total)1 mg/kg6.51Rats plasma proteaseELISARats plasmaIn VivoNoneIB 2021058964 WIC50 of IL-18BP-His was 0.0240 nM
4752
359102762022
MRKSIVRYFVMAFILLFALSTFLTGVQATSVPDKKSPELEKAEIYGDIDVTSDKQTTVIVELKEKSLAEAKADGEKQTKASLKTARSKAKSKALKTLKKAKVNREYDRVFSGFSMKLPASEIPKLLAVKEVKAVYPNATYKPDSVKGKDVTLAADAIYPQMDKSAPFIGADQAWKSGYTGKGIKVAVIDTGVDYTHPDLKNNFGPYKGYDFVDNDYDPQETPTGDPRGGATDHGTHVAGTIAANGQIKGVAPEATLLAYRVLGPGGSGTTENVIAGIEKAVADGAKVMNLSLGNSLNSPDYATSIALDWAMAEGVVAVTSNGNSGPENWTVGSPGTSRVAISVGASQLPYNEYSVTLPSYSSAKVMGYQEEKDLEALNGQEVELVEAGLGQADDFSGKDVKGKVAVIQRGVIPFVDKAENAKNAGAIGAVIYNNATGEIEANVMGMAVPTVKLSKEEGEKLVQQIKEGKHSVVFSFKLDKKLGETIASFSSRGPVMDTWMIKPDVSAPGVNIVSTIPTHDPKNPYGYGSKQGTSMASPHVAGTAAILKQAKPDWTPEQIKGVLMNTAEKLTDENGKPLPHNTQGAGSIRIMEALKASSIVTPGSHSYGTFLKDKGKQTKKQAFTIENLSSHRKAYQLEYSFKGTGITVSGTERVVVPANQTGKAAAKVTVNSAKTKAGTYEGTVYIREDGRKVAEIPLLLIVKEPDYPRVTSVTVEPGAKQGAYTIEAYLPGGAEELAFLVYDENLNLLGQAGVYKNQGKGYQSYQWNGKINDAASLKSGKYYMLAYASAKGKSSYVLTEDPFIVE
KB-SP 806FreeFreeLinearLNoneDerived from Bacillus sp. KB111 strainHaloprotease50°CN.A.90 (Enzyme Activity)N.A.ZymographyEDTA + Tris-HCl + 0.5 M NaCl+ azocaseinIn VitroGenBank id: KUL11341.1NoneKB-SP exhibited more than 50% of the highest activity at pH=6.5–10
4753
359102762022
MRKSIVRYFVMAFILLFALSTFLTGVQATSVPDKKSPELEKAEIYGDIDVTSDKQTTVIVELKEKSLAEAKADGEKQTKASLKTARSKAKSKALKTLKKAKVNREYDRVFSGFSMKLPASEIPKLLAVKEVKAVYPNATYKPDSVKGKDVTLAADAIYPQMDKSAPFIGADQAWKSGYTGKGIKVAVIDTGVDYTHPDLKNNFGPYKGYDFVDNDYDPQETPTGDPRGGATDHGTHVAGTIAANGQIKGVAPEATLLAYRVLGPGGSGTTENVIAGIEKAVADGAKVMNLSLGNSLNSPDYATSIALDWAMAEGVVAVTSNGNSGPENWTVGSPGTSRVAISVGASQLPYNEYSVTLPSYSSAKVMGYQEEKDLEALNGQEVELVEAGLGQADDFSGKDVKGKVAVIQRGVIPFVDKAENAKNAGAIGAVIYNNATGEIEANVMGMAVPTVKLSKEEGEKLVQQIKEGKHSVVFSFKLDKKLGETIASFSSRGPVMDTWMIKPDVSAPGVNIVSTIPTHDPKNPYGYGSKQGTSMASPHVAGTAAILKQAKPDWTPEQIKGVLMNTAEKLTDENGKPLPHNTQGAGSIRIMEALKASSIVTPGSHSYGTFLKDKGKQTKKQAFTIENLSSHRKAYQLEYSFKGTGITVSGTERVVVPANQTGKAAAKVTVNSAKTKAGTYEGTVYIREDGRKVAEIPLLLIVKEPDYPRVTSVTVEPGAKQGAYTIEAYLPGGAEELAFLVYDENLNLLGQAGVYKNQGKGYQSYQWNGKINDAASLKSGKYYMLAYASAKGKSSYVLTEDPFIVE
KB-SP 806FreeFreeLinearLNoneDerived from Bacillus sp. KB111 strainHaloprotease60 °CN.A.10 (Enzyme Activity)N.A.ZymographyEDTA + Tris-HCl + 0.5 M NaCl+ azocaseinIn VitroGenBank id: KUL11341.1NoneKB-SP exhibited more than 50% of the highest activity at pH=6.5–10
4754
359102762022
MRKSIVRYFVMAFILLFALSTFLTGVQATSVPDKKSPELEKAEIYGDIDVTSDKQTTVIVELKEKSLAEAKADGEKQTKASLKTARSKAKSKALKTLKKAKVNREYDRVFSGFSMKLPASEIPKLLAVKEVKAVYPNATYKPDSVKGKDVTLAADAIYPQMDKSAPFIGADQAWKSGYTGKGIKVAVIDTGVDYTHPDLKNNFGPYKGYDFVDNDYDPQETPTGDPRGGATDHGTHVAGTIAANGQIKGVAPEATLLAYRVLGPGGSGTTENVIAGIEKAVADGAKVMNLSLGNSLNSPDYATSIALDWAMAEGVVAVTSNGNSGPENWTVGSPGTSRVAISVGASQLPYNEYSVTLPSYSSAKVMGYQEEKDLEALNGQEVELVEAGLGQADDFSGKDVKGKVAVIQRGVIPFVDKAENAKNAGAIGAVIYNNATGEIEANVMGMAVPTVKLSKEEGEKLVQQIKEGKHSVVFSFKLDKKLGETIASFSSRGPVMDTWMIKPDVSAPGVNIVSTIPTHDPKNPYGYGSKQGTSMASPHVAGTAAILKQAKPDWTPEQIKGVLMNTAEKLTDENGKPLPHNTQGAGSIRIMEALKASSIVTPGSHSYGTFLKDKGKQTKKQAFTIENLSSHRKAYQLEYSFKGTGITVSGTERVVVPANQTGKAAAKVTVNSAKTKAGTYEGTVYIREDGRKVAEIPLLLIVKEPDYPRVTSVTVEPGAKQGAYTIEAYLPGGAEELAFLVYDENLNLLGQAGVYKNQGKGYQSYQWNGKINDAASLKSGKYYMLAYASAKGKSSYVLTEDPFIVE
KB-SP 806FreeFreeLinearLNoneDerived from Bacillus sp. KB111 strainHaloprotease50°CN.A.5 (Enzyme Activity)N.A.ZymographyEDTA + Tris-HCl + 0.5 M NaCl+ azocasein In VitroGenBank id: KUL11341.1NoneKB-SP exhibited more than 50% of the highest activity at pH=6.5–10
4761
357117552022
N.A.
R13 Fae393N.A.N.A.N.A.N.A.N.A.SyntheticXylanasepH 6.0 25 CelsiusN.A.23 (Half Life Activty)N.A.N.A.Phosphate bufferIn VitroNoneNoneN.A.
4762
357117552022
N.A.
R13 Fae393N.A.N.A.N.A.N.A.N.A.SyntheticXylanasepH 6.0 ,35°CN.A.16 (Half Life Activity)N.A.N.A.Phosphate bufferIn VitroNoneNoneN.A.
4766
351338602022
NDRAAAIIRADDLASTGYTGEGQIVGVADSGLDTGDLDRIHPDFEGRVKELYAIGRKGDASDPDGHGTHVAGSIVGTGKASDGOYKGMAPDAKLVFHSMLDEYGYLAGDVSDILEEAYADGARIHSDSWGVDDDGEYGLDSFLFDQFLWEHPDMTALVAAGNAGIYGYETIGTPATAKNVIAVGASENDRPELDEDEADDPDEVAAFSSRGTTADGRLKPDLVAPGSYILSTRSSLAPDENFHGLFNAFYAYLSGTSMATPVLAGGVAQVRQFLQENGVDNPSGALIKAMLISGADDLNEDMRVQGFGRANLRRAIETGFVDEKKGLKTGDVATYRLNVTDDSQPLAITLAWTDYPASLAAERTLVNNLNLRVVTPSGETLNGNDFFHYPYDDEVDNLNNVEQVWIKHPEEGVYTVTVEGYNVPMGPQPYALAANG
mTSS436FreeFreeLinearLNoneDerived from preTSSCollagenolytic protease 75°CN.A.1.5 (Activity Half Life)N.A.N.A.10 mM CaCl2 at pH 9.0In Viro Study NoneNoneIn the presence of 10 mM CaCl2 at pH 9.0, mTSS retained more than 80% or 70% of the original activity after 8 h of incubation at 60°C or 70°C
4767
351338602022
NDRAAAIIRADDLASTGYTGEGQIVGVADSGLDTGDLDRIHPDFEGRVKELYAIGRKGDASDPDGHGTHVAGSIVGTGKASDGOYKGMAPDAKLVFHSMLDEYGYLAGDVSDILEEAYADGARIHSDSWGVDDDGEYGLDSFLFDQFLWEHPDMTALVAAGNAGIYGYETIGTPATAKNVIAVGASENDRPELDEDEADDPDEVAAFSSRGTTADGRLKPDLVAPGSYILSTRSSLAPDENFHGLFNAFYAYLSGTSMATPVLAGGVAQVRQFLQENGVDNPSGALIKAMLISGADDLNEDMRVQGFGRANLRRAIETGFVDEKKGLKTGDVATYRLNVTDDSQPLAITLAWTDYPASLAAERTLVNNLNLRVVTPSGETLNGNDFFHYPYDDEVDNLNNVEQVWIKHPEEGVYTVTVEGYNVPMGPQPYALAANG
mTSS436FreeFreeLinearLNoneDerived from preTSSCollagenolytic protease 60°CN.A.2 (Activity Half Life)N.A.N.A.10 mM CaCl2 at pH 11.0 In Viro Study NoneNoneIn the presence of 10 mM CaCl2 at pH 9.0, mTSS retained more than 80% or 70% of the original activity after 8 h of incubation at 60°C or 70°C
4768
351338602022
NDRAAAIIRADDLASTGYTGEGQIVGVADSGLDTGDLDRIHPDFEGRVKELYAIGRKGDASDPDGHGTHVAGSIVGTGKASDGOYKGMAPDAKLVFHSMLDEYGYLAGDVSDILEEAYADGARIHSDSWGVDDDGEYGLDSFLFDQFLWEHPDMTALVAAGNAGIYGYETIGTPATAKNVIAVGASENDRPELDEDEADDPDEVAAFSSRGTTADGRLKPDLVAPGSYILSTRSSLAPDENFHGLFNAFYAYLSGTSMATPVLAGGVAQVRQFLQENGVDNPSGALIKAMLISGADDLNEDMRVQGFGRANLRRAIETGFVDEKKGLKTGDVATYRLNVTDDSQPLAITLAWTDYPASLAAERTLVNNLNLRVVTPSGETLNGNDFFHYPYDDEVDNLNNVEQVWIKHPEEGVYTVTVEGYNVPMGPQPYALAANG
mTSS436FreeFreeLinearLNoneDerived from preTSSCollagenolytic protease N.A.N.A.>12 (Activity Half Life)N.A.N.A.10 mM CaCl2 at pH 7.5In Viro Study NoneNoneIn the presence of 10 mM CaCl2 at pH 9.0, mTSS retained more than 80% or 70% of the original activity after 8 h of incubation at 60°C or 70°C
4769
351338602022
NDRAAAIIRADDLASTGYTGEGQIVGVADSGLDTGDLDRIHPDFEGRVKELYAIGRKGDASDPDGHGTHVAGSIVGTGKASDGOYKGMAPDAKLVFHSMLDEYGYLAGDVSDILEEAYADGARIHSDSWGVDDDGEYGLDSFLFDQFLWEHPDMTALVAAGNAGIYGYETIGTPATAKNVIAVGASENDRPELDEDEADDPDEVAAFSSRGTTADGRLKPDLVAPGSYILSTRSSLAPDENFHGLFNAFYAYLSGTSMATPVLAGGVAQVRQFLQENGVDNPSGALIKAMLISGADDLNEDMRVQGFGRANLRRAIETGFVDEKKGLKTGDVATYRLNVTDDSQPLAITLAWTDYPASLAAERTLVNNLNLRVVTPSGETLNGNDFFHYPYDDEVDNLNNVEQVWIKHPEEGVYTVTVEGYNVPMGPQPYALAANG
mTSS436FreeFreeLinearLNoneDerived from preTSSCollagenolytic protease 70°CN.A.6 (Activity Half Life)N.A.N.A.pH 9In Viro Study NoneNoneIn the presence of 10 mM CaCl2 at pH 9.0, mTSS retained more than 80% or 70% of the original activity after 8 h of incubation at 60°C or 70°C
4891
346303782021
LAEAKVLANRELDKYGVSDYYKNLINNAKTVEGVKALIDEILAALPGPVEDAITAAIGRVADTVGTGPTNSEAIPALTAAETGHTSQVVPGDTMQTRHVKNYHSRSESTIENFLCRSACVYFTEYENSGAKRYAEWVLTPRQAAQLRRKLEFFTYVRFDLELTFVITSTQQPSTTQNQDAQILTHQIMYVPPGGPVPDKVDSYVWQTSTNPSVFWTEGNAPPRMSIPFLSIGNAYSNFYDGWSEFSRNGVYGINTLNNMGTLYARHVNAGSTGPIKSTIRIYFKPKHVKAWIPRPPRLCQYEKAKNVNFQPSGVTTTRQSITTMTNTGAF
ABD-VP1330ABDFreeLinearLNoneSyntheticTreatment of Coxsackievirus B3 (Cvb3)-Induced Viral Myocarditis 1h at RT0.25 μg/μL280Murine serum proteaseELISAMurine serumIn VivoNoneNoneABD-VP1 increased the 28-day survival rate from about 40% (VP1) to 73%
4892
346303782021
GPVEDAITAAIGRVADTVGTGPTNSEAIPALTAAETGHTSQVVPGDTMQTRHVKNYHSRSESTIENFLCRSACVYFTEYENSGAKRYAEWVLTPRQAAQLRRKLEFFTYVRFDLELTFVITSTQQPSTTQNQDAQILTHQIMYVPPGGPVPDKVDSYVWQTSTNPSVFWTEGNAPPRMSIPFLSIGNAYSNFYDGWSEFSRNGVYGINTLNNMGTLYARHVNAGSTGPIKSTIRIYFKPKHVKAWIPRPPRLCQYEKAKNVNFQPSGVTTTRQSITTMTNTGAF
VP1 vaccine284FreeFreeLinearLNoneSyntheticTreatment of Coxsackievirus B3 (Cvb3)-Induced Viral Myocarditis 1h at RT0.25 μg/μL<15Murine serum proteaseELISAMurine serumIn VivoNoneNoneABD-VP1 increased the 28-day survival rate from about 40% (VP1) to 73%
4898
344590352021
EFKLELVEKLFAEDTEAKNPFSTQDTDLDLEMLAPYIPMDDDFQLRSFDQLSPLESSSASPESASPQSTVTVFQQTQIQEPTANATTTTATTDELKTVTKDRMEDIKILIASPSPTHIHKETT
CODD120FreeFreeLinearLFLAG tagC-Terminal oxygen-dependent degradation domainRegulates gene expressionN.A.N.A.5.8‐Fold Increase Cells lysate proteaseCHX assay, Western blottingHEK293 Flp‐In T‐REx cells lysate after neddylation inhibitionIn VitroNoneNoneN.A.
4935
339188532021
TSQVRQNYHQDSEAAINRQINLELYASYVYLSMSYYFDRDDVALKNFAKYFLHQSHEEREHAEKLMKLQNQRGGRIFLQDIKKPDCDDWESGLNAMECALHLEKNVNQSLLELHKLATDKNDPHLCDFIETHYLNEQVKAIKELGDHVTNLRKMGAPESGLAEYLFDKHTLG
HFn/DOX172FreeFreeLinearLNoneSyntheticAntitumorBlood samples were collected from the retro orbital sinus at fixed time points (10, 30 min, 1, 2, 4, 8, 12, 24, 36, 48 h) at 37 °C3.0 mg/kg3.07 ± 0.06SD rats serum proteaseFluorescence spectrometrySD rats serumIn VivoPDB id: 3AJONoneIC50 (μg mL−1) = 0.49 ± 0.11
4936
339188532021
TSQVRQNYHQDSEAAINRQINLELYASYVYLSMSYYFDRDDVALKNFAKYFLHQSHEEREHAEKLMKLQNQRGGRIFLQDIKKPDCDDWESGLNAMECALHLEKNVNQSLLELHKLATDKNDPHLCDFIETHYLNEQVKAIKELGDHVTNLRKMGAPESGLAEYLFDKHTLG-GGGSGGGTGGGSGGG-GFLG-ASPAAPAPAPAAPAPSAPAASPAAPAPASPAAPAPSAPA-GGSGG
HFn-PAS/DOX235Free15aa linker, enzyme cleavable site, PAS(40), 5 aa flexible linker conjugated at C terminus LinearLNoneSyntheticAntitumorBlood samples were collected from the retro orbital sinus at fixed time points (10, 30 min, 1, 2, 4, 8, 12, 24, 36, 48 h) at 37 °C3.0 mg/kg14.96 ± 0.29SD rats serum proteaseFluorescence spectrometrySD rats serumIn VivoPDB id: 3AJONoneIC50 (μg mL−1) = 0.38 ± 0.09
4937
339188532021
TSQVRQNYHQDSEAAINRQINLELYASYVYLSMSYYFDRDDVALKNFAKYFLHQSHEEREHAEKLMKLQNQRGGRIFLQDIKKPDCDDWESGLNAMECALHLEKNVNQSLLELHKLATDKNDPHLCDFIETHYLNEQVKAIKELGDHVTNLRKMGAPESGLAEYLFDKHTLG-GGGSGGGTGGGSGGG-GFLG-ASPAAPAPAPAAPAPSAPAASPAAPAPASPAAPAPSAPA-GGSGG-RGDK
HFn-GFLG-PAS-RGDK/DOX239FreeAdd RGDK tretapeptide to HFn-PAS C-terminusLinearLNoneSyntheticAntitumorBlood samples were collected from the retro orbital sinus at fixed time points (10, 30 min, 1, 2, 4, 8, 12, 24, 36, 48 h) at 37 °C3.0 mg/kg17.61 ± 0.39SD rats serum proteaseFluorescence spectrometrySD rats serumIn VivoPDB id: 3AJONoneIC50 (μg mL−1) = 0.17 ± 0.01
4938
339188532021
TSQVRQNYHQDSEAAINRQINLELYASYVYLSMSYYFDRDDVALKNFAKYFLHQSHEEREHAEKLMKLQNQRGGRIFLQDIKKPDCDDWESGLNAMECALHLEKNVNQSLLELHKLATDKNDPHLCDFIETHYLNEQVKAIKELGDHVTNLRKMGAPESGLAEYLFDKHTLG-GGGSGGGTGGGSGGG-PLGLAG-ASPAAPAPAPAAPAPSAPAASPAAPAPASPAAPAPSAPA-GGSGG-RGDK
HFn-PLGLAG-PAS-RGDK/DOX241FreeAdd RGDK tretapeptide to HFn-PAS C-terminus and substituite enzyme cleavable linker with PLGLAGLinearLNoneSyntheticAntitumorBlood samples were collected from the retro orbital sinus at fixed time points (10, 30 min, 1, 2, 4, 8, 12, 24, 36, 48 h) at 37 °C3.0 mg/kg18.93 ± 0.61SD rats serum proteaseFluorescence spectrometrySD rats serumIn VivoPDB id: 3AJONoneIC50 (μg mL−1) = 0.18 ± 0.04
4973
336563232021
PTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLTFKFYMPKKATELKHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLISNINVIVLELKGSETTFMCEYADETATIVEFLNRWITFSQSIISTLT
IL-2132FreeFreeCyclic (C57-C104 Disulfide Bond)LNoneSyntheticAnticancer, Autoimmune diseases treatmentSerum samples were collected at 10 min and 2, 6, 12, 20, and 36 h for group I and 1, 4, 8, 16, 24, and 48 h for group II by retro-orbital bleeding, . Serum samples were collected at 0, 2, 5, 20, 30, and 45 min for group I and 10 min and 1, 2, 4, 6, and 8 h for group II by retro-orbital bleeding0.6 mg/kg0.041 ± 0.006 (T1/2a )Mouse plasma proteaseSandwich ELISAMouse plasmaIn Vivopdb id: 5LQB and https://pubs.acs.org/doi/suppl/10.1021/acs.bioconjchem.1c00062/suppl_file/bc1c00062_si_001.pdfNoneKD (M) = (1.952 ± 0.130) × 10−8 for IL-2
4974
336563232021
PTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLTFKFYMPKKATELKHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLISNINVIVLELKGSETTFMCEYADETATIVEFLNRWITFCQSIISTLT-(ED)6-LPETGGGK
B6146FreeLys146 contains Fatty acid moiety which introduces 8-amino-3,6-dioxaoctanoic acid (AEEA) and glutamic acidCyclic (C57-C104 Disulfide Bond) In IL-2LNoneSyntheticAnticancer, Autoimmune diseases treatmentSerum samples were collected at 10 min and 2, 6, 12, 20, and 36 h for group I and 1, 4, 8, 16, 24, and 48 h for group II by retro-orbital bleeding, . Serum samples were collected at 0, 2, 5, 20, 30, and 45 min for group I and 10 min and 1, 2, 4, 6, and 8 h for group II by retro-orbital bleeding0.6 mg/kg0.613 ± 0.063(T1/2a )Mouse plasma proteaseSandwich ELISAMouse plasmaIn Vivopdb id: 5LQB and https://pubs.acs.org/doi/suppl/10.1021/acs.bioconjchem.1c00062/suppl_file/bc1c00062_si_001.pdfNoneKD (M) = (1.952 ± 0.130) × 10−8 for IL-2
4975
336563232021
PTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLTFKFYMPKKATELKHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLISNINVIVLELKGSETTFMCEYADETATIVEFLNRWITFCQSIISTLT-(ED)6-LPETGGGK
B6 control146FreeLys146 contains Fatty acid moiety which introduces 8-amino-3,6-dioxaoctanoic acid (AEEA) and glutamic acidCyclic (C57-C104 Disulfide Bond) In IL-2LNoneSyntheticAnticancer, Autoimmune diseases treatmentSerum samples were collected at 0, 5, and 30 min and 2, 6, and 12 h for group I and 2, 10, and 60 min and 4, 8, and 24 h for group II by retro-orbital bleeding0.6 mg/kg0.035 ± 0.014(T1/2a )Mouse plasma proteaseSandwich ELISAMouse plasmaIn Vivopdb id: 5LQB and https://pubs.acs.org/doi/suppl/10.1021/acs.bioconjchem.1c00062/suppl_file/bc1c00062_si_001.pdfNoneKD (M) = (1.952 ± 0.130) × 10−8 for IL-2
4976
336563232021
PTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLTFKFYMPKKATELKHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLISNINVIVLELKGSETTFMCEYADETATIVEFLNRWITFSQSIISTLT
IL-2132FreeFreeCyclic (C57-C104 Disulfide Bond)LNoneSyntheticAnticancer, Autoimmune diseases treatmentSerum samples were collected at 10 min and 2, 6, 12, 20, and 36 h for group I and 1, 4, 8, 16, 24, and 48 h for group II by retro-orbital bleeding, . Serum samples were collected at 0, 2, 5, 20, 30, and 45 min for group I and 10 min and 1, 2, 4, 6, and 8 h for group II by retro-orbital bleeding0.6 mg/kg0.273 ± 0.040(T1/2b)Mouse plasma proteaseSandwich ELISAMouse plasmaIn Vivopdb id: 5LQB and https://pubs.acs.org/doi/suppl/10.1021/acs.bioconjchem.1c00062/suppl_file/bc1c00062_si_001.pdfNoneKD (M) = (1.952 ± 0.130) × 10−8 for IL-2
4977
336563232021
PTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLTFKFYMPKKATELKHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLISNINVIVLELKGSETTFMCEYADETATIVEFLNRWITFCQSIISTLT-(ED)6-LPETGGGK
B6146FreeLys146 contains Fatty acid moiety which introduces 8-amino-3,6-dioxaoctanoic acid (AEEA) and glutamic acidCyclic (C57-C104 Disulfide Bond) In IL-2LNoneSyntheticAnticancer, Autoimmune diseases treatmentSerum samples were collected at 10 min and 2, 6, 12, 20, and 36 h for group I and 1, 4, 8, 16, 24, and 48 h for group II by retro-orbital bleeding, . Serum samples were collected at 0, 2, 5, 20, 30, and 45 min for group I and 10 min and 1, 2, 4, 6, and 8 h for group II by retro-orbital bleeding0.6 mg/kg3.595 ± 0.518(T1/2b)Mouse plasma proteaseSandwich ELISAMouse plasmaIn Vivopdb id: 5LQB and https://pubs.acs.org/doi/suppl/10.1021/acs.bioconjchem.1c00062/suppl_file/bc1c00062_si_001.pdfNoneKD (M) = (1.952 ± 0.130) × 10−8 for IL-2
4978
336563232021
PTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLTFKFYMPKKATELKHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLISNINVIVLELKGSETTFMCEYADETATIVEFLNRWITFCQSIISTLT-(ED)6-LPETGGGK
B6 control146FreeLys146 contains Fatty acid moiety which introduces 8-amino-3,6-dioxaoctanoic acid (AEEA) and glutamic acidCyclic (C57-C104 Disulfide Bond) In IL-2LNoneSyntheticAnticancer, Autoimmune diseases treatmentSerum samples were collected at 0, 5, and 30 min and 2, 6, and 12 h for group I and 2, 10, and 60 min and 4, 8, and 24 h for group II by retro-orbital bleeding0.6 mg/kg0.196 ± 0.114(T1/2b)Mouse plasma proteaseSandwich ELISAMouse plasmaIn Vivopdb id: 5LQB and https://pubs.acs.org/doi/suppl/10.1021/acs.bioconjchem.1c00062/suppl_file/bc1c00062_si_001.pdfNoneKD (M) = (1.952 ± 0.130) × 10−8 for IL-2
4979
336501552021
DYKDDDDKDYKDDDDKDYKDDDDKMDTARIAVVGAGVVGLSTAVCISKLVPRCSVTIISDKFTPDTTSDVAAGMLIPHTYPDTPIHTQKQWFRETFNHLFAIANSAEAGDAGVHLVSGWQIFQSTPTEEVPFWADVVLGFRKMTEAELKKFPQYVFGQAFTTLKCECPAYLPWLEKRIKGSGGWTLTRRIEDLWELHPSFDIVVNCSGLGSRQLAGDSKIFPVRGQVLQVQAPWVEHFIRDGSGLTYIYPGTSHVTLGGTRQKGDWNLSPDAENSREILSRCCALEPSLHGACNIREKVGLRPYRPGVRLQTELLARDGQRLPVVHHYGHGSGGISVHWGTALEAARLVSECVHALRTPIPKSNL
3XFLAG-hDASPO_3413653XFLAG labellingFreeLinearLNoneFound in the hippocampus of female patients affected by Alzheimer's diseaseDegradation Of D-Aspartate ( D-Asp)10 hours2 μg≈ 100U87 cells lysate proteaseWestern blottingU87 cells lysate with cycloheximide (CHX)In VivoNoneNoneN.A.
4980
336501552021
DYKDDDDKDYKDDDDKDYKDDDDKMRPARHWETRFGARDFGGFQDCFFRDRLMDTARIAVVGAGVVGLSTAVCISKLVPRCSVTIISDKFTPDTTSDVAAGMLIPHTYPDTPIHTQKQWFRETFNHLFAIANSAEAGDAGVHLVSGWQIFQSTPTEEVPFWADVVLGFRKMTEAELKKFPQYVFGQAFTTLKCECPAYLPWLEKRIKGSGGWTLTRRIEDLWELHPSFDIVVNCSGLGSRQLAGDSKIFPVRGQVLQVQAPWVEHFIRDGSGLTYIYPGTSHVTLGGTRQKGDWNLSPDAENSREILSRCCALEPSLHGACNIREKVGLRPYRPGVRLQTELLARDGQRLPVVHHYGHGSGGISVHWGTALEAARLVSECVHALRTPIPKSNL
3XFLAG-hDASPO_3693933XFLAG labellingFreeLinearLNoneFound in the hippocampus of female patients affected by Alzheimer's diseaseDegradation Of D-Aspartate ( D-Asp)10 hours2 μg≈ 100U87 cells lysate proteaseWestern blottingU87 cells lysate with cycloheximide (CHX)In VivoNoneNoneN.A.
5005
333915052021
APGSYTGSAPGVASGFTFSNYGMHIYYDSSKMNYADTVKGSHYVVDVGGGGSGGGGSGGGGSQASQDIGNWLAGATSLADLQAYNTPWTAPGSYTGSAPGAGCKNFFWKTFTSC
[125I]SST-scFv8D3115125I labeledscFv of 8D3 is added to SSTCyclic (Disulfide Bond Bw C-C Of SST)LSerine, threonine and glycine were added to the linker SyntheticTreatment of Alzheimer's diseasesEight microliter blood samples from the tail vein were obtained at 0.5, 1, 2, 4, 6 and 24-h post injection0.44±0.08 MBq6Mice plasma proteaseRadioactivity assayMice plasmaIn VivoNoneNoneThe measured activation of neprilysin by SST-scFv8D3 preserved around 70% of the activation obtained by SST alone 
5006
333875932021
CDLPQTHSLGSRRTLMLLAQMRKISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE
Wild-type (IFN)165FreeFreeLinearLNoneHuman derivedAntiviral, AntiproliferativeBlood samples were taken at different times post-injection 100000 U0.9 ± 0.1 (T1/2 Elimination)Rats plasma proteaseSandwich ELISARats plasma In VivoPDB id: 1ITFNoneAntiviral SBA (IU/ng) = 201 ± 9 in wild-type IFN, Antiproliferative SBA (IU/ng) = 240 ± 50
5007
333875932021
APARSPSPSTQPWECDLPQTHSLGSRRTLMLLAQMRRISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE
GMOP-IFN179GM-CSF O-glycosylated PeptideFreeLinearLNoneSyntheticAntiviral, AntiproliferativeBlood samples were taken at different times post-injection 100000 U3.0 ± 0.4(T1/2 Elimination)Rats plasma proteaseSandwich ELISARats plasma In VivoPDB id: 1ITFNoneAntiviral SBA (IU/ng) = 190 ± 30 in GMOP-IFN, Antiproliferative SBA (IU/ng) = 280 ± 40 
5008
333875932021
APARSPSPTPTPTPT-CDLPQTHSLGSRRTLMLLAQMRRISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE
mGMOP-IFN180Modified GOMPFreeLinearLNoneSyntheticAntiviral, AntiproliferativeBlood samples were taken at different times post-injection 100000 U2.5 ± 0.2 (T1/2 Elimination)Rats plasma proteaseSandwich ELISARats plasmaIn VivoPDB id: 1ITFNoneAntiviral SBA (IU/ng) = 280 ± 50 in mGMOP-IFN, Antiproliferative SBA (IU/ng = 95 ± 5 
5037
320786722020
KTRHYFIAAVERLWDYGMSSSPHVLRNRAQSGSVPQFKKVVFQEFTDGSFTQPLYRGELNEHLGLLGPYIRAEVEDNIMVTFRNQASRPYSFYSSLISYEEDQRQGAEPRKNFVKPNETKTYFWKVQHHMAPTKDEFDCKAWAYFSDVDLEKDVHSGLIGPLLVCHTNTLNPAHGRQVTVQEFALFFTIFDETKSWYFTENMERNCRAPCNIQMEDPTFKENYRFHAINGYIMDTLPGLVMAQDQRIRWYLLSMGSNENIHSIHFSGHVFTVRKKEEYKMALYNLYPGVFETVEMLPSKAGIWRVECLIGEHLHAGMSTLFLVYSNKCQTPLGMASGHIRDFQITASGQYGQWAPKLARLHYSGSINAWSTKEPFSWIKVDLLAPMIIHGIKTQGARQKFSSLYISQFIIMYSLDGKKWQTYRGNSTGTLMVFFGNVDSSGIKHNIFNPPIIARYIRLHPTHYSIRSTLRMELMGCDLNSCSMPLGMESKAISDAQITASSYFTNMFATWSPSKARLHLQGRSNAWRPQVNNPKEWLQVDFQKTMKVTGVTTQGVKSLLTSMYVKEFLISSSQDGHQWTLFFQNGKVKVFQGNQDSFTPVVNSLDPPLLTRYLRIHPQSWVHQIALRMEVLGCEAQDLYDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPG
rFVIIIFc865FreeIgG1 FcLinearLNoneSyntheticRole In ClottingN.A.200 IU/kg16.4HemA mice plasma proteasechromogenic activity assaysHemA mice plasmaIn VivoPDB id : 5K8D, https://pmc.ncbi.nlm.nih.gov/articles/instance/7180082/bin/bloodBLD2019001292-suppl1.pdfNoneED50 values for BIVV001 (7.5 IU/kg) and rFVIII (7.9 IU/kg) were similar
5038
320786722020
KTRHYFIAAVERLWDYGMSSSPHVLRNRAQSGSVPQFKKVVFQEFTDGSFTQPLYRGELNEHLGLLGPYIRAEVEDNIMVTFRNQASRPYSFYSSLISYEEDQRQGAEPRKNFVKPNETKTYFWKVQHHMAPTKDEFDCKAWAYFSDVDLEKDVHSGLIGPLLVCHTNTLNPAHGRQVTVQEFALFFTIFDETKSWYFTENMERNCRAPCNIQMEDPTFKENYRFHAINGYIMDTLPGLVMAQDQRIRWYLLSMGSNENIHSIHFSGHVFTVRKKEEYKMALYNLYPGVFETVEMLPSKAGIWRVECLIGEHLHAGMSTLFLVYSNKCQTPLGMASGHIRDFQITASGQYGQWAPKLARLHYSGSINAWSTKEPFSWIKVDLLAPMIIHGIKTQGARQKFSSLYISQFIIMYSLDGKKWQTYRGNSTGTLMVFFGNVDSSGIKHNIFNPPIIARYIRLHPTHYSIRSTLRMELMGCDLNSCSMPLGMESKAISDAQITASSYFTNMFATWSPSKARLHLQGRSNAWRPQVNNPKEWLQVDFQKTMKVTGVTTQGVKSLLTSMYVKEFLISSSQDGHQWTLFFQNGKVKVFQGNQDSFTPVVNSLDPPLLTRYLRIHPQSWVHQIALRMEVLGCEAQDLYDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPG
rFVIIIFc865FreeIgG1 FcLinearLNoneSyntheticRole In ClottingN.A.200 IU/kg13.2VWF Het mice plasma proteasechromogenic activity assaysVWF Het mice plasmaIn VivoPDB id : 5K8D, https://pmc.ncbi.nlm.nih.gov/articles/instance/7180082/bin/bloodBLD2019001292-suppl1.pdfNoneED50 values for BIVV001 (7.5 IU/kg) and rFVIII (7.9 IU/kg) were similar
5039
320786722020
KTRHYFIAAVERLWDYGMSSSPHVLRNRAQSGSVPQFKKVVFQEFTDGSFTQPLYRGELNEHLGLLGPYIRAEVEDNIMVTFRNQASRPYSFYSSLISYEEDQRQGAEPRKNFVKPNETKTYFWKVQHHMAPTKDEFDCKAWAYFSDVDLEKDVHSGLIGPLLVCHTNTLNPAHGRQVTVQEFALFFTIFDETKSWYFTENMERNCRAPCNIQMEDPTFKENYRFHAINGYIMDTLPGLVMAQDQRIRWYLLSMGSNENIHSIHFSGHVFTVRKKEEYKMALYNLYPGVFETVEMLPSKAGIWRVECLIGEHLHAGMSTLFLVYSNKCQTPLGMASGHIRDFQITASGQYGQWAPKLARLHYSGSINAWSTKEPFSWIKVDLLAPMIIHGIKTQGARQKFSSLYISQFIIMYSLDGKKWQTYRGNSTGTLMVFFGNVDSSGIKHNIFNPPIIARYIRLHPTHYSIRSTLRMELMGCDLNSCSMPLGMESKAISDAQITASSYFTNMFATWSPSKARLHLQGRSNAWRPQVNNPKEWLQVDFQKTMKVTGVTTQGVKSLLTSMYVKEFLISSSQDGHQWTLFFQNGKVKVFQGNQDSFTPVVNSLDPPLLTRYLRIHPQSWVHQIALRMEVLGCEAQDLYDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPG
rFVIIIFc865FreeIgG1 FcLinearLNoneSyntheticRole In ClottingN.A.200 IU/kg1.85DKO mice plasma proteasechromogenic activity assaysDKO mice plasmaIn VivoPDB id : 5K8D, https://pmc.ncbi.nlm.nih.gov/articles/instance/7180082/bin/bloodBLD2019001292-suppl1.pdfNoneED50 values for BIVV001 (7.5 IU/kg) and rFVIII (7.9 IU/kg) were similar
5040
320786722020
KTRHYFIAAVERLWDYGMSSSPHVLRNRAQSGSVPQFKKVVFQEFTDGSFTQPLYRGELNEHLGLLGPYIRAEVEDNIMVTFRNQASRPYSFYSSLISYEEDQRQGAEPRKNFVKPNETKTYFWKVQHHMAPTKDEFDCKAWAYFSDVDLEKDVHSGLIGPLLVCHTNTLNPAHGRQVTVQEFALFFTIFDETKSWYFTENMERNCRAPCNIQMEDPTFKENYRFHAINGYIMDTLPGLVMAQDQRIRWYLLSMGSNENIHSIHFSGHVFTVRKKEEYKMALYNLYPGVFETVEMLPSKAGIWRVECLIGEHLHAGMSTLFLVYSNKCQTPLGMASGHIRDFQITASGQYGQWAPKLARLHYSGSINAWSTKEPFSWIKVDLLAPMIIHGIKTQGARQKFSSLYISQFIIMYSLDGKKWQTYRGNSTGTLMVFFGNVDSSGIKHNIFNPPIIARYIRLHPTHYSIRSTLRMELMGCDLNSCSMPLGMESKAISDAQITASSYFTNMFATWSPSKARLHLQGRSNAWRPQVNNPKEWLQVDFQKTMKVTGVTTQGVKSLLTSMYVKEFLISSSQDGHQWTLFFQNGKVKVFQGNQDSFTPVVNSLDPPLLTRYLRIHPQSWVHQIALRMEVLGCEAQDLYDKTHTCPPCPAPELL
rFVIII654FreeFreeLinearLNoneSyntheticRole In ClottingN.A.125 IU/kg7.63HemA mice plasma proteasechromogenic activity assaysHemA mice plasmaIn VivoPDB id : 5K8D, https://pmc.ncbi.nlm.nih.gov/articles/instance/7180082/bin/bloodBLD2019001292-suppl1.pdfNoneED50 values for BIVV001 (7.5 IU/kg) and rFVIII (7.9 IU/kg) were similar
5041
320786722020
KTRHYFIAAVERLWDYGMSSSPHVLRNRAQSGSVPQFKKVVFQEFTDGSFTQPLYRGELNEHLGLLGPYIRAEVEDNIMVTFRNQASRPYSFYSSLISYEEDQRQGAEPRKNFVKPNETKTYFWKVQHHMAPTKDEFDCKAWAYFSDVDLEKDVHSGLIGPLLVCHTNTLNPAHGRQVTVQEFALFFTIFDETKSWYFTENMERNCRAPCNIQMEDPTFKENYRFHAINGYIMDTLPGLVMAQDQRIRWYLLSMGSNENIHSIHFSGHVFTVRKKEEYKMALYNLYPGVFETVEMLPSKAGIWRVECLIGEHLHAGMSTLFLVYSNKCQTPLGMASGHIRDFQITASGQYGQWAPKLARLHYSGSINAWSTKEPFSWIKVDLLAPMIIHGIKTQGARQKFSSLYISQFIIMYSLDGKKWQTYRGNSTGTLMVFFGNVDSSGIKHNIFNPPIIARYIRLHPTHYSIRSTLRMELMGCDLNSCSMPLGMESKAISDAQITASSYFTNMFATWSPSKARLHLQGRSNAWRPQVNNPKEWLQVDFQKTMKVTGVTTQGVKSLLTSMYVKEFLISSSQDGHQWTLFFQNGKVKVFQGNQDSFTPVVNSLDPPLLTRYLRIHPQSWVHQIALRMEVLGCEAQDLYDKTHTCPPCPAPELL
rFVIII654FreeFreeLinearLNoneSyntheticRole In ClottingN.A.200 IU/kg5.43VWF Het mice plasma proteasechromogenic activity assaysVWF Het mice plasmaIn VivoPDB id : 5K8D, https://pmc.ncbi.nlm.nih.gov/articles/instance/7180082/bin/bloodBLD2019001292-suppl1.pdfNoneED50 values for BIVV001 (7.5 IU/kg) and rFVIII (7.9 IU/kg) were similar
5042
320786722020
KTRHYFIAAVERLWDYGMSSSPHVLRNRAQSGSVPQFKKVVFQEFTDGSFTQPLYRGELNEHLGLLGPYIRAEVEDNIMVTFRNQASRPYSFYSSLISYEEDQRQGAEPRKNFVKPNETKTYFWKVQHHMAPTKDEFDCKAWAYFSDVDLEKDVHSGLIGPLLVCHTNTLNPAHGRQVTVQEFALFFTIFDETKSWYFTENMERNCRAPCNIQMEDPTFKENYRFHAINGYIMDTLPGLVMAQDQRIRWYLLSMGSNENIHSIHFSGHVFTVRKKEEYKMALYNLYPGVFETVEMLPSKAGIWRVECLIGEHLHAGMSTLFLVYSNKCQTPLGMASGHIRDFQITASGQYGQWAPKLARLHYSGSINAWSTKEPFSWIKVDLLAPMIIHGIKTQGARQKFSSLYISQFIIMYSLDGKKWQTYRGNSTGTLMVFFGNVDSSGIKHNIFNPPIIARYIRLHPTHYSIRSTLRMELMGCDLNSCSMPLGMESKAISDAQITASSYFTNMFATWSPSKARLHLQGRSNAWRPQVNNPKEWLQVDFQKTMKVTGVTTQGVKSLLTSMYVKEFLISSSQDGHQWTLFFQNGKVKVFQGNQDSFTPVVNSLDPPLLTRYLRIHPQSWVHQIALRMEVLGCEAQDLYDKTHTCPPCPAPELL
rFVIII654FreeFreeLinearLNoneSyntheticRole In ClottingN.A.150 IU/kg0.23DKO mice plasma proteasechromogenic activity assaysDKO mice plasmaIn VivoPDB id : 5K8D, https://pmc.ncbi.nlm.nih.gov/articles/instance/7180082/bin/bloodBLD2019001292-suppl1.pdfNoneED50 values for BIVV001 (7.5 IU/kg) and rFVIII (7.9 IU/kg) were similar
5057
332039162020
VRERGPQRVAAHITGTRGRSNTLSSPNSKNEKALGRKINSWESSRSGHSFLSNLHLRNGELVIHEKGFYYIYSQTYFRFQEEIKENTKNDKQMVQYIYKYTSYPDPILLMKSARNSCWSKDAEYGLYSIYQGGIFELKENDRIFVSVTNEHLIDMDHEASFFGAFLVG
Native TRAIL168FreeFreeLinearLNoneSyntheticAnticancerBlood samples (25–30 μL) were collected at 5, 15, 30, 60, 180, 360, 720 min, and 24 h0.01 mg/mL3.4 ± 1.1 BALB/c wild type mice plasma proteaseWestern blottingBALB/c wild type mice plasmaIn VivoPDB id: 1D0GNoneKD (M) = (6.02 ± 1.99) × 10–8 (Binding kinetics of TRAIL-ATNC and TRAIL against TRAIL receptor DR5.)
5058
332039162020
VRERGPQRVAAHITGTRGRSNTLSSPNSKNEKALGRKINSWESSRSGHSFLSNLHLRNGELVIHEKGFYYIYSQTYFRFQEEIKENTKNDKQMVQYIYKYTSYPDPILLMKSARNSCWSKDAEYGLYSIYQGGIFELKENDRIFVSVTNEHLIDMDHEASFFGAFLVG-GSGGGSG
TRAIL-ATNC168FreeTRAIL joined with ATNC using flexible linkers consisting of small amino acids (GSGGGSG) that could form a bridge between the C-terminal of TRAIL and the triple helixLinearLNoneSyntheticAnticancerBlood samples (25–30 μL) were collected at 5, 15, 30, 60, 180, 360, 720 min, and 24 h1 mg/mL56.1 ± 5.8BALB/c wild type mice plasma proteaseWestern blottingBALB/c wild type mice plasmaIn VivoPDB id: 1D0GNoneKD (M) = (2.56 ± 2.58) × 10–10 (Binding kinetics of TRAIL-ATNC and TRAIL against TRAIL receptor DR5.)
5059
332039162020
VRERGPQRVAAHITGTRGRSNTLSSPNSKNEKALGRKINSWESSRSGHSFLSNLHLRNGELVIHEKGFYYIYSQTYFRFQEEIKENTKNDKQMVQYIYKYTSYPDPILLMKSARNSCWSKDAEYGLYSIYQGGIFELKENDRIFVSVTNEHLIDMDHEASFFGAFLVG-GSGGGSG
TRAIL-ATNCIL4rP168FreeTRAIL joined with ATNC using flexible linkers consisting of small amino acids (GSGGGSG) that could form a bridge between the C-terminal of TRAIL and the triple helix followed by (MMP2) cleavage site (GPLGLAG) then IL4rP (CRKRLDRNC)LinearLNoneSyntheticAnticancerBlood samples (25–30 μL) were collected at 5, 15, 30, 60, 180, 360, 720 min, and 24 h1 mg/mL53.6 ± 5.8BALB/c wild type mice plasma proteaseWestern blottingBALB/c wild type mice plasmaIn VivoPDB id: 1D0GNoneIC50 value of 0.48 nM for TRAIL-ATNCIL4rP
5066
330570632020
GTSHLVKCAEKEKTFCVNGGECFMVKDLSNPSRYLCKCPNEFTGDRCQNYVMASFLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSQEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKGLPSSIEKTISKAKGQPREPQVYTFPPSQEEMTKNQVSLRCLVKGFYPSDIAVEWESNGQPENNYKTTKPVLDSDGSFRLESRLTVDKSRWQEGNVFSCSVMHEALHNHYTQKSLSLS
NRG1-MFc268Freefusion of the C-terminus of NRG1 to the N-terminus of the Fc fragmentLinearLNoneSyntheticHer4-Selective AgonismOvernight at 4 °C10 μg/mL1.4Mouse serum proteaseELISAMouse serumIn VitroPDB ID: 3U7UNoneHER4 binding KD = 640 nM
5067
330570632020
GTSELVKCAEKEKTFCVNGGECFMVGDLSNHSRYLCKCPNEFTGDRCQNYVMASFLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSQEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKGLPSSIEKTISKAKGQPREPQVYTFPPSQEEMTKNQVSLRCLVKGFYPSDIAVEWESNGQPENNYKTTKPVLDSDGSFRLESRLTVDKSRWQEGNVFSCSVMHEALHNHYTQKSLSLS
1F7-MFc268FreeC-terminus of 1F7 is directly fused to the Fc fragmentLinearLSmall set of mutations, including His2, Lys24, and P29SyntheticHer4-Selective AgonismOvernight at 4 °C10 μg/mL6.6Mouse serum proteaseELISAMouse serumIn VitroPDB ID: 3U7UNoneEC50 (nM) = 0.4 for 1F7 in HER2/HER4 Luc
5069
330570632020
GGGGSGGGGSGTSHLVKCAEKEKTFCVNGGECFMVKDLSNPSRYLCKCPNEFTGDRCQNYVMASFGGGGSGGGGSGTSELVKCAEKEKTFCVNGGECFMVGDLSNHSRYLCKCPNEFTGDRCQNYVMASF
ALM6-1F7130FreeC-terminus of ALM6 is directly fused to 1F7LinearLSmall set of mutations, including His2, Lys24, and P29SyntheticHer4-Selective AgonismOvernight at 4 °C10 μg/mL6.6Mouse serum proteaseELISAMouse serumIn VitroNoneNoneEC50 (nM) = 0.4 for 1F7 in HER2/HER4 Luc
5100
328478502020
IRDVPPADQEKLFIQKLRQCCVLFDFVSDPLSDLKWKEVKRAALSEMVEYITHNRNVITEPIYPEVVHMFAVNMFRTLPPSSNPTGAEFDPEEDEPTLEAAWPHLQLVYEFFLRFLESPDFQPNIAKKYIDQKFVLQLLELFDSEDPRERDFLKTTLHRIYGKFLGLRAYIRKQINNIFYRFIYETEHHNGIAELLEILGSIINGFALPLKEEHKIFLLKVLLPLHKVKSLSVYHPQLAYCVVQFLEKDSTLTEPVVMALLKYWPKTHSPKEVMFLNELEEILDVIEPSEFVKIMEPLFRQLAKCVSSPHFQVAERALYYWNNEYIMSLISDNAAKILPIMFPSLYRNSKTHWNKTIHGLIYNALKLFMEMNQKLFDDCTQQFKAEKLKEKLKMKEREEAWVKIENL
PPP2R5A407FreeFreeLinearLBlue fluorescent protein (BFP) labelingencoded by the PPP2R5A gene in humansAntiviral48 hours250 ng~2293T Cell Line Lysate Proteaseflow cytometry293T cell line lysate with VifIn VivoPDB id = 2IAENoneN.A.
5113
328086592020
GEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGKGGGSGGGSGGGSLRKHNCLQRRCMPLHSRVPFP
Fc-ELA-21266Fc joined with ELA-21 by linker (GGGS)3FreeLinearLNoneDerived from ELAAnti-Heart Failure ActivityAbout 10 μl of blood was collected at each time point of 0, 1, 2, 4, 8, 24, 32, 48, 56, and 72 h after administration5 mg/kg∼44Mice plasma proteaseWestern blottingMice plasmaIn Vivohttps://sci-hub.se/10.1016/j.ijcard.2019.04.089NoneEC50 =1.58 nM (cAMP supression)
5115
328030732020
GSLTSSERIDKQIRYILDGISALRKETCNKSNMCESSKEALAENNLNLPKMAEKDGCFQSGFNEETCLVKIITGLLEFEVYLEYLQNRFESSEEQARAVQMSTKVLIQFLQKKAKNL-AzF-AITTPDPTTNASLLTKLQAQNQWLQDMTTHLILRSFKEFLQSSLRALRQM
Pal-Rb169FreeFreeLinearLConjugation of palmitic acid at AzF, biotinylated labelling, , (AzF) was incorporated into the position 126 on the repebody followed by lipid conjugationSyntheticAntitumorBlood was collected in predetermined time points postinjection (n = 5; 0.05, 0.5, 1, 2, 4, 6, 12 and 24 h10 mg/kg10.7 (Elimination Half-Life)Mice plasma proteaseSandwich ELISAMice plasmaIn VivoPDB ID: 4J4LNoneThe tumor size remained around 200 mm3 until 27 days when Pal-Rb was administered (p < 0.01), whereas tumor continued to grow over 600 mm3 when WT-Rb and PBS were injected.
5116
328030732020
GSLTSSERIDKQIRYILDGISALRKETCNKSNMCESSKEALAENNLNLPKMAEKDGCFQSGFNEETCLVKIITGLLEFEVYLEYLQNRFESSEEQARAVQMSTKVLIQFLQKKAKNLDAITTPDPTTNASLLTKLQAQNQWLQDMTTHLILRSFKEFLQSSLRALRQM
WT-Rb168FreeFreeLinearLBiotinylationSyntheticAntitumorBlood was collected in predetermined time points postinjection (n = 5; 0.05, 0.5, 1, 2, 4, 6, 12 and 24 h10 mg/kg20 (Initial Half-Life)Mice plasma proteaseSandwich ELISAMice plasmaIn VivoPDB ID: 4J4LNoneThe tumor size remained around 200 mm3 until 27 days when Pal-Rb was administered (p < 0.01), whereas tumor continued to grow over 600 mm3 when WT-Rb and PBS were injected.
5125
327362622020
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPSLKEAKEKAIEELKKAGITSDYYFDLINKAKTVEGVNALKDEILKAVDAKYAKEFESAAHEIRWLPNLTYDQRVAFIHKLSDDPSQSSELLSEAKKLNDSQAPK
EX-ABD-AFF142FreeABD-AFFLinearLNoneSyntheticAntiobesityblood 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/kg166.4ICR 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))
5126
327362622020
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPSLKEAKEKAIEELKKAGITSDYYFDLINKAKTVEGVNALKDEILKAVDAKYAKEFESAAHEIRWLPNLTYDQRVAFIHKLSDDPSQSSELLSEAKKLNDSQAPK
EX-ABD-AFF142FreeABD-AFFLinearLNoneSyntheticAntiobesityblood 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/kg140.2ICR 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))
5176
323161692020
HAEGTFTSDDAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLVAASQAALGLSSYLEGQAAKEFIAWLVRGRG
GLP1_16HSA615FreeFreeLinearLIncorporation of HSA at V16 of GLP_1CSyntheticAntidiabetesBlood samples (below 70 μL) were collected from the retroorbital venous sinus at 0.16, 1, 2, 4, 8, 12, and 24 h after administration10 nmol/kg8.4Mice serum proteaseSandwich ELISAMice serumIn VivoNoneNoneEC50 = 0.70 μM
5177
323161692020
HAEGTFTSDVSSDAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLVAASQAALGLLEGQAAKEFIAWLVRGRG
GLP1_19HSA615FreeFreeLinearLIncorporation of HSA at Y19 of GLP_1CSyntheticAntidiabetesBlood samples (below 70 μL) were collected from the retroorbital venous sinus at 0.16, 1, 2, 4, 8, 12, and 24 h after administration10 nmol/kg7.4Mice serum proteaseSandwich ELISAMice serumIn VivoNoneNoneEC50 = 1.91 μM
5178
323161692020
HAEGTFTSDVSSYLEGQAAKEDAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLVAASQAALGLIAWLVRGRG
GLP1_28HSA615FreeFreeLinearLIncorporation of HSA at F28 of GLP_1CSyntheticAntidiabetesBlood samples (below 70 μL) were collected from the retroorbital venous sinus at 0.16, 1, 2, 4, 8, 12, and 24 h after administration10 nmol/kg8Mice serum proteaseSandwich ELISAMice serumIn VivoNoneNoneEC50 = 6.85 μM
5180
322431772020
MTTASTSQVRQNYHQDSEAAINRQINLELYASYVYLSMSYYFDRDDVALKNFAKYFLHQSHEEREHAEKLMKLQNQRGGRIFLQDIKKPDCDDWESGLNAMECALHLEKNVNQSLLELHKLATDKNDPHLCDFIETHYLNEQVKAIKELGDHVTNLRKMGAPESGLAEYLFDKHTLGDSDNES
FITC-labeled HFt183FITC labelledFreeLinearLNoneDerived from human FtAntidiabetesAt different time points (30 min, 1, 2, 4, 8, 10, 24, 48, 72, and 96 h) after injection100 μg51.1Mice plasma proteaseBCA protein assayMice plasmaIn VivoNoneNoneThe GLP-HFt nanocage dose-dependently reduced the nonfasting blood glucose of the STZ-induced diabetic mice
5181
322431772020
HGEGTFTSDVSSYLEGQAAKEFIAWLVKGRGSGGMTTASTSQVRQNYHQDSEAAINRQINLELYASYVYLSMSYYFDRDDVALKNFAKYFLHQSHEEREHAEKLMKLQNQRGGRIFLQDIKKPDCDDWESGLNAMECALHLEKNVNQSLLELHKLATDKNDPHLCDFIETHYLNEQVKAIKELGDHVTNLRKMGAPESGLAEYLFDKHTLGDSDNES
GLP-HFt217GLP-1 A8G modification linked by GSGGFreeLinearLNoneSyntheticAntidiabetesAt different time points (30 min, 1, 2, 4, 8, 10, 24, 48, 72, and 96 h) after injection100 μg51.9Mice plasma proteaseBCA protein assayMice plasmaIn VivoNoneNoneThe GLP-HFt nanocage dose-dependently reduced the nonfasting blood glucose of the STZ-induced diabetic mice
5198
321690632020
MALTFALLVALLVLSCKSSCSVGCDLPQTHSLGSRRTLMLLAQMRRISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKESSSSKAPPPSLPSPSRLPGPSDTPILPQ
IFN-1CTPON216FreeCarboxyl-terminal peptide (CTP) of the human chorionic gonadotropin β subunit and N-linked glycosylation sequences were linked to rhIFN-α2b at C terminusLinearLNoneDerived from rhIFN-α2bAntiviral, AntitumorIntraocular venous blood was collected at 0.5, 1, 2, 4, 8, and 24 h postinjection50 μg/kg2.62 ± 0.34Mice blood proteaseELISAMice blood sampleIn VivoPDB id: 1ITFNoneAntiviral activities of IFN-1CTPON = 8.22 × 106 IU/mg
5199
321690632020
SSSSKAPPPSLPSPSRLPGPSDTPILPQMALTFALLVALLVLSCKSSCSVGCDLPQTHSLGSRRTLMLLAQMRRISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKESSSSKAPPPSLPSPSRLPGPSDTPILPQ
IFN-2CTPON244Carboxyl-terminal peptide (CTP) of the human chorionic gonadotropin β su bunit and N-linked glycosylation sequences were linked to rhIFN-α2b at N terminusCarboxyl-terminal peptide (CTP) of the human chorionic gonadotropin β su bunit and N-linked glycosylation sequences were linked to rhIFN-α2b at C terminusLinearLNoneSyntheticAntiviral, AntitumorIntraocular venous blood was collected at 0.5, 1, 2, 4, 8, and 24 h postinjection50 μg/kg3.45 ± 0.87 Mice blood proteaseELISAMice blood sampleIn VivoPDB id: 1ITFNoneAntiviral activities of IFN-2CTPON = 3.12 × 106 IU/mg
5200
321690632020
CDLPQTHSLGSRRTLMLLAQMRRISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMNEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE
rhIFN-α2b165FreeFreeLinearLNoneSyntheticAntiviral, AntitumorIntraocular venous blood was collected at 0.5, 1, 2, 4, 8, and 24 h postinjection50 μg/kg1.34 ± 0.48Mice blood proteaseELISAMice blood sampleIn VivoPDB id: 1RH2NoneAntiviral activities of rhIFN-α2b = 5.29 × 107 IU/mg
5207
320829722020
PHWSYGLRPGGGGGSGGGGSGGGGSESKYGPPCPSCPAPEFLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSQEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKGLPSSIEKTISKAKGQPREPQVYTLPPSQEEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSRLTVDKSRWQEGNVFSCSVMHEALHNHYTQKSLSLSGGGGSGGGGSGGGGSIVRRADRAAVPGGGGACDCRGDCFC
LMRAP291FreehIgG4 Fc-linker-AP25LinearLNoneSyntheticAntitumorThe experimental sampling time points were: SD rats at 5 min before administration and then 0, 5, 10, 30 min, 1, 2, 4, 6, 8, 12, 24, 36, 48, 72, 96, 120, 144, 168, 192, and 216 h after LMRAP administration12.5 mg/kg45.237 (Elimination Half Life)SD rats plasma proteaseELISASD rats plasma In VivoNoneNoneThe inhibition rates of each dose of LMRAP at 0.1, 0.2, 0.4, 0.8 and 1.6 μmol/L were 45.8 ± 5.9%, 43.8 ± 18.4%, 57.2 ± 10.2%, 76.6 ± 3.2% and 84.9 ± 2.8%, respectively
5208
320829722020
PHWSYGLRPGGGGGSGGGGSGGGGSESKYGPPCPSCPAPEFLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSQEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKGLPSSIEKTISKAKGQPREPQVYTLPPSQEEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSRLTVDKSRWQEGNVFSCSVMHEALHNHYTQKSLSLSGGGGSGGGGSGGGGSIVRRADRAAVPGGGGACDCRGDCFC
LMRAP291FreehIgG4 Fc-linker-AP25LinearLNoneSyntheticAntitumorThe experimental sampling time points were: SD rats at 5 min before administration and then 0, 5, 10, 30 min, 1, 2, 4, 6, 8, 12, 24, 36, 48, 72, 96, 120, 144, 168, 192, and 216 h after LMRAP administration12.5 mg/kg29.187 (Elimination Half Life)SD rats plasma proteaseELISASD rats plasma In VivoNoneNoneThe inhibition rates of each dose of LMRAP at 0.1, 0.2, 0.4, 0.8 and 1.6 μmol/L were 45.8 ± 5.9%, 43.8 ± 18.4%, 57.2 ± 10.2%, 76.6 ± 3.2% and 84.9 ± 2.8%, respectively
5209
320829722020
PHWSYGLRPGGGGGSGGGGSGGGGSESKYGPPCPSCPAPEFLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSQEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKGLPSSIEKTISKAKGQPREPQVYTLPPSQEEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSRLTVDKSRWQEGNVFSCSVMHEALHNHYTQKSLSLSGGGGSGGGGSGGGGSIVRRADRAAVPGGGGACDCRGDCFC
LMRAP291FreehIgG4 Fc-linker-AP25LinearLNoneSyntheticAntitumorThe experimental sampling time points were: SD rats at 5 min before administration and then 0, 5, 10, 30 min, 1, 2, 4, 6, 8, 12, 24, 36, 48, 72, 96, 120, 144, 168, 192, and 216 h after LMRAP administration12.5 mg/kg50.979 (Eliminatoin Half Life)SD rats plasma proteaseELISASD rats plasma In VivoNoneNoneThe inhibition rates of each dose of LMRAP at 0.1, 0.2, 0.4, 0.8 and 1.6 μmol/L were 45.8 ± 5.9%, 43.8 ± 18.4%, 57.2 ± 10.2%, 76.6 ± 3.2% and 84.9 ± 2.8%, respectively
5210
320829722020
PHWSYGLRPGGGGGSGGGGSGGGGSESKYGPPCPSCPAPEFLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSQEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKGLPSSIEKTISKAKGQPREPQVYTLPPSQEEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSRLTVDKSRWQEGNVFSCSVMHEALHNHYTQKSLSLSGGGGSGGGGSGGGGSIVRRADRAAVPGGGGACDCRGDCFC
LMRAP291FreehIgG4 Fc-linker-AP25LinearLNoneSyntheticAntitumorThe experimental sampling time points were: SD rats at 5 min before administration and then 0, 5, 10, 30 min, 1, 2, 4, 6, 8, 12, 24, 36, 48, 72, 96, 120, 144, 168, 192, and 216 h after LMRAP administration12.5 mg/kg18.256 (Elimination Half Life)SD rats plasma proteaseELISASD rats plasma In VivoNoneNoneThe inhibition rates of each dose of LMRAP at 0.1, 0.2, 0.4, 0.8 and 1.6 μmol/L were 45.8 ± 5.9%, 43.8 ± 18.4%, 57.2 ± 10.2%, 76.6 ± 3.2% and 84.9 ± 2.8%, respectively
5211
320829722020
PHWSYGLRPGGGGGSGGGGSGGGGSESKYGPPCPSCPAPEFLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSQEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKGLPSSIEKTISKAKGQPREPQVYTLPPSQEEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSRLTVDKSRWQEGNVFSCSVMHEALHNHYTQKSLSLSGGGGSGGGGSGGGGSIVRRADRAAVPGGGGACDCRGDCFC
LMRAP291FreehIgG4 Fc-linker-AP25LinearLNoneSyntheticAntitumorThe experimental sampling time points were: SD rats at 5 min before administration and then 0, 5, 10, 30 min, 1, 2, 4, 6, 8, 12, 24, 36, 48, 72, 96, 120, 144, 168, 192, and 216 h after LMRAP administration12.5 mg/kg27.879 (Elimination Half Life)SD rats plasma proteaseELISASD rats plasma In VivoNoneNoneThe inhibition rates of each dose of LMRAP at 0.1, 0.2, 0.4, 0.8 and 1.6 μmol/L were 45.8 ± 5.9%, 43.8 ± 18.4%, 57.2 ± 10.2%, 76.6 ± 3.2% and 84.9 ± 2.8%, respectively
5212
320829722020
PHWSYGLRPGGGGGSGGGGSGGGGSESKYGPPCPSCPAPEFLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSQEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKGLPSSIEKTISKAKGQPREPQVYTLPPSQEEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSRLTVDKSRWQEGNVFSCSVMHEALHNHYTQKSLSLSGGGGSGGGGSGGGGSIVRRADRAAVPGGGGACDCRGDCFC
LMRAP291FreehIgG4 Fc-linker-AP25LinearLNoneSyntheticAntitumorThe experimental sampling time points were: SD rats at 5 min before administration and then 0, 5, 10, 30 min, 1, 2, 4, 6, 8, 12, 24, 36, 48, 72, 96, 120, 144, 168, 192, and 216 h after LMRAP administration12.5 mg/kg28.452 (Elimination Half Life)SD rats plasma proteaseELISASD rats plasma In VivoNoneNoneThe inhibition rates of each dose of LMRAP at 0.1, 0.2, 0.4, 0.8 and 1.6 μmol/L were 45.8 ± 5.9%, 43.8 ± 18.4%, 57.2 ± 10.2%, 76.6 ± 3.2% and 84.9 ± 2.8%, respectively
5255
315290972020
FPTIPLSRLFDNAMLRAHRLHQLAFDTYQEFEEAYIPKEQKYSFLQNPQTSLCFSESIPTPSNREETQQKSNLELLRISLLLIQSWLEPVQFLRSVFANSLVYGASDSNVYDLLKDLEEGIQTLMGRLEDGSPRTGQIFKQTYSKFDTNSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF
GH191FreeFreeLinearLNoneProduced by the somatotroph cells in the anterior pituitary glandInvolved in the regulation of growth and metabolismN.A.N.A.13.9 ± 3.6Human blood plasma protease2-site immunoassayHuman blood plasmaIn Vivopdb id: 1HWGNoneN.A.
5256
315290972020
FPTIPLSRLFDNAMLRAHRLHQLAFDTYQEFEEAYIPKEQKYSFLQNPQTSLCFSESIPTPSNREETQQKSNLELLRISLLLIQSWLEPVQFLRSVFANSLVYGASDSNVYDLLKDLEEGIQTLMGRLEDGSPRTGQIFKQTYSKFDTNSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF
GH191FreeFreeLinearLNoneProduced by the somatotroph cells in the anterior pituitary glandInvolved in the regulation of growth and metabolismN.A.N.A.17.0 ± 6.8Human blood plasma protease2-site immunoassayHuman blood plasma after SitagliptinIn Vivopdb id: 1HWGNoneN.A.
5257
315290972020
FPTIPLSRLFDNAMLRAHRLHQLAFDTYQEFEEAYIPKEQKYSFLQNPQTSLCFSESIPTPSNREETQQKSNLELLRISLLLIQSWLEPVQFLRSVFANSLVYGASDSNVYDLLKDLEEGIQTLMGRLEDGSPRTGQIFKQTYSKFDTNSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF
GH191FreeFreeLinearLNoneProduced by the somatotroph cells in the anterior pituitary glandInvolved in the regulation of growth and metabolismGH levels were obtained every 10 minutes from 8 PM until 8 AMN.A.13.9Human blood plasma protease2-site immunoassayHuman blood plasmaIn Vivopdb id: 1HWGNoneN.A.
5258
315290972020
FPTIPLSRLFDNAMLRAHRLHQLAFDTYQEFEEAYIPKEQKYSFLQNPQTSLCFSESIPTPSNREETQQKSNLELLRISLLLIQSWLEPVQFLRSVFANSLVYGASDSNVYDLLKDLEEGIQTLMGRLEDGSPRTGQIFKQTYSKFDTNSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF
GH191FreeFreeLinearLNoneProduced by the somatotroph cells in the anterior pituitary glandInvolved in the regulation of growth and metabolismGH levels were obtained every 10 minutes from 8 PM until 8 AMN.A.14.5Human blood plasma protease2-site immunoassayHuman blood plasma after 1month of SitagliptinIn Vivopdb id: 1HWGNoneN.A.
5286
328030732020
GSLTSSERIDKQIRYILDGISALRKETCNKSNMCESSKEALAENNLNLPKMAEKDGCFQSGFNEETCLVKIITGLLEFEVYLEYLQNRFESSEEQARAVQMSTKVLIQFLQKKAKNL-AzF-AITTPDPTTNASLLTKLQAQNQWLQDMTTHLILRSFKEFLQSSLRALRQM
Pal-Rb169FreeFreeLinearLConjugation of palmitic acid, biotinylated labelling, , (AzF) was incorporated into the position 126 on the repebody followed by lipid conjugationSyntheticAntitumorBlood was collected in predetermined time points postinjection (n = 5; 0.05, 0.5, 1, 2, 4, 6, 12 and 24 h)10 mg/kg4.2 (Distribution Half-Life)Mice plasma proteaseSandwich ELISAmice plasmaIn VivoNoneNoneThe tumor size remained around 200 mm3 until 27 days when Pal-Rb was administered (p < 0.01), whereas tumor continued to grow over 600 mm3 when WT-Rb and PBS were injected.
5287
318455782020
N.A.
Man25449FreeFreeLinearLNoneβ-mannanase from Thermoanaerobacterium aotearoenseRole in cellulosic biomass degradation 55 °CN.A.40.2 (Activity Half Life)N.A.N.A.N.A.N.A.NoneNoneMan25 retaining more than 50% activity at its optimal pH of 5.5
5288
318455782020
N.A.
ManM3-3449FreeFreeLinearLD143A amino acid substituitionDerived from Man25Role in cellulosic biomass degradation 55 °CN.A.143.4 (Activity Half Life)N.A.N.A.N.A.N.A.NoneNoneMan25 retaining more than 50% activity at its optimal pH of 5.5
5289
318455782020
N.A.
ManM5-10 449FreeFreeLinearLE32K, E34S amino acid substituitionDerived from Man25Role in cellulosic biomass degradation 55 °CN.A.74.4 (Activity Half Life)N.A.N.A.N.A.N.A.NoneNoneMan25 retaining more than 50% activity at its optimal pH of 5.5
5299
318182122019
DKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGKGGGGSGGGGSGGGGSQLYSALANKCCHVGCTKRSLARFCGGGGSGGGGSGGGGSSWMEEVIKLCGRELVRAQIAICGMSTWS
RELAX10 309FreeFreeLinearLFusion of Human Relaxin 2 with Fc IgG using linkerHuman Relaxin analogueTreatment prevents and reverses isoproterenol induced hypertrophy and fibrosis in mouse heartBlood samples were collected at various time points after drug administration4 mg/kg3.59Wistar rats plasma proteaseELISAWistar rats plasmaIn Vivohttps://www.lens.org/lens/patent/078-521-931-782-236/fulltextNoneRELAX10 was active in CHO cells overexpressing the relaxin‐2 receptor, RXFP1, with an average half‐maximal effective concentration value of 1.94 nmol/L
5300
318182122019
DKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGKGGGGSGGGGSGGGGSQLYSALANKCCHVGCTKRSLARFCGGGGSGGGGSGGGGSSWMEEVIKLCGRELVRAQIAICGMSTWS
RELAX10 309FreeFreeLinearLFusion of Human Relaxin 2 with Fc IgG using linkerHuman Relaxin analogueTreatment prevents and reverses isoproterenol induced hypertrophy and fibrosis in mouse heartBlood samples were collected at various time points after drug administration4 mg/kg3.75Wistar rats plasma proteaseELISAWistar rats plasmaIn Vivohttps://www.lens.org/lens/patent/078-521-931-782-236/fulltextNoneRELAX10 was active in CHO cells overexpressing the relaxin‐2 receptor, RXFP1, with an average half‐maximal effective concentration value of 1.94 nmol/L
5301
318182122019
DKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGKGGGGSGGGGSGGGGSQLYSALANKCCHVGCTKRSLARFCGGGGSGGGGSGGGGSSWMEEVIKLCGRELVRAQIAICGMSTWS
RELAX10 309FreeFreeLinearLFusion of Human Relaxin 2 with Fc IgG using linkerHuman Relaxin analogueTreatment prevents and reverses isoproterenol induced hypertrophy and fibrosis in mouse heartBlood samples were collected at various time points after drug administration6 mg/kg5.58Wistar rats plasma proteaseELISAWistar rats plasmaIn Vivohttps://www.lens.org/lens/patent/078-521-931-782-236/fulltextNoneRELAX10 was active in CHO cells overexpressing the relaxin‐2 receptor, RXFP1, with an average half‐maximal effective concentration value of 1.94 nmol/L
5302
318182122019
DKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGKGGGGSGGGGSGGGGSQLYSALANKCCHVGCTKRSLARFCGGGGSGGGGSGGGGSSWMEEVIKLCGRELVRAQIAICGMSTWS
RELAX10 309FreeFreeLinearLFusion of Human Relaxin 2 with Fc IgG using linkerHuman Relaxin analogueTreatment prevents and reverses isoproterenol induced hypertrophy and fibrosis in mouse heartBlood samples were collected at various time points after drug administration6 mg/kg7.06Wistar rats plasma proteaseELISAWistar rats plasmaIn Vivohttps://www.lens.org/lens/patent/078-521-931-782-236/fulltextNoneRELAX10 was active in CHO cells overexpressing the relaxin‐2 receptor, RXFP1, with an average half‐maximal effective concentration value of 1.94 nmol/L
5303
318182122019
DKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGKGGGGSGGGGSGGGGSQLYSALANKCCHVGCTKRSLARFCGGGGSGGGGSGGGGSSWMEEVIKLCGRELVRAQIAICGMSTWS
RELAX10 309FreeFreeLinearLFusion of Human Relaxin 2 with Fc IgG using linkerHuman Relaxin analogueTreatment prevents and reverses isoproterenol induced hypertrophy and fibrosis in mouse heartBlood samples were collected at various time points after drug administration1, 6, or 30 mg/kg 4.59 - 7.06Wistar rats plasma proteaseELISAWistar rats plasmaIn Vivohttps://www.lens.org/lens/patent/078-521-931-782-236/fulltextNoneRELAX10 was active in CHO cells overexpressing the relaxin‐2 receptor, RXFP1, with an average half‐maximal effective concentration value of 1.94 nmol/L
5326
314431812019
MGVPRPQPWALGLLLFLLPGSLGAESHLSLLYHLTAVSSPAPGTPAFWVSGWLGPQQYLSYNSLRGEAEPCGAWVWENQVSWYWEKETTDLRIKEKLFLEAFKALGGKGPYTLQGLLGCELGPDNTSVPTAKFALNGEEFMNFDLKQGTWGGDWPEALAISQRWQQQDKAANKELTFLLFSCPHRLREHLERGRGNLEWKEPPSMRLKARPSSPGFSVLTCSAFSFYPPELQLRFLRNGLAAGTGQGDFGPNSDGSFHASSSLTVKSGDEHHYCCIVQHAGLAQPLRVELESPAKSSVLVVGIVIGVLLLTAAAVGGALLWRRMRSGLPAPWISLRGDDTGVLLPTPGEAQDADLKDVNVIPATA
FcRn365FreeFreeLinearLNoneIsolated from human gastric juiceRole in extending the serum half life of therapeutic antibodiesBlood collection at 0, 1.5, 3, 4.5, 6, 7.5, 9, 12, 15, 18, 21, 24, 27, 30, 33, 36 hrsN.A.10.6PBMC lysate protease (African American)LC-MS/MSPBMC lysate (African American)In VitroUniprot id: P55899NoneN.A.
5327
314431812019
MGVPRPQPWALGLLLFLLPGSLGAESHLSLLYHLTAVSSPAPGTPAFWVSGWLGPQQYLSYNSLRGEAEPCGAWVWENQVSWYWEKETTDLRIKEKLFLEAFKALGGKGPYTLQGLLGCELGPDNTSVPTAKFALNGEEFMNFDLKQGTWGGDWPEALAISQRWQQQDKAANKELTFLLFSCPHRLREHLERGRGNLEWKEPPSMRLKARPSSPGFSVLTCSAFSFYPPELQLRFLRNGLAAGTGQGDFGPNSDGSFHASSSLTVKSGDEHHYCCIVQHAGLAQPLRVELESPAKSSVLVVGIVIGVLLLTAAAVGGALLWRRMRSGLPAPWISLRGDDTGVLLPTPGEAQDADLKDVNVIPATA
FcRn365FreeFreeLinearLNoneIsolated from human gastric juiceRole in extending the serum half life of therapeutic antibodiesBlood collection at 0, 1.5, 3, 4.5, 6, 7.5, 9, 12, 15, 18, 21, 24, 27, 30, 33, 36 hrsN.A.11.6PBMC lysate protease (African American)LC-MS/MSPBMC lysate (African American)In VitroUniprot id: P55899NoneN.A.
5342
313104332019
[(VPGVG)11(VPGKG)1(VPGVG)1]9-DPNYPRGHEAEDLQVGQVELGGGPGAGSLQPLALEGSLQ
K9-C-peptide hydrogel624FreeHuman C-peptide genetically conjugated at the C-terminus of nine repeats of lysine-containing elastin-like polypeptideLinearLCy3 conjugationELP analoguesAntidiabetes120 minutesN.A.72.3% DegradationElastase-2Confocal microscopyReaction buffer + elastase-2In VitroNoneNoneEC50 values of the four enzymes (collagenase-2, elastase-2, pepsin, and trypsin) were 0.17, 0.23, 510.00, and 124.60 U m/L for K9-C peptide
5343
313104332019
[(VPGVG)11(VPGKG)1(VPGVG)1]9-DPNYPRGHEAEDLQVGQVELGGGPGAGSLQPLALEGSLQ
K9-C-peptide hydrogel624FreeHuman C-peptide genetically conjugated at the C-terminus of nine repeats of lysine-containing elastin-like polypeptideLinearLCy3 conjugationELP analoguesAntidiabetesN.A.N.A.<10% DegradationN.A.Confocal microscopyReaction bufferIn VitroNoneNoneEC50 values of the four enzymes (collagenase-2, elastase-2, pepsin, and trypsin) were 0.17, 0.23, 510.00, and 124.60 U m/L for K9-C peptide
5344
313104332019
[(VPGVG)11(VPGKG)1(VPGVG)1]9-DPNYPRGHEAEDLQVGQVELGGGPGAGSLQPLALEGSLQ
K9-C-peptide hydrogel624FreeHuman C-peptide genetically conjugated at the C-terminus of nine repeats of lysine-containing elastin-like polypeptideLinearLCy3 conjugationELP analoguesAntidiabetesRepeated 30-min elastase-2 treatmentsN.A.48.6 ± 0.8% Degradation After First TreatmentElastase-2Confocal microscopyReaction buffer + elastase-2In VitroNoneNoneEC50 values of the four enzymes (collagenase-2, elastase-2, pepsin, and trypsin) were 0.17, 0.23, 510.00, and 124.60 U m/L for K9-C peptide
5345
313104332019
[(VPGVG)11(VPGKG)1(VPGVG)1]9-DPNYPRGHEAEDLQVGQVELGGGPGAGSLQPLALEGSLQ
K9-C-peptide hydrogel624FreeHuman C-peptide genetically conjugated at the C-terminus of nine repeats of lysine-containing elastin-like polypeptideLinearLCy3 conjugationELP analoguesAntidiabetesN.A.N.A.89.7 ± 0.2% Degradation After Fifth Elastase TreatmentElastase-2Confocal microscopyReaction buffer + elastase-2In VitroNoneNoneEC50 values of the four enzymes (collagenase-2, elastase-2, pepsin, and trypsin) were 0.17, 0.23, 510.00, and 124.60 U m/L for K9-C peptide
5346
313104332019
[(VPGVG)11(VPGKG)1(VPGVG)1]9-DPNYPRGHEAEDLQVGQVELGGGPGAGSLQPLALEGSLQ
K9-C-peptide hydrogel624FreeHuman C-peptide genetically conjugated at the C-terminus of nine repeats of lysine-containing elastin-like polypeptideLinearLCy3 conjugationELP analoguesAntidiabetesN.A.N.A.1.3 ± 0.6% Degradation After 1St Buffer TreatmentN.A.Confocal microscopyReaction bufferIn VitroNoneNoneEC50 values of the four enzymes (collagenase-2, elastase-2, pepsin, and trypsin) were 0.17, 0.23, 510.00, and 124.60 U m/L for K9-C peptide
5347
313104332019
[(VPGVG)11(VPGKG)1(VPGVG)1]9-DPNYPRGHEAEDLQVGQVELGGGPGAGSLQPLALEGSLQ
K9-C-peptide hydrogel624FreeHuman C-peptide genetically conjugated at the C-terminus of nine repeats of lysine-containing elastin-like polypeptideLinearLCy3 conjugationELP analoguesAntidiabetesN.A.N.A.27.9 ± 2.5% Degradation After 5Th Buffer Treatment N.A.Confocal microscopyReaction bufferIn VitroNoneNoneEC50 values of the four enzymes (collagenase-2, elastase-2, pepsin, and trypsin) were 0.17, 0.23, 510.00, and 124.60 U m/L for K9-C peptide
5370
311560412019
LQVDIVPSQGEISVGESKFFLCQVAGDAKDKDISWFSPNGEKLTPNQQRISVVWNDDSSSTLTIYNANIDDAGIYKCVVTGEDGSESEATVNVKIFQAAADYKDDDDKAADYKDDDDK
AD-114-Im7-FH 118Freelm7-FH fusionLinearLNoneFusion protein of AD-114 with lm7 and FHAttenuates Renal fibrosis through blockade Of CXCRBlood samples were collected 5 min, 2, 6, 12, 24, 72 h post dosing3 mg/kg0.18Mouse plasma proteaseLC–MS/MSMouse plasmaIn VivoPDB id: >5AEA_1NoneKd(nM) = 9.1 (Human CXCR4 affinity)
5371
311560412019
LQVDIVPSQGEISVGESKFFLCQVAGDAKDKDISWFSPNGEKLTPNQQRISVVWNDDSSSTLTIYNANIDDAGIYKCVVTGEDGSESEATVNVKIFQAAADYKDDDDKAADYKDDDDK
AD-114-Im7-FH-SA21 118Freelm7-FH-SA21LinearLNoneFusion protein of AD-114 with lm7 and FH, SA21Attenuates Renal fibrosis through blockade Of CXCRBlood samples were collected 5 min, 2, 6, 12, 24, 72 h post dosing2 mg/kg0.95Mouse plasma proteaseLC–MS/MSMouse plasmaIn VivoPDB id: >5AEA_1NoneKd(nM) = 9.2 (Human CXCR4 affinity)
5372
311560412019
LQVDIVPSQGEISVGESKFFLCQVAGDAKDKDISWFSPNGEKLTPNQQRISVVWNDDSSSTLTIYNANIDDAGIYKCVVTGEDGSESEATVNVKIFQAAADYKDDDDKAADYKDDDDK
AD-114-Im7 PEG 30K 118Freelm7-PEG30KLinearLNoneFusion protein of AD-114 with lm7Attenuates Renal fibrosis through blockade Of CXCRBlood samples were collected 5 min, 2, 6, 12, 24, 72 h post dosing3 mg/kg11.85Mouse plasma proteaseLC–MS/MSMouse plasmaIn VivoPDB id: >5AEA_1NoneKd(nM) = 0.7 (Human CXCR4 affinity) for AD-114-Im7-FH-PEG 30K 
5373
311560412019
LQVDIVPSQGEISVGESKFFLCQVAGDAKDKDISWFSPNGEKLTPNQQRISVVWNDDSSSTLTIYNANIDDAGIYKCVVTGEDGSESEATVNVKIFQAAADYKDDDDKAADYKDDDDK
AD-114-Im7 PEG 2×20K 118Freelm7-PEG2*20KLinearLNoneFusion protein of AD-114 with lm7Attenuates Renal fibrosis through blockade Of CXCRBlood samples were collected 5 min, 2, 6, 12, 24, 72 h post dosing1.25 mg/kg19.24Mouse plasma proteaseLC–MS/MSMouse plasmaIn VivoPDB id: >5AEA_1NoneKd(nM) = 0.7 (Human CXCR4 affinity) for AD-114-Im7-FH-PEG 30K 
5374
311560412019
LQVDIVPSQGEISVGESKFFLCQVAGDAKDKDISWFSPNGEKLTPNQQRISVVWNDDSSSTLTIYNANIDDAGIYKCVVTGEDGSESEATVNVKIFQAAADYKDDDDKAADYKDDDDK
AD-114-PA600-6H 118FreePA-600-6HLinearLNoneFusion protein of AD-114 with PA600Attenuates Renal fibrosis through blockade Of CXCRBlood samples were collected 5 min, 2, 6, 12, 24, 72 h post dosing10 mg/kg7.77Mouse plasma proteaseLC–MS/MSMouse plasmaIn VivoPDB id: >5AEA_1NoneKd(nM) = 5.2 (Human CXCR4 affinity) for AD-114-Im7-FH-PEG 30K 
5375
311560412019
LQVDIVPSQGEISVGESKFFLCQVAGDAKDKDISWFSPNGEKLTPNQQRISVVWNDDSSSTLTIYNANIDDAGIYKCVVTGEDGSESEATVNVKIFQAAADYKDDDDKAADYKDDDDK
AD-114-PA600-6H 118FreePA-600-6HLinearLNoneFusion protein of AD-114 with PA600Attenuates Renal fibrosis through blockade Of CXCRBlood samples were collected at 15, 30 min, 1, 2, 3, 4, 8, 12,18, 24, 36, 48 and 72 h post dosing10 mg/kg7.03Mouse plasma proteaseELISAMouse plasmaIn VivoPDB id: >5AEA_1NoneKd(nM) = 5.2 (Human CXCR4 affinity) for AD-114-Im7-FH-PEG 30K 
5376
311560412019
LQVDIVPSQGEISVGESKFFLCQVAGDAKDKDISWFSPNGEKLTPNQQRISVVWNDDSSSTLTIYNANIDDAGIYKCVVTGEDGSESEATVNVKIFQAAADYKDDDDKAADYKDDDDK
AD-114-PA600-6H 118FreePA-600-6HLinearLNoneFusion protein of AD-114 with PA600Attenuates Renal fibrosis through blockade Of CXCRBlood samples were collected at 15, 30 min, 1, 2, 3, 4, 8, 12,18, 24, 36, 48 and 72 h post dosing10 mg/kg10.25Mouse plasma proteaseELISAMouse plasmaIn VivoPDB id: >5AEA_1NoneKd(nM) = 5.2 (Human CXCR4 affinity) for AD-114-Im7-FH-PEG 30K 
5377
311560412019
LQVDIVPSQGEISVGESKFFLCQVAGDAKDKDISWFSPNGEKLTPNQQRISVVWNDDSSSTLTIYNANIDDAGIYKCVVTGEDGSESEATVNVKIFQAAADYKDDDDKAADYKDDDDK
AD-114-PA600 118FreePA-600LinearLNoneFusion protein of AD-114 with PA600Attenuates Renal fibrosis through blockade Of CXCRBlood samples were collected immediately post dosing and at 5, 30 min, 2, 8, 24, 72 h post dosing3.5 mg/kg9.5Rats plasma proteaseLC–MS/MSRats plasmaIn VivoPDB id: >5AEA_1NoneKd(nM) = 4 (Human CXCR4 affinity) for AD-114-Im7-FH-PEG 30K 
5378
311560412019
LQVDIVPSQGEISVGESKFFLCQVAGDAKDKDISWFSPNGEKLTPNQQRISVVWNDDSSSTLTIYNANIDDAGIYKCVVTGEDGSESEATVNVKIFQAAADYKDDDDKAADYKDDDDK
AD-114-PA600-6H 118FreePA-600-6HLinearLNoneFusion protein of AD-114 with PA600Attenuates Renal fibrosis through blockade Of CXCRBlood samples were collected immediately following dosing and at 5, 15, and 30 min and 1, 2, 4, 8, 12, 24, 36, 48, 60, 72, 84, 96, 120, 144, 168, and 192-h post-dosing2 mg/kg24.27 ± 0.24Cynomolgus monkeys plasma proteaseLC–MS/MSCynomolgus monkeys plasmaIn VivoPDB id: >5AEA_1NoneKd(nM) = 5.2 (Human CXCR4 affinity) for AD-114-Im7-FH-PEG 30K 
5379
311560412019
LQVDIVPSQGEISVGESKFFLCQVAGDAKDKDISWFSPNGEKLTPNQQRISVVWNDDSSSTLTIYNANIDDAGIYKCVVTGEDGSESEATVNVKIFQAAADYKDDDDKAADYKDDDDK
AD-114-PA600 118FreePA-600LinearLNoneFusion protein of AD-114 with PA600Attenuates Renal fibrosis through blockade Of CXCRBlood samples were collected pre-dosing and at the following time points post each dosing: 30 min, 1, 2, 4, 8, 12, 24, 48, 72, 96, 120, and 144 h3 mg/kg25.41 ± 5.17Cynomolgus monkeys plasma proteaseLC–MS/MSCynomolgus monkeys plasmaIn VivoPDB id: >5AEA_1NoneKd(nM) = 4 (Human CXCR4 affinity) for AD-114-Im7-FH-PEG 30K 
5380
311560412019
LQVDIVPSQGEISVGESKFFLCQVAGDAKDKDISWFSPNGEKLTPNQQRISVVWNDDSSSTLTIYNANIDDAGIYKCVVTGEDGSESEATVNVKIFQAAADYKDDDDKAADYKDDDDK
AD-114-PA600 118FreePA-600LinearLNoneFusion protein of AD-114 with PA600Attenuates Renal fibrosis through blockade Of CXCRBlood samples were collected pre-dosing and at the following time points post-dosing: 5 min, 1, 4, 12, 24, 48, 96, 168 h. 3 mg/kg10.2 ± 3.9Cynomolgus monkeys plasma proteaseLC–MS/MSCynomolgus monkeys plasma dosed at Day 1In VivoPDB id: >5AEA_1NoneKd(nM) = 4 (Human CXCR4 affinity) for AD-114-Im7-FH-PEG 30K 
5381
311560412019
LQVDIVPSQGEISVGESKFFLCQVAGDAKDKDISWFSPNGEKLTPNQQRISVVWNDDSSSTLTIYNANIDDAGIYKCVVTGEDGSESEATVNVKIFQAAADYKDDDDKAADYKDDDDK
AD-114-PA600118FreePA-600LinearLNoneFusion protein of AD-114 with PA600Attenuates Renal fibrosis through blockade Of CXCRBlood samples were collected pre-dosing and at the following time points post-dosing: 5 min, 1, 4, 12, 24, 48, 96, 168 h. 0.1 mg/kg23.53Cynomolgus monkeys plasma proteaseLC–MS/MSCynomolgus monkeys plasma dosed at Day 1In VivoPDB id: >5AEA_1NoneKd(nM) = 4 (Human CXCR4 affinity) for AD-114-Im7-FH-PEG 30K 
5382
311560412019
LQVDIVPSQGEISVGESKFFLCQVAGDAKDKDISWFSPNGEKLTPNQQRISVVWNDDSSSTLTIYNANIDDAGIYKCVVTGEDGSESEATVNVKIFQAAADYKDDDDKAADYKDDDDK
AD-114-PA600118FreePA-600LinearLNoneFusion protein of AD-114 with PA600Attenuates Renal fibrosis through blockade Of CXCRBlood samples were collected pre-dosing and at the following time points post-dosing: 5 min, 1, 4, 12, 24, 48, 96, 168 h. 3 mg/kg8.31Cynomolgus monkeys plasma proteaseLC–MS/MSCynomolgus monkeys plasma dosed at Day 8In VivoPDB id: >5AEA_1NoneKd(nM) = 4 (Human CXCR4 affinity) for AD-114-Im7-FH-PEG 30K 
5383
311560412019
LQVDIVPSQGEISVGESKFFLCQVAGDAKDKDISWFSPNGEKLTPNQQRISVVWNDDSSSTLTIYNANIDDAGIYKCVVTGEDGSESEATVNVKIFQAAADYKDDDDKAADYKDDDDK
AD-114-PA600118FreePA-600LinearLNoneFusion protein of AD-114 with PA600Attenuates Renal fibrosis through blockade Of CXCRBlood samples were collected pre-dosing and at the following time points post-dosing: 5 min, 1, 4, 12, 24, 48, 96, 168 h. 10 mg/kg6.7 ± 1.1 Cynomolgus monkeys plasma proteaseLC–MS/MSCynomolgus monkeys plasma dosed at Day 8In VivoPDB id: >5AEA_1NoneKd(nM) = 4 (Human CXCR4 affinity) for AD-114-Im7-FH-PEG 30K 
5384
311008062019
MAATHEHSAQWLNNYKKGYGYGPYPLGINGGMHYGVDFFMNIGTPVKAISSGKIVEAGWSNYGGGNQIGLIENDGVHRQWYMHLSKYNVKVGDYVKAGQIIGWSGSTGYSTAPHLHFQRMVNSFSNSTAQDPMPFLKSAGYGKAGGTVTPTPNTGWKTNKYGTLYKSESASFTPNTDIITRTTGPFRSMPQSGVLKAGQTIHYDEVMKQDGHVWVGYTGNSGQRIYLPVRTWNKSTNTLGVLWGTIKLEHHHHHH
Lysostaphin 255FreeFreeLinearLNoneProduced by Staphylococcus simulansAntibacterialThe blood was sampled from the tail vein at 25 min, 40 min, 1 h, 2 h, and 4 h time points in the group that received lysostaphin1 mg/ml1.5 ± 0.7 Rats plasma proteaseSandwich ELISARats plasmaIn VivoPDB id: 4LXCNoneMinimum inhibitory concentration (MIC) of Lst-HDD towards S. aureus ATCC 29,213 was 3.2 µg/mL and concentration is 0.1 µg/mL
5385
311008062019
MGSAATHEHSAQWLNNYKKGYGYGPYPLGINGGMHYGVDFFMNIGTPVKAISSGKIVEAGWSNYGGGNQIGLIENDGVHRQWYMHLSKYNVKVGDYVKAGQIIGWSGSTGYSTAPHLHFQRMVNSFSNSTAQDPMPFLKSAGYGKAGGTVTPTPNTGWKTNKYGTLYKSESASFTPNTDIITRTTGPFRSMPQSGVLKAGQTIHYDEVMKQDGHVWVGYTGNSGQRIYLPVRTWNKSTNTLGVLWGTIKGRSPGSGSGSGSGSGARSGSKQLEKELKQLEKELQAIEKQLAQLQWKAQARKKKLAQLKKKLQAPGSGSRS
Lst-HDD320FreeFreeLinearLNoneDerived from Lysostaphin Antibacterial25 min, 40 min, 1 h, 2 h, 4 h, and 6 h time points in the group that received Lst-HDD1 mg/ml3.1 ± 0.6Rats plasma proteaseSandwich ELISARats plasmaIn VivoNoneNoneMIC of Lst-HDD is 32 times higher than the MIC of lysostaphin in S. aureus ATCC 29,213 in —0.1 µg/mL
5386
311008062019
MAATHEHSAQWLNNYKKGYGYGPYPLGINGGMHYGVDFFMNIGTPVKAISSGKIVEAGWSNYGGGNQIGLIENDGVHRQWYMHLSKYNVKVGDYVKAGQIIGWSGSTGYSTAPHLHFQRMVNSFSNSTAQDPMPFLKSAGYGKAGGTVTPTPNTGWKTNKYGTLYKSESASFTPNTDIITRTTGPFRSMPQSGVLKAGQTIHYDEVMKQDGHVWVGYTGNSGQRIYLPVRTWNKSTNTLGVLWGTIKLEHHHHHH
lysostaphin 255FreeFreeLinearLNoneProduced by Staphylococcus simulansAnti-Staphylococcal lysinBlood was collected by orbital bleeding at 1, 4, 7, and 24 h postadministration40 mg/kg<1Mice serum proteaseELISAMice serum In VivoNoneNoneUnconjugated lysostaphin shows a standard antibody binding response from 0.3 to 20 ng/ml.
5387
311008062019
MTCYYAGDFETTTNEEETEVWLSCFAKVIDYDKLDTFKVNTSLEDFLKSLYLDLDKTYTETGEDEFIIFFHNLKFDGSFLLSFFLNNDIECTYFINDMGVWYSITLEFPDFTLTFRDSLKILNFSIATMAGLFKMPIAKGTTPLLKHKPEVIKPEWIDYIHVDVAILARGIFAMYYEENFTKYTSASEALTEFKRIFRKSKRKFRDFFPILDEKVDDFCRKHIVGAGRLPTLKHRGRTLNQLIDIYDINSMYPATMLQNALPIGIPKRYKGKPKEIKEDHYYIYHIKADFDLKRGYLPTIQIKKKLDALRIGVRTSDYVTTSKNEVIDLYLTNFDLDLFLKHYDATIMYVETLEFQTESDLFDDYITTYRYKKENAQSPAEKQKAKIMLNSLYGKFGAKIISVKKLAYLDDKGILRFKNDDEEEVQPVYAPVALFVTSIARHFIISNAQENYDNFLYADTDSLHLFHSDSLVLDIDPSEFGKWAHEGRAVKAKYLRSKLYIEELIQEDGTTHLDVKGAGMTPEIKEKITFENFVIGATFEGKRASKQIKGGTLIYETTFKIRETDYLV
Cpl-1568FreeFreeLinearLNoneLytic enzyme of a pneumococcal bacteriophageAntimicrobial for Pneumococcal BacteremiaBlood was collected after 5, 10, and15 min from three animals and after 30, 60, and 120 min from the other three animals1.6 mg20.5Mice plasma proteaseWestern blotting and spot densitometryMice serumIn VivoNoneNoneMICs of Cpl-1 = 32 μg/ml
5388
311008062019
MEINVSKLRTDLPQVGVQPYRQVHAHSTGNPHSTVQNEADYHWRKDPELGFFSHIVGNGCIMQVGPVDNGAWDVGGGWNAETYAAVELIESHSTKEEFMTDYRLYIELLRNLADEAGLPKTLDTGSLAGIKTHEYCTNNQPNNHSDHVDPYPYLAKWGISREQFKHDIENGLTIETGWQKNDTGYWYVHSDGSYPKDKFEKINGTWYYFDSSGYMLADRWRKHTDGNWYWFDNSGEMATGWKKIADKWYYFNEEGAMKTGWVKYKDTWYYLDAKEGAMVSNAFIQSADGTGWYYLKPDGTLADRPEFTVEPDGLITVK
LytA318FreeFreeLinearLNoneDerived from Streptococcus pneumoniaeTherapeutic agent in experimental peritonitis sepsis caused by highly Β-lactam resistant Streptococcus PneumoniaeBlood samples were obtained from three animals per group, which were killed at 5, 15, 60, and 120 min3.1 mg/ml22.5Adult swiss mice plasma proteaseN.A.Adult swiss mice plasmaIn VivoNoneNoneMICs of LytA = 16 μg/ml 
5415
310389302019
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPSC-Mal-DBCO-N3-KPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPG
Exenatide-Fc261FreeConjugation between Ex-Mal-DBCO and N3−Lys-FcLinearLNoneDerived from the Lys-Fc directly expressed by Expi293FAntidiabetesBlood samples (ca. 0.6 mL) were collected from the posterior aorta 1, 2, 8, 24, 48, 72, 96, 120, and 168 h after administration3.13 nmo/kg43.8Mice plasma proteaseELISAMice plasmaIn VivoPDB id: 7MLLNoneExenatide-Fc presented similar GLP-1 activities with EC50 values of 1.5 nM
5416
310389302019
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPSC-Mal-DBCO-N3-KPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPG
Exenatide-Fc261FreeConjugation between Ex-Mal-DBCO and N3−Lys-FcLinearLNoneDerived from the Lys-Fc directly expressed by Expi293FAntidiabetesBlood samples (ca. 0.6 mL) were collected from the posterior aorta 1, 2, 8, 24, 48, 72, 96, 120, and 168 h after administration12.5 nmol/kg40.4Mice plasma proteaseELISAMice plasmaIn VivoPDB id: 7MLLNoneExenatide-Fc presented similar GLP-1 activities with EC50 values of 1.5 nM
5417
310389302019
HGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPSC-Mal-DBCO-N3-KPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPG
Exenatide-Fc261FreeConjugation between Ex-Mal-DBCO and N3−Lys-FcLinearLNoneDerived from the Lys-Fc directly expressed by Expi293FAntidiabetesBlood samples (ca. 0.6 mL) were collected from the posterior aorta 1, 2, 8, 24, 48, 72, 96, 120, and 168 h after administration25 nmol/kg87.8Mice plasma proteaseELISAMice plasmaIn VivoPDB id: 7MLLNoneExenatide-Fc presented similar GLP-1 activities with EC50 values of 1.5 nM
5429
309046182019
GGGGSEEEEEEEEPLGLAGRRRRRRRRKLAKLAKKLAKLAKC
PAK253KLA linked with PsTag216 using flexible linker GGGGS at N terminalFreeLinearLNoneFusion protein of PsTag216 and KLAAntitumorAt 0.25 h, 0.5 h, 1 h, 2 h, 4 h, 8 h, 24 h, and 48 h post injection, a blood sample was obtained from the eye socket vein in mice1 μmol/kg5.05 ± 0.26Mice serum proteaseELISAMice serum In VivoNoneNoneIC50 (μM) = 11.05 ± 0.73 for the cell line A375 (In vitro antitumor effects)
5437
308536512019
(PAS)40
DiR dye-loaded PAS40 nanoghosts 120FreeFreeLinearLNoneSyntheticIncreases the circulation time of a cell membrane based nanotherapeuticMeasuring the residual fluorescence intensity of the dye in serum at 0, 8, 24 and 48 h50 mg/kg37Mouse serum proteaseFluorescence assayMouse serumIn VivoNoneNoneN.A.
5451
307421452019
MAQAKHKQRKRLKSSCKRHPLYVDFSDVGWNDWIVAPPGYHAFYCHGECPFPLADHLNSTNHAIVQTLVNSVNSKIPKACCVPTELSAISMLYLDENEKVVLKNYQDMVVEGCGCR
n(BMP-2)116FreeFreeLinearLNoneSyntheticPromotes Bone repairN.A.0.5 mg/kg48N.A.Fluorescence spectrometryRatsIn VivoPDB id: 1ES7Nonen(BMP-2) did not enhance ALP expression in MSCs compared with native BMP-2 unless pretreated with IV collagenase, which significantly enhanced ALP expression and calcium deposition​
5452
307421452019
MAQAKHKQRKRLKSSCKRHPLYVDFSDVGWNDWIVAPPGYHAFYCHGECPFPLADHLNSTNHAIVQTLVNSVNSKIPKACCVPTELSAISMLYLDENEKVVLKNYQDMVVEGCGCR
Native BMP-2116FreeFreeLinearLNoneSyntheticPromotes Bone repairN.A.0.5 mg/kg<30N.A.Fluorescence spectrometryRatsIn VivoPDB id: 1ES7Nonen(BMP-2) did not enhance ALP expression in MSCs compared with native BMP-2 unless pretreated with IV collagenase, which significantly enhanced ALP expression and calcium deposition​
5528
305170732019
QDSTSDLIPAPPLSKVPLQQNFQDNQFHGKWYVVGVAGNGFLREDKDPIKMAATIYELKEDKSYNVTFNKFPMKKCQYNTDTLVPGSQPGEFTLGNIKSEPGYTSWLVRVVSTNYNQHAMVFFKAVQQNREDFFITLYGRTKELTSELKENFIRFSKSLGLPENHIVFPVPIDQCIDG
D6.2178FreeFreeLinearLV69M/I80T/F83L mutation in D6.1LCN-2 derivativeTightly complexes the plant poison colchicine for use as antidote as well as bioanalytical applications 25°C 256 nM1.5N.A.Surface Plasmon Resonance (SPR) PBSIn VitroUniprot id: P80188NoneKD(pM) = 790
5529
305170732019
QDSTSDLIPAPPLSKVPLQQNFQDNQFHGKWYVVGVAGNGFLREDMDPIKMAATIYELKEDKSYNVTFMKFPMKXCQYNTDTLVPGSQPGEFTLGNIKSEPGYTSWLVRVVSTNYNQHAMVFFIAVQQNREDFFITLYGRTIELTSELKENFIRFSKSLGLPENHIVFPVPIDQCIDG
EI.1178FreeFreeLinearLK46M/K75X/N79M/ K142I mutations on D6.2LCN-2 derivativeTightly complexes the plant poison colchicine for use as antidote as well as bioanalytical applications 25°C 256 nM3.1N.A.Surface Plasmon Resonance (SPR) PBSIn VitroUniprot id: P80188NoneKD(pM) = 829
5530
305170732019
QDSTSDLIPAPPLSKVPLQQNFQDNQFHGEWYVVGVAGNGFLREDKDPIKMAATIYELKEDKSYNVTFMKFPMKKCQYNTDTLVPGSQPGEFILGNIKSEPGYTSWLVRVVSTNYNQHAMVFFKAVQQNREDFFITLYGRTKELTSELKENFIRFSKSLGLPENHIVFPVPIDQCIDG
EI.3178FreeFreeLinearLK30E/I41F/X75K/T135I/I142K mutation on El.1LCN-2 derivativeTightly complexes the plant poison colchicine for use as antidote as well as bioanalytical applications 25°C 256 nM3.4N.A.Surface Plasmon Resonance (SPR) PBSIn VitroUniprot id: P80188NoneKD(pM) = 548
5531
305170732019
QDSTSDLIPAPPLSKVPLQQNFQDNQFHGEWYVVGVAGNGFLREDKDPIKMAATIYELKEDKSYNVTFMKFPMKKCQYNTDTLVPGSQPGEFILGNIKSEPGYTSWLVRVVSTNYNQHAMVFFKAVQQNREDFFITLYGRTIELTSELKENFIRFSKSLGLPENHIVFPVPIDQCIDG
D6.4178FreeFreeLinearLK142I mutation in El.3LCN-2 derivativeTightly complexes the plant poison colchicine for use as antidote as well as bioanalytical applications 25°C 256 nM5.3N.A.Surface Plasmon Resonance (SPR) PBSIn VitroUniprot id: P80188NoneKD(pM) =622
5532
305170732019
QDSTSDLIPAPPLSKVPLQQNFQDNQFHGEWYVVGVAGNGFLREDKDPIKMAATIYELKEDKSYNVTFMKFPMKKCQYNTDTLVPGSQPGEFILGNIKSEPGYTSWLVRVVSTNYNQHAMVFFKAVQQNREDFFITLYGRTIELTSELKENFIRFSKSLGLPENHIVFPVPIDQCIDG
D6.4178FreeFreeLinearLQ77E mutationLCN-2 derivativeTightly complexes the plant poison colchicine for use as antidote as well as bioanalytical applications 25°C 256 nM6.7N.A.Surface Plasmon Resonance (SPR) PBSIn VitroUniprot id: P80188NoneKD(pM) =451
5533
305170732019
QDSTSDLIPAPPLSKVPLQQNFQDNQFHGEWYVVGVAGNGFLREDKDPIKMAATIYELKEDKSYNVTFMKFPMKKCQYNTDTLVPGSQPGEFILGNIKSEPGYTSWLVRVVSTNYNQHAMVFFKAVQQNREDFFIVLYGRTIELTSELKENFIRFSKSLGLPENHIVFPVPIDQCIDG
D6.5178FreeFreeLinearLT136V mutation in D6.4LCN-2 derivativeTightly complexes the plant poison colchicine for use as antidote as well as bioanalytical applications 25°C 256 nM6.8N.A.Surface Plasmon Resonance (SPR) PBSIn VitroUniprot id: P80188NoneKD(pM) = 620
5534
305170732019
QDSTSDLIPAPPLSKVPLQQNFQDNQFHGEWYVVGVAGNGFLREDKDPIKMAATIYELKEDKSYNVTFMKFPMKKCEYNTDTLVPGSQPGEFILGNIKSEPGYTSWLVRVVSTNYNQHAMVFFKAVQQNREDFFIVLYGRTIELTSELKENFIRFSKSLGLPENHIVFPVPIDQCIDG
D6.6178FreeFreeLinearLQ77E mutation in D6.5LCN-2 derivativeTightly complexes the plant poison colchicine for use as antidote as well as bioanalytical applications 25°C 256 nM9.4N.A.Surface Plasmon Resonance (SPR) PBSIn VitroUniprot id: P80188NoneKD(pM) = 702
5535
305040812019
(VPGAG)80
VPGAG80400A leader sequence (GCGYPG) was added to the N-terminus of the ZIPPs and ELPs to site specifically conjugate the maleimide derivative of Alexa488FreeLinearLX1 =G , X2= AZwitterionic polypeptide derivativeIntrinsically disordered zwitterionic polypeptides for drug delivery10 μl blood samples were collected into tubes with 100 μl of heparin at 40 s, 15 min, 0.5, 2, 4, 8, 24, 48 and 72 h after injection into the tail vein300 μM5.0 ± 0.1N.A.N.A.N.A.In VitroNoneNoneEC50 = 10 nM for GLP1-VPGAG160
5536
305040812019
(VPGAG)120
VPGAG120600A leader sequence (GCGYPG) was added to the N-terminus of the ZIPPs and ELPs to site specifically conjugate the maleimide derivative of Alexa488FreeLinearLX1 =G , X2= AZwitterionic polypeptide derivativeIntrinsically disordered zwitterionic polypeptides for drug delivery10 μl blood samples were collected into tubes with 100 μl of heparin at 40 s, 15 min, 0.5, 2, 4, 8, 24, 48 and 72 h after injection into the tail vein300 μM5.2 ± 0.1N.A.N.A.N.A.In VitroNoneNoneEC50 = 10 nM for GLP1-VPGAG160
5537
305040812019
(VPGAG)160
VPGAG160800A leader sequence (GCGYPG) was added to the N-terminus of the ZIPPs and ELPs to site specifically conjugate the maleimide derivative of Alexa488FreeLinearLX1 =G , X2= AZwitterionic polypeptide derivativeIntrinsically disordered zwitterionic polypeptides for drug delivery10 μl blood samples were collected into tubes with 100 μl of heparin at 40 s, 15 min, 0.5, 2, 4, 8, 24, 48 and 72 h after injection into the tail vein300 μM7.3 ± 0.2N.A.N.A.N.A.In VitroNoneNoneEC50 = 10 nM for GLP1-VPGAG160
5538
305040812019
(VPKEG)80
VPKEG80400A leader sequence (GCGYPG) was added to the N-terminus of the ZIPPs and ELPs to site specifically conjugate the maleimide derivative of Alexa488FreeLinearLX1 =K, X2= EZwitterionic polypeptide derivativeIntrinsically disordered zwitterionic polypeptides for drug delivery10 μl blood samples were collected into tubes with 100 μl of heparin at 40 s, 15 min, 0.5, 2, 4, 8, 24, 48 and 72 h after injection into the tail vein300 μM12.4 ± 0.1N.A.N.A.N.A.In VitroNoneNoneEC50 = 17 nM for GLP1-VPKEG120
5539
305040812019
(VPKEG)120
VPKEG120600A leader sequence (GCGYPG) was added to the N-terminus of the ZIPPs and ELPs to site specifically conjugate the maleimide derivative of Alexa488FreeLinearLX1 =K, X2= EZwitterionic polypeptide derivativeIntrinsically disordered zwitterionic polypeptides for drug delivery10 μl blood samples were collected into tubes with 100 μl of heparin at 40 s, 15 min, 0.5, 2, 4, 8, 24, 48 and 72 h after injection into the tail vein300 μM12.9 ± 0.2N.A.N.A.N.A.In VitroNoneNoneEC50 = 17 nM for GLP1-VPKEG120
5540
305040812019
(VPGAG)120 
VPGAG120 600A leader sequence (GCGYPG) was added to the N-terminus of the ZIPPs and ELPs to site specifically conjugate the maleimide derivative of Alexa488FreeLinearLX1 =G , X2= AZwitterionic polypeptide derivativeIntrinsically disordered zwitterionic polypeptides for drug delivery10 μl blood samples were collected into tubes with 100 μl of heparin at 40 s, 15 min, 0.5, 2, 4, 8, 24, 48 and 72 h after injection into the tail vein300 μM4.5 ± 0.2Mice plasma proteaseFluorescence assayMice plasmaIn VivoNoneNoneEC50 = 10 nM for GLP1-VPGAG160
5541
305040812019
(VPGAG)160
VPGAG160800A leader sequence (GCGYPG) was added to the N-terminus of the ZIPPs and ELPs to site specifically conjugate the maleimide derivative of Alexa488FreeLinearLX1 =G , X2= AZwitterionic polypeptide derivativeIntrinsically disordered zwitterionic polypeptides for drug delivery10 μl blood samples were collected into tubes with 100 μl of heparin at 40 s, 15 min, 0.5, 2, 4, 8, 24, 48 and 72 h after injection into the tail vein300 μM6.6 ± 0.3Mice plasma proteaseFluorescence assayMice plasmaIn VivoNoneNoneEC50 = 10 nM for GLP1-VPGAG160
5542
305040812019
(VPKEG)120 
VPKEG120 600A leader sequence (GCGYPG) was added to the N-terminus of the ZIPPs and ELPs to site specifically conjugate the maleimide derivative of Alexa488FreeLinearLX1 =K, X2= EZwitterionic polypeptide derivativeIntrinsically disordered zwitterionic polypeptides for drug delivery10 μl blood samples were collected into tubes with 100 μl of heparin at 40 s, 15 min, 0.5, 2, 4, 8, 24, 48 and 72 h after injection into the tail vein300 μM12.0 ± 0.4Mice plasma proteaseFluorescence assayMice plasmaIn VivoNoneNoneEC50 = 17 nM for GLP1-VPKEG120
5543
305040812019
(VPREG)120 
VPREG120 600A leader sequence (GCGYPG) was added to the N-terminus of the ZIPPs and ELPs to site specifically conjugate the maleimide derivative of Alexa488FreeLinearLX1 =R, X2= EZwitterionic polypeptide derivativeIntrinsically disordered zwitterionic polypeptides for drug delivery10 μl blood samples were collected into tubes with 100 μl of heparin at 40 s, 15 min, 0.5, 2, 4, 8, 24, 48 and 72 h after injection into the tail vein300 μM9.6 ± 0.5Mice plasma proteaseFluorescence assayMice plasmaIn VivoNoneNoneN.A.
5544
305040812019
(VPKDG)120
VPKDG120600A leader sequence (GCGYPG) was added to the N-terminus of the ZIPPs and ELPs to site specifically conjugate the maleimide derivative of Alexa488FreeLinearLX1 =K, X2= DZwitterionic polypeptide derivativeIntrinsically disordered zwitterionic polypeptides for drug delivery10 μl blood samples were collected into tubes with 100 μl of heparin at 40 s, 15 min, 0.5, 2, 4, 8, 24, 48 and 72 h after injection into the tail vein300 μM10.8 ± 0.2Mice plasma proteaseFluorescence assayMice plasmaIn VivoNoneNoneN.A.
5545
305040812019
(VPRDG)120 
VPRDG120 600A leader sequence (GCGYPG) was added to the N-terminus of the ZIPPs and ELPs to site specifically conjugate the maleimide derivative of Alexa488FreeLinearLX1 =R, X2= DZwitterionic polypeptide derivativeIntrinsically disordered zwitterionic polypeptides for drug delivery10 μl blood samples were collected into tubes with 100 μl of heparin at 40 s, 15 min, 0.5, 2, 4, 8, 24, 48 and 72 h after injection into the tail vein300 μM8.2 ± 0.3Mice plasma proteaseFluorescence assayMice plasmaIn VivoNoneNoneN.A.
5546
305040812019
(VPGAG)120
VPGAG120600A leader sequence (GCGYPG) was added to the N-terminus of the ZIPPs and ELPs to site specifically conjugate the maleimide derivative of Alexa488FreeLinearLX1 =G , X2= AZwitterionic polypeptide derivativeIntrinsically disordered zwitterionic polypeptides for drug delivery10 μl blood samples were collected into tubes with 100 μl of heparin at 40 s, 15 min, 0.5, 2, 4, 8, 24, 48 and 72 h after injection into the tail vein300 μM10.6 ± 1.6Mice plasma proteaseFluorescence assayMice plasmaIn VivoNoneNoneEC50 = 10 nM for GLP1-VPGAG160
5547
305040812019
(VPGAG)160
VPGAG160800A leader sequence (GCGYPG) was added to the N-terminus of the ZIPPs and ELPs to site specifically conjugate the maleimide derivative of Alexa488FreeLinearLX1 =G , X2= AZwitterionic polypeptide derivativeIntrinsically disordered zwitterionic polypeptides for drug delivery10 μl blood samples were collected into tubes with 100 μl of heparin at 40 s, 15 min, 0.5, 2, 4, 8, 24, 48 and 72 h after injection into the tail vein300 μM12.4 ± 0.8Mice plasma proteaseFluorescence assayMice plasmaIn VivoNoneNoneEC50 = 10 nM for GLP1-VPGAG160
5548
305040812019
(VPKEG)120 
VPKEG120 600A leader sequence (GCGYPG) was added to the N-terminus of the ZIPPs and ELPs to site specifically conjugate the maleimide derivative of Alexa488FreeLinearLX1 =K, X2= EZwitterionic polypeptide derivativeIntrinsically disordered zwitterionic polypeptides for drug delivery10 μl blood samples were collected into tubes with 100 μl of heparin at 40 s, 15 min, 0.5, 2, 4, 8, 24, 48 and 72 h after injection into the tail vein300 μM15.6 ± 0.6 Mice plasma proteaseFluorescence assayMice plasmaIn VivoNoneNoneEC50 = 17 nM for GLP1-VPKEG120
5549
305040812019
(VPKDG)120 
VPKDG120 600A leader sequence (GCGYPG) was added to the N-terminus of the ZIPPs and ELPs to site specifically conjugate the maleimide derivative of Alexa488FreeLinearLX1 =K, X2= DZwitterionic polypeptide derivativeIntrinsically disordered zwitterionic polypeptides for drug delivery10 μl blood samples were collected into tubes with 100 μl of heparin at 40 s, 15 min, 0.5, 2, 4, 8, 24, 48 and 72 h after injection into the tail vein300 μM11.8 ± 1 Mice plasma proteaseFluorescence assayMice plasmaIn VivoNoneNoneN.A.
5550
303341712019
CDLPQTHSLGSRRTLMLLAQMRRISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMNEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE
rhIFN-α2b165FreeFreeLinearLNoneSyntheticAntiviral, Antitumor, And Immunomodulatory EffectsN.A.500 μg/kg0.54 (Elimination Half Life)Rats plasma proteasesandwich ELISARats plasmaIn VivoPDB id: 1RH2NonerhIFN-α2b had a high specific antiviral activity (2.5 × 108 ± 1.1 × 108IU/mg protein)
5551
301652472019
MAPTSAFLTALVLLSCNAICSLGCDLPQTHSLAHTRALRLLAQMRRISPFSCLDHRRDFGSPHEAFGGNQVQKAQAMALVHEMLQQTFQLFSTEGSAAAWNESLLHQFCTGLDQQLRDLEACVMQEAGLEGTPLLEEDSILAVRKYFHRLTLYLQEKSYSPCAWEIVRAEVMRSFSSSRNLQDRLRKKEMEKEKKVKYFLRKSAFGLASVSAAFLVGSTVFAVDSPIEDTPIIRNGGELTNLLGNSETTLALRNEESATADLTAAAVADTVAAAAAENAGAAAWEAAAAADALAKAKADALKEFNKYGVSDYYKNLINNAKTVEGVKDLQAQVVESAKKARISEATDGLSDFLKSQTPAEDTVKSIELAEAKVLANRELDKYGVSDYHKNLINNAKTVEGVKDLQAQVVESAKKARISEATDGLSDFLKSQTPAEDTVKSIELAEAKVLANRELDKYGVSDYYKNLINNAKTVEGVKALIDEILAALPKTDTYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDGEWTYDDATKTFTVTEKPEVIDASELTPAVTTYKLVINGKTLKGETTTEADAATAEKVFKQYANDNGVDGEWTYDDATKTFTVTEKPEVIDASELTPAVTTYKLVINGKTLKGETTTKAVDAETAEKAFKQYANDNGVDGVWTYDDATKTFTVTEMVTEVPGDAPTEPEKPEASIPLVPLTPATPIAKDDAKKDDTKKEDAKKPEAKKEDAKKAETLPTTGEGSNPFFTAAALAVMAGAGALAVASKRKED
PoIFNα -C2781FreeSPG C2 domainLinearLNoneFusion protein of Ig-binding C2 domain of streptococcal protein G (SPG) with PoIFN-αAntiviral And Immune Regulatory EffectsSerum samples were collected at 0.5, 2.0, 4.0, 8.0, 12, 24,48, 72, 96, 120 and 144 h post injection2.5 mg/kg56.82 ± 0.70Rats serum proteaseELISARats serumIn VivoGenBank accession no. AY345969, X06173.1NoneOn MDBK cell, PoIFNα-C2 protein showed almost 10-fold lower anti-VSV activity (3.0 × 107 U/μM) than that (2.4 × 108 U/μM) of PoIFN-α standard
5552
301652472019
MAPTSAFLTALVLLSCNAICSLGCDLPQTHSLAHTRALRLLAQMRRISPFSCLDHRRDFGSPHEAFGGNQVQKAQAMALVHEMLQQTFQLFSTEGSAAAWNESLLHQFCTGLDQQLRDLEACVMQEAGLEGTPLLEEDSILAVRKYFHRLTLYLQEKSYSPCAWEIVRAEVMRSFSSSRNLQDRLRKKE
PoIFN-α 189FreeFreeLinearLNonePorcine IFN-αAntiviral And Immune Regulatory EffectsSerum samples were collected at 0.5, 2.0, 4.0, 8.0, 12, 24,48, 72, 96, 120 and 144 h post injection2.5 mg/kg4.02 ± 0.06Rats serum proteaseELISARats serumIn VivoNoneNoneOn MDBK cell, PoIFNα-C2 protein showed almost 10-fold lower anti-VSV activity (3.0 × 107 U/μM) than that (2.4 × 108 U/μM) of PoIFN-α standard
5553
301652472019
MAPTSAFLTALVLLSCNAICSLGCDLPQTHSLAHTRALRLLAQMRRISPFSCLDHRRDFGSPHEAFGGNQVQKAQAMALVHEMLQQTFQLFSTEGSAAAWNESLLHQFCTGLDQQLRDLEACVMQEAGLEGTPLLEEDSILAVRKYFHRLTLYLQEKSYSPCAWEIVRAEVMRSFSSSRNLQDRLRKKEMEKEKKVKYFLRKSAFGLASVSAAFLVGSTVFAVDSPIEDTPIIRNGGELTNLLGNSETTLALRNEESATADLTAAAVADTVAAAAAENAGAAAWEAAAAADALAKAKADALKEFNKYGVSDYYKNLINNAKTVEGVKDLQAQVVESAKKARISEATDGLSDFLKSQTPAEDTVKSIELAEAKVLANRELDKYGVSDYHKNLINNAKTVEGVKDLQAQVVESAKKARISEATDGLSDFLKSQTPAEDTVKSIELAEAKVLANRELDKYGVSDYYKNLINNAKTVEGVKALIDEILAALPKTDTYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDGEWTYDDATKTFTVTEKPEVIDASELTPAVTTYKLVINGKTLKGETTTEADAATAEKVFKQYANDNGVDGEWTYDDATKTFTVTEKPEVIDASELTPAVTTYKLVINGKTLKGETTTKAVDAETAEKAFKQYANDNGVDGVWTYDDATKTFTVTEMVTEVPGDAPTEPEKPEASIPLVPLTPATPIAKDDAKKDDTKKEDAKKPEAKKEDAKKAETLPTTGEGSNPFFTAAALAVMAGAGALAVASKRKED
PoIFNα -C2781FreeSPG C2 domainLinearLNoneFusion protein of Ig-binding C2 domain of streptococcal protein G (SPG) with PoIFN-αAntiviral And Immune Regulatory EffectsSerum samples were collected at 0.5, 2.0, 4.0, 8.0, 12, 24,48, 72, 96, 120 and 144 h post injection2.5 mg/kg61.58 ± 1.998Rats serum proteaseELISARats serumIn VivoNoneNoneOn MDBK cell, PoIFNα-C2 protein showed almost 10-fold lower anti-VSV activity (3.0 × 107 U/μM) than that (2.4 × 108 U/μM) of PoIFN-α standard
5554
301652472019
MAPTSAFLTALVLLSCNAICSLGCDLPQTHSLAHTRALRLLAQMRRISPFSCLDHRRDFGSPHEAFGGNQVQKAQAMALVHEMLQQTFQLFSTEGSAAAWNESLLHQFCTGLDQQLRDLEACVMQEAGLEGTPLLEEDSILAVRKYFHRLTLYLQEKSYSPCAWEIVRAEVMRSFSSSRNLQDRLRKKE
PoIFN-α 189FreeFreeLinearLNonePorcine IFN-αAntiviral And Immune Regulatory EffectsSerum samples were collected at 0.5, 2.0, 4.0, 8.0, 12, 24,48, 72, 96, 120 and 144 h post injection2.5 mg/kg6.54 ± 0.16Rats serum proteaseELISARats serumIn VivoNoneNoneOn MDBK cell, PoIFNα-C2 protein showed almost 10-fold lower anti-VSV activity (3.0 × 107 U/μM) than that (2.4 × 108 U/μM) of PoIFN-α standard
5565
313764862019
MRLTWTCLLTLVLVTAACEAPGEEPVPAEEAVPALKEVFADAFLVGAALNPDQFYGRDTLGVALITKHFNTITPENVMKWEQIHPEPDRYDFEAADRFVAFGEERDLFIVGHTLVWHNQTPDWVFEDDRGEPLTREALLERMRDHIQTVVGRYRGRVDGWDVVNEALNEDGTLRPTRWLEIIGEDYLAHAFRFAHEADPQAELYYNDYSLTNPAKREGAVRLVQGLLDAGVPVTGIGMQGHYALTYPTLEELETSITTFAGLGVDVMITELDVAVLPRPSEYWGADVSRREELRAELDPYREAFPDSMQQALADRYAGFFEVFLRQQEALTRVTFWGVTDGDSWLNNWPIRGRTSYPLLFDRAYRPKPAFFAVVATARE
Recombinant XynRA1379FreeFreeLinearLNoneDerived from Rhodothermaceae bacterium RAEndo-1,4-β-xylanase 60 °CN.A.1 (Activity Half Life)N.A.BCA Protein AssayN.A.In VitroUniprot id: A0A1V0DJ74NoneXynRA1 enzyme retained 80% of its maximal activity for 5 h
5574
310677822019
G(VPGVG)96Y
Rhodamine-labeled V96482FreeFreeLinearLRhodamine labelingSyntheticIncreases half life37°C, Small aliquots of the solution (100 µL) were withdrawn at predetermined intervals (5, 15, 30 min, 1, 2, 4, 8, 24, 48, 72, 96, 120, 168 h) 100 µM0.2 (T1/2 Fast Release Kinetics)N.A.Fluorescence assayProclear CompatiblesTM contact lensesIn VivoNoneNoneN.A.
5575
310677822019
G(VPGVG)96Y
Rhodamine-labeled V96482FreeFreeLinearLRhodamine labelingSyntheticIncreases half life37°C, Small aliquots of the solution (100 µL) were withdrawn at predetermined intervals (5, 15, 30 min, 1, 2, 4, 8, 24, 48, 72, 96, 120, 168 h) 100 µM4615 (T1/2 Slow Release Kinetics)N.A.Fluorescence assayProclear CompatiblesTM contact lensesIn VivoNoneNoneN.A.
5576
310677822019
G(VPGVG)96Y
Rhodamine-labeled V96482FreeFreeLinearLRhodamine labelingSyntheticIncreases half life4°C, Small aliquots of the solution (100 µL) were withdrawn at predetermined intervals (5, 15, 30 min, 1, 2, 4, 8, 24, 48, 72, 96, 120, 168 h) 100 µM0.2 (T1/2 Fast Release Kinetics)N.A.Fluorescence assayProclear CompatiblesTM contact lensesIn VivoNoneNoneN.A.
5577
310677822019
G(VPGVG)96Y
Rhodamine-labeled V96482FreeFreeLinearLRhodamine labelingSyntheticIncreases half life4°C, Small aliquots of the solution (100 µL) were withdrawn at predetermined intervals (5, 15, 30 min, 1, 2, 4, 8, 24, 48, 72, 96, 120, 168 h) 100 µM96.2 (T1/2 Slow Release Kinetics)N.A.Fluorescence assayProclear CompatiblesTM contact lensesIn VivoNoneNoneN.A.
5578
310677822019
G(VPGSG)96Y
Rhodamine-labeled S96482FreeFreeLinearLRhodamine labelingSyntheticIncreases half life37°C, Small aliquots of the solution (100 µL) were withdrawn at predetermined intervals (5, 15, 30 min, 1, 2, 4, 8, 24, 48, 72, 96, 120, 168 h) 100 µM0.2 (T1/2 Fast Release Kinetics)N.A.Fluorescence assayProclear CompatiblesTM contact lensesIn VivoNoneNoneN.A.
5579
310677822019
G(VPGSG)96Y
Rhodamine-labeled S96482FreeFreeLinearLRhodamine labelingSyntheticIncreases half life37°C, Small aliquots of the solution (100 µL) were withdrawn at predetermined intervals (5, 15, 30 min, 1, 2, 4, 8, 24, 48, 72, 96, 120, 168 h) 100 µM137.1 (T1/2 Slow Release Kinetics)N.A.Fluorescence assayProclear CompatiblesTM contact lensesIn VivoNoneNoneN.A.
5580
310677822019
G(VPGVG)96Y
V96482FreeFreeLinearLNoneSyntheticIncreases half lifeN.A.N.A.4 (Retention Half Life)N.A.N.A.SolutionN.A.NoneNoneN.A.
5636
304965752018
GPVPTSKPTTTKGGCHIGRFKSLSPQELASFKKARDALEESLKLKNWSCSSPVFPGNWDLRLLQVRERPVALEAELALTLKVLEAAAGPALEDVLDQPLHTLHHILSQLQACIQPQPTAGPRPRGRLHHWLHRLQEAPKKESAGCLEASVTFNLFRLLTRDLKYVADGNLCLRTSTHPEST
rhIFN-λ1181FreeHuman chorionic gonadotropin β subunit carboxyl-terminal peptide (CTP) and an N-glycosylation sequence linked to its C-terminusLinearLNoneRecombinant human interferon-λ1Antiviral, Antiproliferation, And Nk Cell Cytotoxicity-Promoting ActivitiesVenous blood was collected at 0.5 h, 1 h, 2 h, 4 h, 8 h, and 24 h post-injection40 μg/kg3.37 ± 0.70Mice blood proteaseELISAMice blood sampleIn VivoNoneNoneAntiviral activity of the purified rhIFN-λ1 expressed by CHO cells was 2.5 × 105 IU/mg 
5637
304965752018
GPVPTSKPTTTKGGCHIGRFKSLSPQELASFKKARDALEESLKLKNWSCSSPVFPGNWDLRLLQVRERPVALEAELALTLKVLEAAAGPALEDVLDQPLHTLHHILSQLQACIQPQPTAGPRPRGRLHHWLHRLQEAPKKESAGCLEASVTFNLFRLLTRDLKYVADGNLCLRTSTHPESTSSGSSSSSSSKAPPPSLPSPSRLPGPSDTPILPQNGS
rhIFN-λ1-CTPON218FreeHuman chorionic gonadotropin β subunit carboxyl-terminal peptide (CTP) and an N-glycosylation sequence linked to its C-terminus via linkerLinearLNoneRecombinant human interferon-λ1 derivativeAntiviral, Antiproliferation, And Nk Cell Cytotoxicity-Promoting ActivitiesVenous blood was collected at 0.5 h, 1 h, 2 h, 4 h, 8 h, and 24 h post-injection40 μg/kg10.326 ± 0.87Mice blood proteaseELISAMice blood sampleIn VivoNoneNoneAntiviral activity of the purified rhIFN-λ1 expressed by CHO cells was 2.5 × 105 IU/mg 
5659
301610022018
SVRSSSRTPSDKPVAHVVANPQAEGQLQWLNRRANALLANGVELRDNQLVVPSEGLYLIYSQVLFKGQGCPSTHVLLTHTISRIAVSYQTKVNLLSAIKSPCQRETPEGAEAKPWYEPIYLGGVFQLEKGDRLSAEINRPDYLDFAESGQVYFGIIAL
TNF-a158FreeFreeLinearLNoneTNF-aAntitumorOrbital blood samples were collected from 3 mice at different time points (0, 0.25, 0.5, 1, 2, 4, 8, 12, 16, 24, and 48 h)5 mg/kg0.43BALB/c mice plasma proteaseLC-MSBALB/c mice plasmaIn VivoPDB id: 6OP0NoneN.A.
5762
296698112018
MKYLLPTAAAGLLLLAAQPAMAAHHHHHHGSSGGGENLYFQGSSGQVQLVQSGAEVKKPGASVKVSCKASGYTFTDHAIHWVRQAPGQRLEWMGYFSPGNDDFKYSQKFQGRVTITADKSSSTAYMELSSLRSEDTAVYYCARSWIMQYWGQGTLVTVSSGGGGSDIVMTQSPDSLAVSLGERATINCKSSQSVLYSSNNKNYLAWYQQKPGQPPKLLIYWASTRESGVPDRFSGSGSGTDFTLTISSLQAEDVAVYYCQQYYSYPLTFGGGTKVEIK
125I-3E8.G4S278125I labelledFreeLinearL125I-labeled, VH and VL joined by G4S linkerDerived from the 3E8 antibodyOptimizes biophysical properties, serum half-life and high-specificity tumor imagingBlood samples (5 μl) were drawn from the saphenous vein by puncture, using a 30-gauge syringe needle, at 0.5, 1, 5, 24, 48, and 72 h postinjection for 3E8.G4S5 μCi0.67Mice blood proteaseRadioiodination assayMice blood sampleIn Vivohttps://pmc.ncbi.nlm.nih.gov/articles/instance/5995523/bin/supp_RA118.002538_136163_1_supp_109995_p6kvvq.pdfNoneKD of 3.6 nM for 3E8.G4S
5763
296698112018
MKYLLPTAAAGLLLLAAQPAMAAHHHHHHGSSGGGENLYFQGSSGQVQLVQSGAEVKKPGASVKVSCKASGYTFTDHAIHWVRQAPGQRLEWMGYFSPGNDDFKYSQKFQGRVTITADKSSSTAYMELSSLRSEDTAVYYCARSWIMQYWGQGTLVTVSSGGGGSDIVMTQSPDSLAVSLGERATINCKSSQSVLYSSNNKNYLAWYQQKPGQPPKLLIYWASTRESGVPDRFSGSGSGTDFTLTISSLQAEDVAVYYCQQYYSYPLTFGGGTKVEIK-GGGGS-125I-MKYLLPTAAAGLLLLAAQPAMAAHHHHHHGSSGGGENLYFQGSSGQVQLVQSGAEVKKPGASVKVSCKASGYTFTDHAIHWVRQAPGQRLEWMGYFSPGNDDFKYSQKFQGRVTITADKSSSTAYMELSSLRSEDTAVYYCARSWIMQYWGQGTLVTVSSGGGGSDIVMTQSPDSLAVSLGERATINCKSSQSVLYSSNNKNYLAWYQQKPGQPPKLLIYWASTRESGVPDRFSGSGSGTDFTLTISSLQAEDVAVYYCQQYYSYPLTFGGGTKVEIK
125I-3E8.G4S dimer561125I labelledFreeLinearL125I-labeled, 2 ScFv joined by G4S linkerDerived from the 3E8 antibodyOptimizes biophysical properties, serum half-life and high-specificity tumor imagingBlood samples (5 μl) were drawn from the saphenous vein by puncture, using a 30-gauge syringe needle, at 0.5, 1, 5, 24, 48, and 72 h postinjection for 3E8.G4S5 μCi2Mice blood proteaseRadioiodination assayMice blood sampleIn VivoNoneNoneKD of 3.6 nM for 3E8.G4S
5764
296698112018
MKYLLPTAAAGLLLLAAQPAMAAHHHHHHGSSGGGENLYFQGSSGQVQLVQSGAEVKKPGASVKVSCKASGYTFTDHAIHWVRQAPGQRLEWMGYFSPGNDDFKYSQKFQGRVTITADKSSSTAYMELSSLRSEDTAVYYCARSWIMQYWGQGTLVTVSSGGGGSDIVMTQSPDSLAVSLGERATINCKSSQSVLYSSNNKNYLAWYQQKPGQPPKLLIYWASTRESGVPDRFSGSGSGTDFTLTISSLQAEDVAVYYCQQYYSYPLTFGGGTKVEIK-GGGGS-125I-MKYLLPTAAAGLLLLAAQPAMAAHHHHHHGSSGGGENLYFQGSSGQVQLVQSGAEVKKPGASVKVSCKASGYTFTDHAIHWVRQAPGQRLEWMGYFSPGNDDFKYSQKFQGRVTITADKSSSTAYMELSSLRSEDTAVYYCARSWIMQYWGQGTLVTVSSGGGGSDIVMTQSPDSLAVSLGERATINCKSSQSVLYSSNNKNYLAWYQQKPGQPPKLLIYWASTRESGVPDRFSGSGSGTDFTLTISSLQAEDVAVYYCQQYYSYPLTFGGGTKVEIK-GGGGS-125I-MKYLLPTAAAGLLLLAAQPAMAAHHHHHHGSSGGGENLYFQGSSGQVQLVQSGAEVKKPGASVKVSCKASGYTFTDHAIHWVRQAPGQRLEWMGYFSPGNDDFKYSQKFQGRVTITADKSSSTAYMELSSLRSEDTAVYYCARSWIMQYWGQGTLVTVSSGGGGSDIVMTQSPDSLAVSLGERATINCKSSQSVLYSSNNKNYLAWYQQKPGQPPKLLIYWASTRESGVPDRFSGSGSGTDFTLTISSLQAEDVAVYYCQQYYSYPLTFGGGTKVEIK
125I-3E8.G4S oligomer (Trimeric)844125I labelledFreeLinearL125I-labeled, 3 ScFv joined by G4S linkerDerived from the 3E8 antibodyOptimizes biophysical properties, serum half-life and high-specificity tumor imaging0.5, 1.5, 3, 6, 24, 48, and 72 h 5 μCi3.3Mice blood proteaseRadioiodination assayMice blood sampleIn VivoNoneNoneKD of 3.6 nM for 3E8.G4S
5765
296698112018
MKYLLPTAAAGLLLLAAQPAMAAHHHHHHGSSGGGENLYFQGSSGQVQLVQSGAEVKKPGASVKVSCKASGYTFTDHAIHWVRQAPGQRLEWMGYFSPGNDDFKYSQKFQGRVTITADKSSSTAYMELSSLRSEDTAVYYCARSWIMQYWGQGTLVTVSSGGGGSDIVMTQSPDSLAVSLGERATINCKSSQSVLYSSNNKNYLAWYQQKPGQPPKLLIYWASTRESGVPDRFSGSGSGTDFTLTISSLQAEDVAVYYCQQYYSYPLTFGGGTKVEIK-GGGGS-125I-MKYLLPTAAAGLLLLAAQPAMAAHHHHHHGSSGGGENLYFQGSSGQVQLVQSGAEVKKPGASVKVSCKASGYTFTDHAIHWVRQAPGQRLEWMGYFSPGNDDFKYSQKFQGRVTITADKSSSTAYMELSSLRSEDTAVYYCARSWIMQYWGQGTLVTVSSGGGGSDIVMTQSPDSLAVSLGERATINCKSSQSVLYSSNNKNYLAWYQQKPGQPPKLLIYWASTRESGVPDRFSGSGSGTDFTLTISSLQAEDVAVYYCQQYYSYPLTFGGGTKVEIK-GGGGS-125I-MKYLLPTAAAGLLLLAAQPAMAAHHHHHHGSSGGGENLYFQGSSGQVQLVQSGAEVKKPGASVKVSCKASGYTFTDHAIHWVRQAPGQRLEWMGYFSPGNDDFKYSQKFQGRVTITADKSSSTAYMELSSLRSEDTAVYYCARSWIMQYWGQGTLVTVSSGGGGSDIVMTQSPDSLAVSLGERATINCKSSQSVLYSSNNKNYLAWYQQKPGQPPKLLIYWASTRESGVPDRFSGSGSGTDFTLTISSLQAEDVAVYYCQQYYSYPLTFGGGTKVEIK-GGGGS-125I-MKYLLPTAAAGLLLLAAQPAMAAHHHHHHGSSGGGENLYFQGSSGQVQLVQSGAEVKKPGASVKVSCKASGYTFTDHAIHWVRQAPGQRLEWMGYFSPGNDDFKYSQKFQGRVTITADKSSSTAYMELSSLRSEDTAVYYCARSWIMQYWGQGTLVTVSSGGGGSDIVMTQSPDSLAVSLGERATINCKSSQSVLYSSNNKNYLAWYQQKPGQPPKLLIYWASTRESGVPDRFSGSGSGTDFTLTISSLQAEDVAVYYCQQYYSYPLTFGGGTKVEIK
125I-3E8.G4S oligomer (Tetrameric)1127125I labelledFreeLinearL125I-labeled, 4 ScFv joined by G4S linkerDerived from the 3E8 antibodyOptimizes biophysical properties, serum half-life and high-specificity tumor imaging0.5, 1.5, 3, 6, 24, 48, and 72 h 5 μCi3.3Mice blood proteaseRadioiodination assayMice blood sampleIn VivoNoneNoneKD of 3.6 nM for 3E8.G4S
5899
N.A.2018
QRVAAHITGTRGRSNTLSSPNSKNEKALGRKINSWESSRSGHSFLSNLHLRNGELVIHEKGFYYIYSQTYFRFQEEIKENTKNDKQMVQYIYKYTSYPDPILLMKSARNSCWSKDAEYGLYSIYQGGIFELKENDRIFVSVTNEHLIDMDHEASFFGAFLVGSSGSSGSSGSGLPDVASLRQQVEALQGQVQHLQAAFSQYKKVELFPNGQSVGEKIFKTAGFVKPFTEAQLLCTQAGGQLASPRSAAENAALQQLVVAKNEAAFLSMTDSKTEGKFTYPTGESLVYSNWAPGEPNDDGGSEDCVEIFTNGKWNDRACGEKRLVVCEFGGSPSSSSSSAWSHPQFEK
TRAIL-ASPD347FreeC-type lectin domain of human SP-D joined with Strep-tag II using linkerLinearLNoneTrail-SPD Fusion ProteinTherapeutic, diagnostic and/or research applicationsSerum samples were collected after several time points (predose, 5 min., 30 min., 2H, 6H and 24H)10 μg 7CD1 mice serum proteaseELISACD1 mice serumIn VivoNoneEP 17197297 ATRAIL-SPD fusion proteins induced no hepatotoxic effects, even if ligands were secondarily cross-linked by antibodies
5900
N.A.2018
QRVAAHITGTRGRSNTLSSPNSKNEKALGRKINSWESSRSGHSFLSNLHLRNGELVIHEKGFYYIYSQTYFRFQEEIKENTKNDKQMVQYIYKYTSYPDPILLMKSARNSCWSKDAEYGLYSIYQGGIFELKENDRIFVSVTNEHLIDMDHEASFFGAFLVGSSGSSGSSGSGLPDVASLRQQVEALQGQVQHLQAAFSQYKKVELFPNGQSVGEKIFKTAGFVKPFTEAQLLCTQAGGQLASPRSAAENAALQQLVVAKNEAAFLSMTDSKTEGKFTYPTGESLVYSNWAPGEPNDDGGSEDCVEIDTNGKWNDRACGEKRLVVCEFGGSPSSSSSSAWSHPQFEK
TRAIL-ASPD_F335D 347FreeC-type lectin domain of human SP-D joined with Strep-tag II using linkerLinearLPhe355 -> Asp355 modificationTrail-SPD Fusion ProteinTherapeutic, diagnostic and/or research applicationsSerum samples were collected after several time points (predose, 5 min., 30 min., 2H, 6H and 24H)10 μg 14CD1 mice serum proteaseELISACD1 mice serumIn VivoNoneEP 17197297 AFive hours of co-incubation of primary human hepatocytes with trimeric TRAIL-ASPD_F335D together with chemotherapeutic drugs induced no caspase activity (E)
5924
293856662018
MKGSWWRRVAMIALSAGLLAGSLSMGTGIRKADAAAGNQNYAEALQKAIYFYEAQRSGPLPASNRVEWRGNSGIQDGADVGVDLTGGWYDAGDHVKFGFPMAASATMLAWSVVEYSDGYEQAGQLEEIKDNIRWATDYFMKAHTKPNELWGQVGAGNTDHAWWGPAEVMQMNRPSFKIDASCPGSDLAAETAAALAASSIVFADDDPAYSARLLQHAKELYNFAYTYRGEYTDCITDAAAFYNSWTGYEDELAWGGAWLYLATNDSAYLSKAIAATDRWSSSGGSANWPYTWTQGWDSKHYGAQILLARITSSLNMPEATRFIQSTERNLDYWTVGVNGTRVKYTPGGLAWLDQWGSLRYAANASFISFVYSDWVSDPVKKSRYQDFAVSQMNYILGDNPRQSSYVVGYGQNAPQHPHHRTAHGSWLNNEDIPANHRHILYGAMVGGPDASDGYTDDIGDYVSNEVATDYNAGFTGALAKMNLLFGQNHQPLANFPAPEVKGDEFFVEAAIKSSGANYTEIRAQLNNRSAWPARMGDQLSFKYFLDLSEVYAAGRTVSDVQVTTSYTEGATVSQPVVVNAAQHIYAITANFGNTKIYPGGEGNYRKEVQFRITGPQGAWNASNDHSFQTLTTGTPVKSIYLPVYDAGVKVYGQEPGLTPVTVPGAPAGVQAVAGSSQVNLTWAAVSGAESYTVKRSEVSGGPYTTVATGVNGLTYTNTGLTNGTTYYYVVTAVNSAGESSGSVQVSATPQAASTVPGALTLSGTAGNAQSVLTWTTASGATTYKVQRSVAGGTYADVATGLSVLTYTDTTALNGTTYNYRIAAVNANGQTLSNVLALTPSAPPVTTGTLEVQYRSGGSGNSSNAATPQFNVKNTGTQAIDLSTVKIRYYFTKDGADQMTFWCDYAEMGTANVEGTFVTVNPAKGTADTYLEISFKSGAGSLAAGAETGVIQARFSKNNWSNFDLSNDYSYDASKTAFAAWNKVTGYQGNTKVWGLEP
Cel9K997FreeFreeLinearLNoneCloned using the shot-gun method from Paenibacillus sp. X4Endo-β-1,4-glucanase 50°CN.A.59.2 (Activity Half Life)N.A.N.A.Cel9KIn VitroNoneNoneN.A.
5927
300638372018
DSDDRVTPPAEPLDRMPDP-(3-chloro-Tyr)-RPSYGRAETVVNNYIRKWQQVYSHRDGRKQQMTEEQREWLS-(3-choro-Tyr)-GCVGVTWVNSGQYPTNRLAFASFDEDRFKNELKNGRPRSGETRAEFEGRVAKESFDEEKGFQRAREVASVMNRALENAHDESAYLDNLKKELANGNDALRNEDARSPF-(3-chloro-Tyr)-SALRNTPSFKERNGGNHDPSRMKAVIYSKHFWSGQDRSSSADKRKYGDPDAFRPAPGTGLVDMSRDRNIPRSPTSPGEGFVNFDYGWFGAQTEADADKTVWTHGNHYHAPNGSLGAMHVYESKFRNWSEGYSDFDRGAYVITFIPKSWNTAPDKVKQGWP
MTG variant331FreeFreeLinearLClY20/62/171 modifications, ClY = 3-Chloro-TyrosineDerived from Streptoverticillium mobaraenseTransglutaminase60°C for 10 minN.A.5.1-Fold Longer Than That Of The Wild-Type Enzyme (Activity Half Life)N.A.N.A.BufferIn Vitropdb id: 1IU4NoneN.A.
5951
288214622017
MTTASTSQVRQNYHQDSEAAINRQINLELYASYVYLSMSYYFDRDDVALKNFAKYFLHQSHEEREHAEKLMKLQNQRGGRIFLQDIQKPDCDDWESGLNAMECALHLEKNVNQSLLELHKLATDKNDPHLCDFIETHYLNEQVKAIKELGDHVTNLRKMGAPESGLAEYLFDKHTLGDSDNES
wtFN183FreeFreeLinearLCy5 dye (Lumiprobe) were chemically conjugated to the amine groups of lysine residues on the exterior surface of the nanocagesSyntheticAntitumorN.A.50 mg/kg1.1 ± 0.1Mice plasma proteaseFluorescence assayMice plasmaIn VivoPDB id: 1FHANoneN.A.
5952
288214622017
MTTASTSQVRQNYHQDSEAAINRQINLELYASYVYLSMSYYFDRDDVALKNFAKYFLHQSHEEREHAEKLMKLQNQRGGRIFLQDIQKPDCDDWESGLNAMECALHLEKNVNQSLLELHKLATDKNDPHLCDFIETHYLNEQVKAIKELGDHVTNLRKMGAPESGLAEYLFDKHTLGDSDNESGSSGGSGSSGGSGGGDEADGSRGSQKAGVDE
LCFN36183FreeFusing the XTEN peptide of 36 amino acids through a linkerLinearLGly-rich linker (GSSGGSGSSGGSGGGDEADGSRGSQKAGVDE) is used, Cy5 dye (Lumiprobe) were chemically conjugated to the amine groups of lysine residues on the exterior surface of the nanocageswtFN derivativeAntitumorN.A.50 mg/kg3.5 ± 0.3Mice plasma proteaseFluorescence assayMice plasmaIn VivoNoneNoneN.A.
5953
288214622017
MTTASTSQVRQNYHQDSEAAINRQINLELYASYVYLSMSYYFDRDDVALKNFAKYFLHQSHEEREHAEKLMKLQNQRGGRIFLQDIQKPDCDDWESGLNAMECALHLEKNVNQSLLELHKLATDKNDPHLCDFIETHYLNEQVKAIKELGDHVTNLRKMGAPESGLAEYLFDKHTLGDSDNESGSSGGSGSSGGSGGGDEADGSRGSQKAGVDE
LCFN72183FreeFusing the XTEN peptide of 72 amino acids through a linkerLinearLGly-rich linker (GSSGGSGSSGGSGGGDEADGSRGSQKAGVDE) is used, Cy5 dye (Lumiprobe) were chemically conjugated to the amine groups of lysine residues on the exterior surface of the nanocageswtFN derivativeAntitumorN.A.50 mg/kg5.5 ± 0.1Mice plasma proteaseFluorescence assayMice plasmaIn VivoNoneNoneN.A.
5954
288214622017
MTTASTSQVRQNYHQDSEAAINRQINLELYASYVYLSMSYYFDRDDVALKNFAKYFLHQSHEEREHAEKLMKLQNQRGGRIFLQDIQKPDCDDWESGLNAMECALHLEKNVNQSLLELHKLATDKNDPHLCDFIETHYLNEQVKAIKELGDHVTNLRKMGAPESGLAEYLFDKHTLGDSDNESGSSGGSGSSGGSGGGDEADGSRGSQKAGVDE
LCFN144183FreeFusing the XTEN peptide of 144 amino acids through a linkerLinearLGly-rich linker (GSSGGSGSSGGSGGGDEADGSRGSQKAGVDE) is used, Cy5 dye (Lumiprobe) were chemically conjugated to the amine groups of lysine residues on the exterior surface of the nanocageswtFN derivativeAntitumorN.A.50 mg/kg11.3 ± 1.0Mice plasma proteaseFluorescence assayMice plasmaIn VivoNoneNoneN.A.
5955
288214622017
MTTASTSQVRQNYHQDSEAAINRQINLELYASYVYLSMSYYFDRDDVALKNFAKYFLHQSHEEREHAEKLMKLQNQRGGRIFLQDIQKPDCDDWESGLNAMECALHLEKNVNQSLLELHKLATDKNDPHLCDFIETHYLNEQVKAIKELGDHVTNLRKMGAPESGLAEYLFDKHTLGDSDNESGSSGGSGSSGGSGGGDEADGSRGSQKAGVDE
LCFN288183FreeFusing the XTEN peptide of 288 amino acids through a linkerLinearLGly-rich linker (GSSGGSGSSGGSGGGDEADGSRGSQKAGVDE) is used, Cy5 dye (Lumiprobe) were chemically conjugated to the amine groups of lysine residues on the exterior surface of the nanocageswtFN derivativeAntitumorN.A.50 mg/kg10.2 ± 0.3Mice plasma proteaseFluorescence assayMice plasmaIn VivoNoneNoneN.A.
5958
287993262017
DAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLVAASQAALGL
WT-albumin585FreeFreeLinearLNoneProduced by secretion from yeastCarrier proteinBlood samples were collected from the tail vessel in time intervals of predose 0.5, 1, 2, 4, 8, 12, 24, 48, 72, 96, 120, 144, 168 and 192 hours5 mg/kg21.5NMR1 mice serum proteaseAlphaLISANMR1 mice serumIn VivoNoneNoneKD±SD (nM) = 548.7 ±90.2 against human FcRn receptor
5959
287993262017
HGEGTFTSDVSSYLEGQAAKEFIAWLVKGRKDAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLVAASQAALGL
GLP-1-PEG-WT-albumin616FreeGLP-1 modified PEG-Mal group reacts with the free C34 of rHSA, chemical group attached between Lys31 (8-amino-3,6-dioxaoctanoyl-maleimidopropionyl) and D32LinearLNoneProduced by secretion from yeastAntidiabetesBlood samples were collected from the tail vessel in time intervals of predose 0.5, 1, 2, 4, 8, 12, 24, 48, 72, 96, 120, 144, 168 and 192 hours5 mg/kg8.5NMR1 mice serum proteaseAlphaLISANMR1 mice serumIn VivoNoneNoneKD±SD (nM) = 856.5±94.9 against human FcRn receptor
5960
287993262017
HGEGTFTSDVSSYLEGQAAKEFIAWLVKGRKDAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGPKLVAASQAALGL
GLP-1-PEG-HB-albumin616FreeGLP-1 modified PEG-Mal group reacts with the free C34 of rHSA, chemical group attached between Lys31 (8-amino-3,6-dioxaoctanoyl-maleimidopropionyl) and D32LinearLK573P modification in HSA,GLP-1 modified with PEG-maleimideProduced by secretion from yeastAntidiabetesBlood samples were collected from the tail vessel in time intervals of predose 0.5, 1, 2, 4, 8, 12, 24, 48, 72, 96, 120, 144, 168 and 192 hours5 mg/kg9.9NMR1 mice serum proteaseAlphaLISANMR1 mice serumIn VivoNoneNoneKD±SD (nM) = 26.1±2.7 against human FcRn receptor
5970
287215922017
MAGPATQSPMKLMALQLLLWHSALWTVQEATPLGPASSLPQSFLLKCLEQVRKIQGDGAALQEKLCATYKLCHPEELVLLGHSLGIPWAPLSSCPSQALQLAGCLSQLHSGLFLYQGLLQALEGISPELGPTLDTLQLDVADFATTIWQQMEELGMAPALQPTQGAMPAFASAFQRRAGGVLVASHLQSFLEVSYRVLRHLAQP
G-CSF204Met addition at N terminal of G-CSFFreeLinearLNoneHuman derivedSelectively stimulate proliferation Blood samples were drawn from the rats at selected time points (0, 3, 6, 12, 18, and 24 h after injection)150 μg/kg 1.2Rats serum proteaseELISARats serumIn VivoGenbank accession no. NM_172219Nonein vitro activity of GCSF-La reached 48% of that of the G-CSF monomer
5971
287215922017
MAGPATQSPMKLMALQLLLWHSALWTVQEATPLGPASSLPQSFLLKCLEQVRKIQGDGAALQEKLCATYKLCHPEELVLLGHSLGIPWAPLSSCPSQALQLAGCLSQLHSGLFLYQGLLQALEGISPELGPTLDTLQLDVADFATTIWQQMEELGMAPALQPTQGAMPAFASAFQRRAGGVLVASHLQSFLEVSYRVLRHLAQPSGLEAEAAAKEAAAKEAAAKEAAAKALEAEAAAKEAAAKEAAAKEAAAKALEGSMAGPATQSPMKLMALQLLLWHSALWTVQEATPLGPASSLPQSFLLKCLEQVRKIQGDGAALQEKLCATYKLCHPEELVLLGHSLGIPWAPLSSCPSQALQLAGCLSQLHSGLFLYQGLLQALEGISPELGPTLDTLQLDVADFATTIWQQMEELGMAPALQPTQGAMPAFASAFQRRAGGVLVASHLQSFLEVSYRVLRHLAQP
GCSF-Lα462Met addition at N terminal of G-CSFFreeLinearLDimer joined by linker La - SGLEA–(EAAAK)4–ALEA–(EAAAK)4–ALEGSHomodimeric G-CSF Selectively stimulate proliferation Blood samples were drawn from the rats at selected time points (0, 3, 6, 12, 18, and 24 h after injection)150 μg/kg 8.7Rats serum proteaseELISARats serumIn VivoGenbank accession no. NM_172219Nonein vitro activity of GCSF-La reached 48% of that of the G-CSF monomer
5982
287117302017
MAFTEHSPLTPHRRDLCSRSIWLARKIRSDLTALTESYVKHQGLNKNINLDSADGMPVASTDQWSELTEAERLQENLQAYRTFHVLLARLLEDQQVHFTPTEGDFHQAIHTLLLQVAAFAYQIEELMILLEYKIPRNEADGMPINVGDGGLFEKKLWGLKVLQELSQWTVRSIHDLRFISSHQTGIP
rhCNTF187FreeFreeLinearLNoneSyntheticTreatment of Neurodegenerative or Metabolic diseasesAt different time points (15min, 45min, 90min, 3h, 6h, 12h, 24h and 48h) 1 mg/kg34.28SD rats serum proteaseELISASD rats serumIn VivoPDB id: 1CNTNoneEC50±SD = 0.48±0.12ng/ml for rhCNTF 
5983
287117302017
MAFTEHSPLTPHRRDLCSRSIWLARKIRSDLTALTESYVKHQGLNKNINLDSADGMPVASTDQWSELTEAERLQENLQAYRTFHVLLARLLEDQQVHFTPTEGDFHQAIHTLLLQVAAFAYQIEELMILLEYKIPRNEADGMPINVGDGGLFEKKLWGLKVLQELSQWTVRSIHDLRFISSHQTGIP(GGGGSGGGGSGGGGSAMALAEAKVLANRELDKYGVSDFYKRLINKAKTVEGVEALKLHILAALP
rhCNTF-ABD251FreeABD035LinearLLinked by (G4S)3 linkerFusion of recombinant human CNTF (rhCNTF) with an albumin-binding domain (ABD)Treatment of Neurodegenerative or Metabolic diseasesAt different time points (15min, 45min, 90min, 3h, 6h, 12h, 24h and 48h) 1 mg/kg483.39SD rats serum proteaseELISASD rats serumIn VivoNoneNoneEC50±SD = 0.51±0.18 for rhCNTF-ABD 
5984
287117302017
MAFTEHSPLTPHRRDLCSRSIWLARKIRSDLTALTESYVKHQGLNKNINLDSADGMPVASTDQWSELTEAERLQENLQAYRTFHVLLARLLEDQQVHFTPTEGDFHQAIHTLLLQVAAFAYQIEELMILLEYKIPRNEADGMPINVGDGGLFEKKLWGLKVLQELSQWTVRSIHDLRFISSHQTGIP
PEG-20k-rhCNTF 187PEGylation (20KDa)FreeLinearLNoneSyntheticTreatment of Neurodegenerative or Metabolic diseasesAt different time points (15min, 45min, 90min, 3h, 6h, 12h, 24h and 48h) 1 mg/kg441.24SD rats serum proteaseELISASD rats serumIn VivoNoneNoneEC50±SD = 0.48±0.12ng/ml for rhCNTF 
5985
287117302017
MAFTEHSPLTPHRRDLCSRSIWLARKIRSDLTALTESYVKHQGLNKNINLDSADGMPVASTDQWSELTEAERLQENLQAYRTFHVLLARLLEDQQVHFTPTEGDFHQAIHTLLLQVAAFAYQIEELMILLEYKIPRNEADGMPINVGDGGLFEKKLWGLKVLQELSQWTVRSIHDLRFISSHQTGIP
PEG-40k-rhCNTF 187PEGylation (40KDa)FreeLinearLNoneSyntheticTreatment of Neurodegenerative or Metabolic diseasesAt different time points (15min, 45min, 90min, 3h, 6h, 12h, 24h and 48h) 1 mg/kg523.89SD rats serum proteaseELISASD rats serumIn VivoNoneNoneEC50±SD = 0.48±0.12ng/ml for rhCNTF 
6031
283239652017
SSSSKAPPPSLPSPSRLPGPSDTPILPQFPTIPLSRLFQNAMLRAHRLHQLAFDTYEEFEEAYIPKEQKYSFLQAPQASLCFSESIPTPSNREQAQQKSNLQLLRISLLLIQSWLEPVGFLRSVFANSLVYGASDSDVYDLLKDLEEGIQTLMGRLEDGSPRTGQAFKQTYAKFDANSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGFSSSSKAPPPSLPSPSRLPGPSDTPILPQSSSSKAPPPSLPSPSRLPGPSDTPILPQ
MOD-4023275CTP fused to hGH2 CTP fusedLinearLNoneSyntheticTreatment of GHDMeasured at the final randomized dose (following the second dose)0.25 mg/kg36.1Human serum proteaseIDS-iSys chemiluminescence assayHuman serumIn Vivohttps://pmc.ncbi.nlm.nih.gov/articles/PMC3159989/, PDB id: 1HGU, https://sci-hub.se/10.1021/acs.molpharmaceut.5b00868NoneEC50 = 15.8 ± 2.0 ng/ml (Proliferation of BAFB2B2 cells)
6032
283239652017
SSSSKAPPPSLPSPSRLPGPSDTPILPQFPTIPLSRLFQNAMLRAHRLHQLAFDTYEEFEEAYIPKEQKYSFLQAPQASLCFSESIPTPSNREQAQQKSNLQLLRISLLLIQSWLEPVGFLRSVFANSLVYGASDSDVYDLLKDLEEGIQTLMGRLEDGSPRTGQAFKQTYAKFDANSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGFSSSSKAPPPSLPSPSRLPGPSDTPILPQSSSSKAPPPSLPSPSRLPGPSDTPILPQ
MOD-4023275CTP fused to hGH2 CTP fusedLinearLNoneSyntheticTreatment of GHDMeasured at the final randomized dose (following the second dose)0.48 mg/kg18.3Human serum proteaseIDS-iSys chemiluminescence assayHuman serumIn Vivohttps://pmc.ncbi.nlm.nih.gov/articles/PMC3159989/, PDB id: 1HGU, https://sci-hub.se/10.1021/acs.molpharmaceut.5b00868NoneEC50 = 15.8 ± 2.0 ng/ml (Proliferation of BAFB2B2 cells)
6033
283239652017
SSSSKAPPPSLPSPSRLPGPSDTPILPQFPTIPLSRLFQNAMLRAHRLHQLAFDTYEEFEEAYIPKEQKYSFLQAPQASLCFSESIPTPSNREQAQQKSNLQLLRISLLLIQSWLEPVGFLRSVFANSLVYGASDSDVYDLLKDLEEGIQTLMGRLEDGSPRTGQAFKQTYAKFDANSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGFSSSSKAPPPSLPSPSRLPGPSDTPILPQSSSSKAPPPSLPSPSRLPGPSDTPILPQ
MOD-4023275CTP fused to hGH2 CTP fusedLinearLNoneSyntheticTreatment of GHDMeasured at the final randomized dose (following the second dose)0.66 mg/kg22.4Human serum proteaseIDS-iSys chemiluminescence assayHuman serumIn Vivohttps://pmc.ncbi.nlm.nih.gov/articles/PMC3159989/, PDB id: 1HGU, https://sci-hub.se/10.1021/acs.molpharmaceut.5b00868NoneEC50 = 15.8 ± 2.0 ng/ml (Proliferation of BAFB2B2 cells)
6034
283239652017
FPTIPLSRLFQNAMLRAHRLHQLAFDTYEEFEEAYIPKEQKYSFLQAPQASLCFSESIPTPSNREQAQQKSNLQLLRISLLLIQSWLEPVGFLRSVFANSLVYGASDSDVYDLLKDLEEGIQTLMGRLEDGSPRTGQAFKQTYAKFDANSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF
r-HGH191FreeFreeLinearLNoneSyntheticTreatment of GHDMeasured following 2 weeks of daily administration0.24 mg/kg3.5Human serum proteaseIDS-iSys chemiluminescence assayHuman serumIn Vivohttps://pmc.ncbi.nlm.nih.gov/articles/PMC3159989/, PDB id: 1HGU, https://sci-hub.se/10.1021/acs.molpharmaceut.5b00868NoneEC50 = 0.36 ± 0.06 ng/ml (Proliferation of BAFB2B2 cells)
6035
282818682017
DAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLVAASQAALGLMALCKFCDVRFSTCDNQKSCMSNCSITSICEKPQEVCVAVWRKNDENITLETVCHDPKLPYHDFILEDAASPTCIMKEKKKPGETFFMCSCSSDECNDNIIFSEEYNTSNPD
HSA-eTGFBR2697FreeeTGFBR2 fused at the C-terminal of HSALinearLNoneSyntheticNeutralize TGF-Β1 activityBlood samples were collected 5 min, 15 min, 30 min, 1 h, 2 h, 6 h,12 h, 24 h3 nmol/kg11.84Mice serum proteaseHuman TGF-b RII Duo Set ELISA Mice serumIn Vivopdb id: 4P7U, 7DJNNoneKD = 1.42* 10-8M of HSA-eTGFBR2 for TGF-B1
6036
282818682017
MALCKFCDVRFSTCDNQKSCMSNCSITSICEKPQEVCVAVWRKNDENITLETVCHDPKLPYHDFILEDAASPTCIMKEKKKPGETFFMCSCSSDECNDNIIFSEEYNTSNPD
eTGFBR2112FreeFreeLinearLNoneSyntheticNeutralize TGF-Β1 activityBlood samples were collected through the eyes at 5 min, 15 min, 30 min, 60 min, 120 min3 nmol/kg41.42Mice serum proteaseHuman TGF-b RII Duo Set ELISA Mice serumIn VivoNoneNoneKD = 9.49* 10-9M of eTGFBR2 for TGF-B1
6071
277846922017
MCGPGVG-(VPGxG)160-VPGWPGSG
ELP815FreeFreeLinearLx = Val,Gly or AlaSyntheticCarrier proteinWhole-animal fluorescence images were collected at regular intervals for 24 hours100 mg/kg52.6 (T1/2,Terminal)Rats plasma proteasewhole-body fluorescence imaging Rats plasmaIn VivoNoneNoneKTP-ELP, ELP, and SynB1-ELP show no toxicity in any of the renal cell lines tested, even at concentrations up to 40 μM for 72 hours
6072
277846922017
MCLPVASCGGPGVG-(VPGxG)160-VPGWPGSGGC
KTP-ELP822Conjugation of KTP cyclic peptide at N terminalFreeLinearLx = Val,Gly or AlaFusion protein of KTP and ELPCarrier proteinWhole-animal fluorescence images were collected at regular intervals for 24 hours100 mg/kg234.83 (T1/2,Terminal)Rats plasma proteasewhole-body fluorescence imaging Rats plasmaIn VivoNoneNoneKTP-ELP, ELP, and SynB1-ELP show no toxicity in any of the renal cell lines tested, even at concentrations up to 40 μM for 72 hours
6073
277846922017
MCGPGVG-(VPGxG)160-VPGWPGSG
ELP815FreeFreeLinearLx = Val,Gly or AlaSyntheticCarrier proteinWhole-animal fluorescence images were collected at regular intervals for 24 hours5 mg/kg90.3 (T1/2,Terminal)Swine plasma proteasewhole-body fluorescence imaging Swine plasmaIn VivoNoneNoneKTP-ELP, ELP, and SynB1-ELP show no toxicity in any of the renal cell lines tested, even at concentrations up to 40 μM for 72 hours
6074
277846922017
MCLPVASCGGPGVG-(VPGxG)160-VPGWPGSGGC
KTP-ELP822Conjugation of KTP cyclic peptide at N terminalFreeLinearLx = Val,Gly or AlaFusion protein of KTP and ELPCarrier proteinWhole-animal fluorescence images were collected at regular intervals for 24 hours5 mg/kg118.6 (T1/2,Terminal)Swine plasma proteasewhole-body fluorescence imaging Swine plasmaIn VivoNoneNoneKTP-ELP, ELP, and SynB1-ELP show no toxicity in any of the renal cell lines tested, even at concentrations up to 40 μM for 72 hours
6083
N.A.2017
ASDEEIQDVSGTWYLKAMTVDRFKIASWPRSVTPMTLTTLEGGNLEAKVTMNWWGRSQEVKAVLERTDEPGKYTAQGDRHVAYIIRSPVKDHYIFYSEGNLQGETVPGVWLVGRDPKNNLEALEDFEKAAGARGLSTESILIPRQSETSSPG
SEQ ID NO 62152FreeFreeLinearLNoneLipocalin muteins Pcsk9-Specific Lipocalin MuteinsN.A.N.A.0.99Rats plasma proteaseSandwich ELISARats plasmaIn VivoNoneUS 201715445066 AIC50(nM) = 1.36 without HSA for LDLR binding
6084
N.A.2017
GASDEEIQDVSGTWYLKAMTVDRFKIASWPRSVTPMTLTTLEGGNLEAKVTMNWWGRSQEVKAVLERTDEPGKYTAQGDRHVAYIIRSHVKDHYIFYSEGNLQGETVPGVWLVGRDPKNNLEALEDFEKAAGARGLSTESILIPRQSETSSPG
SEQ ID NO 82153FreeFreeLinearLNoneLipocalin muteins Pcsk9-Specific Lipocalin MuteinsN.A.N.A.0.86Rats plasma proteaseSandwich ELISARats plasmaIn VivoNoneUS 201715445066 AIC50(nM) = 1.68 without HSA for LDLR binding
6085
N.A.2017
ASDEEIQDVSGTWYLKAMTVDRFKIASWPRSVTPMTLTTLEGGNLEAKVTMNWWGRSQEVKAVLERTDEPGKYTAQGDRHVAYIIRSPVKDHYIFYSEGNLQGETVPGVWLVGRDPKNNLEALEDFEKAAGARGLSTESILIPRQSETSSPGGGGSLAEAKEAANAELDSYGVSDFYKRLIDKAKTVEGVEALKDAILAALPG
SEQ ID NO 83203FreeABP-G148 (Albumin binding protein) conjugationLinearLNoneLipocalin muteins Pcsk9-Specific Lipocalin MuteinsN.A.N.A.24Rats plasma proteaseSandwich ELISARats plasmaIn VivoNoneUS 201715445066 AIC50(nM) = 1.93 without HSA for LDLR binding
6086
N.A.2017
GASDEEIQDVSGTWYLKAMTVDRFKIASWPRSVTPMTLTTLEGGNLEAKVTMNWWGRSQEVKAVLERTDEPGKYTAQGDRHVAYIIRSHVKDHYIFYSEGNLQGETVPGVWLVGRDPKNNLEALEDFEKAAGARGLSTESILIPRQSETSSPGKLGGGGSLAEAKEAANAELDSYGVSDFYKRLIDKAKTVEGVEALKDAILAALPGKLN
SEQ ID NO 84210FreeABP-G148 (Albumin binding protein) conjugationLinearLNoneLipocalin muteins Pcsk9-Specific Lipocalin MuteinsN.A.N.A.32Rats plasma proteaseSandwich ELISARats plasmaIn VivoNoneUS 201715445066 AIC50(nM) = 1.09 without HSA for LDLR binding
6097
277846922017
MCGPGVG-(VPGxG)160-VPGWPGSG
ELP815FreeFreeLinearLx = Val,Gly or AlaSyntheticCarrier proteinWhole-animal fluorescence images were collected at regular intervals for 24 hours100 mg/kg3.63 (T1/2,Distribution)Rats plasma proteasewhole-body fluorescence imaging Rats plasmaIn VivoNoneNoneN.A.
6098
277846922017
MCLPVASCGGPGVG-(VPGxG)160-VPGWPGSGGC
KTP-ELP822Conjugation of KTP cyclic peptide at N terminalFreeLinearLx = Val,Gly or AlaFusion protein of KTP and ELPCarrier proteinWhole-animal fluorescence images were collected at regular intervals for 24 hours100 mg/kg39.12 (T1/2,Distribution)Rats plasma proteasewhole-body fluorescence imaging Rats plasmaIn VivoNoneNoneN.A.
6099
277846922017
MCGPGVG-(VPGxG)160-VPGWPGSG
ELP815FreeFreeLinearLx = Val,Gly or AlaSyntheticCarrier proteinWhole-animal fluorescence images were collected at regular intervals for 24 hours5 mg/kg3.8 (T1/2,Distribution)Swine plasma proteasewhole-body fluorescence imaging Swine plasmaIn VivoNoneNoneN.A.
6100
277846922017
MCLPVASCGGPGVG-(VPGxG)160-VPGWPGSGGC
KTP-ELP822Conjugation of KTP cyclic peptide at N terminalFreeLinearLx = Val,Gly or AlaFusion protein of KTP and ELPcarriersWhole-animal fluorescence images were collected at regular intervals for 24 hours5 mg/kg6 (T1/2,Distribution)Swine plasma proteasewhole-body fluorescence imaging Swine plasmaIn VivoNoneNoneN.A.
6101
287176542017
N.A.
RT1.14opt-in561FreeFreeLinearL(D185N, D186N, E478Q) amino acid modificationsDerived from HIV-1 MNInduce oxidative stressAfter 0, 2, 4, and 6 hours of incubation, the cells were harvested, lysedN.A.2 (Activity Half Life)HeLa cells lysate protease, E64 (10 μM),leupeptin (10 μg/ml), aprotinin (10 μg/ml), pepstatin A (7,5 μM), MG132 (5 μM), or epoxomicin (0,1 μM)Cycloheximide chase assay and Western blotHeLa cells lysate after treatment with cycloheximideIn VivoTransfection route**NoneLysates of 105 cells expressing RT1.14opt-in retained 0,00012% activity
6102
287176542017
RNPTMSMSFLLAGGLVLAMTLGVGA
RT1.14oil586N-Terminally fused to a leader signal sequence from the NS1 protein Rt1.14LinearL(D185N, D186N, E478Q) amino acid modificationsDerived from HIV-1 MNInduce oxidative stressAfter 0, 2, 4, and 6 hours of incubation, the cells were harvested, lysedN.A.~15 (Activity Half Life)HeLa cells lysate protease, E64 (10 μM),leupeptin (10 μg/ml), aprotinin (10 μg/ml), pepstatin A (7,5 μM), MG132 (5 μM), or epoxomicin (0,1 μM)Cycloheximide chase assay and Western blotHeLa cells lysate after treatment with cycloheximideIn VivoTransfection route**NoneLysates of 105 cells expressing RT1.14oil retained 0,00005% of the activity
6118
273936542016
CDLPQTHSLGSRRTLMLLAQMRKISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE
IFN-α165FreeFreeLinearLNoneHuman derivedAntiproliferative, Immunoregulatory and AntiviralAt desired time points (1, 5, 15, 30 min, 1, 3, 6, 24,48, 72 and 96 h)1 mg IFN-α equivalent/kg1.49 (T1/2b-Terminal Half Life) Mice plasma proteaseELISAMice plasmaIn VivoPDB id: 1ITFNoneIC50 = 10.77 pg/mL
6119
273936542016
CDLPQTHSLGSRRTLMLLAQMRKISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE-(PMPC)
IFN-PMPC165Freepoly(2-methacryloyloxyethyl phosphorylcholine)LinearLNoneHuman derivedAntiproliferative, Immunoregulatory and AntiviralAt desired time points (1, 5, 15, 30 min, 1, 3, 6, 24,48, 72 and 96 h)1 mg IFN-α equivalent/kg51.6 (T1/2b-Terminal Half Life) Mice plasma proteaseELISAMice plasmaIn VivoNoneNoneIC50 = 20.02 pg/mL
6172
268064902016
CDLPQTHSLGSRRTLMLLAQMRRISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMNEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE
Wild-type IFN165FreeFreeLinearLNoneRecombinant human IFN-α2bAntiviral, AnticancerN.A.1*106 U / 200 g1.4 ± 0.3 (Elimination Half Life)Wistar rats plasma proteaseN.A.Female Wistar rats plasmaIn VivoPDB id: 1RH2NoneSpecific antiviral bioactivity (U ng−1) = 185 ± 30, Specific antiproliferative bioactivity (U ng−1) = 309 ± 65
6173
268064902016
SSSSKAPPPSLPSPSRLPGPSDTPILPQCDLPQTHSLGSRRTLMLLAQMRRISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMNEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE
CTP-IFN193CTP ( the terminal peptide of the β subunit of human chorionic gonadotropin (hCG))FreeLinearLNoneRecombinant human IFN-α2bAntiviral, AnticancerN.A.1*106 U / 200 g7.8 ± 0.7 (Elimination Half Life)Wistar rats plasma proteaseN.A.Female Wistar rats plasmaIn VivoPDB id: 1HCNNoneSpecific antiviral bioactivity (U ng−1) = 65 ± 3, Specific antiproliferative bioactivity (U ng−1) = 19 ± 9
6174
268064902016
CDLPQTHSLGSRRTLMLLAQMRRISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMNEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKESSSSKAPPPSLPSPSRLPGPSDTPILPQ
IFN-CTP193FreeCTP ( the terminal peptide of the β subunit of human chorionic gonadotropin (hCG))LinearLNoneRecombinant human IFN-α2bAntiviral, AnticancerN.A.1*106 U / 200 g8.4 ± 1.5 (Elimination Half Life)Wistar rats plasma proteaseN.A.Female Wistar rats plasmaIn VivoNoneNoneSpecific antiviral bioactivity (U ng−1) = 58 ± 6, Specific antiproliferative bioactivity (U ng−1) = 26 ± 8
6175
268064902016
SSSSKAPPPSLPSPSRLPGPSDTPILPQCDLPQTHSLGSRRTLMLLAQMRRISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMNEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE-SSSSKAPPPSLPSPSRLPGPSDTPILPQ
CTP-IFN-CTP221CTP ( the terminal peptide of the β subunit of human chorionic gonadotropin (hCG))CTP ( the terminal peptide of the β subunit of human chorionic gonadotropin (hCG))LinearLNoneRecombinant human IFN-α2bAntiviral, AnticancerN.A.1*106 U / 200 g13.4 ± 1.5 (Elimination Half Life)Wistar rats plasma proteaseN.A.Female Wistar rats plasmaIn VivoNoneNoneSpecific antiviral bioactivity (U ng−1) = 44 ± 3, Specific antiproliferative bioactivity (U ng−1) = 9 ± 1
6180
267547852016
MDTQTQTKLTVGCKCNPCKCQPLCKCGTTSSCNCQPCENCDPCSCNPCKCGATESCQCNPCKCAECKCCTHAVKTSACKCDPCSCNPCKCGVTQSCQCNPCTCAECKC
TfCuMT108FreeFreeCyclic (4 Disulfide Bond Cys-Cys)LNoneCopper metallothionein derived from ciliate Tetrahymena farahensisInvolved in metal homeostasis and metal detoxification by forming metal-thiolate complex37°CN.A.103N.A.SDS PAGESonicated sample (20ml) +5 ml SDS loading buffer (50% glycerol, 10% SDS,0.5 M dithiothreitol, 0.25% bromophenol blue, 0.25 M Tris-Cl pH6.8)In VitroNoneNoneN.A.
6199
267138392016
SSSSKAPPPSLPSPSRLPGPSDTPILPQFPTIPLSRLFQNAMLRAHRLHQLAFDTYEEFEEAYIPKEQKYSFLQAPQASLCFSESIPTPSNREQAQQKSNLQLLRISLLLIQSWLEPVGFLRSVFANSLVYGASDSDVYDLLKDLEEGIQTLMGRLEDGSPRTGQAFKQTYAKFDANSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF-(SSSSKAPPPSLPSPSRLPGPSDTPILPQSSSSKAPPPSLPSPSRLPGPSDTPILPQ
MOD-4023275CTP fused to hGH2 CTP fusedLinearLNoneSyntheticTreatment of GHDDay 13.6 mg/kg3.12Rats serum proteaseSandwich ELISARats serumIn Vivohttps://pmc.ncbi.nlm.nih.gov/articles/PMC3159989/, PDB id: 1HGUNoneEC50 = 15.8 ± 2.0 ng/ml (Proliferation of BAFB2B2 cells)
6200
267138392016
SSSSKAPPPSLPSPSRLPGPSDTPILPQFPTIPLSRLFQNAMLRAHRLHQLAFDTYEEFEEAYIPKEQKYSFLQAPQASLCFSESIPTPSNREQAQQKSNLQLLRISLLLIQSWLEPVGFLRSVFANSLVYGASDSDVYDLLKDLEEGIQTLMGRLEDGSPRTGQAFKQTYAKFDANSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF-(SSSSKAPPPSLPSPSRLPGPSDTPILPQSSSSKAPPPSLPSPSRLPGPSDTPILPQ
MOD-4023275CTP fused to hGH2 CTP fusedLinearLNoneSyntheticTreatment of GHDDay 13.6 mg/kg4.33Rats serum proteaseSandwich ELISARats serumIn Vivohttps://pmc.ncbi.nlm.nih.gov/articles/PMC3159989/, PDB id: 1HGUNoneEC50 = 15.8 ± 2.0 ng/ml (Proliferation of BAFB2B2 cells)
6201
267138392016
SSSSKAPPPSLPSPSRLPGPSDTPILPQFPTIPLSRLFQNAMLRAHRLHQLAFDTYEEFEEAYIPKEQKYSFLQAPQASLCFSESIPTPSNREQAQQKSNLQLLRISLLLIQSWLEPVGFLRSVFANSLVYGASDSDVYDLLKDLEEGIQTLMGRLEDGSPRTGQAFKQTYAKFDANSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF-(SSSSKAPPPSLPSPSRLPGPSDTPILPQSSSSKAPPPSLPSPSRLPGPSDTPILPQ
MOD-4023275CTP fused to hGH2 CTP fusedLinearLNoneSyntheticTreatment of GHDDay 136 mg/kg3.69Rats serum proteaseSandwich ELISARats serumIn Vivohttps://pmc.ncbi.nlm.nih.gov/articles/PMC3159989/, PDB id: 1HGUNoneEC50 = 15.8 ± 2.0 ng/ml (Proliferation of BAFB2B2 cells)
6202
267138392016
SSSSKAPPPSLPSPSRLPGPSDTPILPQFPTIPLSRLFQNAMLRAHRLHQLAFDTYEEFEEAYIPKEQKYSFLQAPQASLCFSESIPTPSNREQAQQKSNLQLLRISLLLIQSWLEPVGFLRSVFANSLVYGASDSDVYDLLKDLEEGIQTLMGRLEDGSPRTGQAFKQTYAKFDANSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF-(SSSSKAPPPSLPSPSRLPGPSDTPILPQSSSSKAPPPSLPSPSRLPGPSDTPILPQ
MOD-4023275CTP fused to hGH2 CTP fusedLinearLNoneSyntheticTreatment of GHDDay 136 mg/kg5.18Rats serum proteaseSandwich ELISARats serumIn Vivohttps://pmc.ncbi.nlm.nih.gov/articles/PMC3159989/, PDB id: 1HGUNoneEC50 = 15.8 ± 2.0 ng/ml (Proliferation of BAFB2B2 cells)
6203
267138392016
SSSSKAPPPSLPSPSRLPGPSDTPILPQFPTIPLSRLFQNAMLRAHRLHQLAFDTYEEFEEAYIPKEQKYSFLQAPQASLCFSESIPTPSNREQAQQKSNLQLLRISLLLIQSWLEPVGFLRSVFANSLVYGASDSDVYDLLKDLEEGIQTLMGRLEDGSPRTGQAFKQTYAKFDANSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF-(SSSSKAPPPSLPSPSRLPGPSDTPILPQSSSSKAPPPSLPSPSRLPGPSDTPILPQ
MOD-4023275CTP fused to hGH2 CTP fusedLinearLNoneSyntheticTreatment of GHDDay 1180 mg/kg4.79Rats serum proteaseSandwich ELISARats serumIn Vivohttps://pmc.ncbi.nlm.nih.gov/articles/PMC3159989/, PDB id: 1HGUNoneEC50 = 15.8 ± 2.0 ng/ml (Proliferation of BAFB2B2 cells)
6204
267138392016
SSSSKAPPPSLPSPSRLPGPSDTPILPQFPTIPLSRLFQNAMLRAHRLHQLAFDTYEEFEEAYIPKEQKYSFLQAPQASLCFSESIPTPSNREQAQQKSNLQLLRISLLLIQSWLEPVGFLRSVFANSLVYGASDSDVYDLLKDLEEGIQTLMGRLEDGSPRTGQAFKQTYAKFDANSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF-(SSSSKAPPPSLPSPSRLPGPSDTPILPQSSSSKAPPPSLPSPSRLPGPSDTPILPQ
MOD-4023275CTP fused to hGH2 CTP fusedLinearLNoneSyntheticTreatment of GHDDay 1180 mg/kg5.5Rats serum proteaseSandwich ELISARats serumIn Vivohttps://pmc.ncbi.nlm.nih.gov/articles/PMC3159989/, PDB id: 1HGUNoneEC50 = 15.8 ± 2.0 ng/ml (Proliferation of BAFB2B2 cells)
6205
267138392016
SSSSKAPPPSLPSPSRLPGPSDTPILPQFPTIPLSRLFQNAMLRAHRLHQLAFDTYEEFEEAYIPKEQKYSFLQAPQASLCFSESIPTPSNREQAQQKSNLQLLRISLLLIQSWLEPVGFLRSVFANSLVYGASDSDVYDLLKDLEEGIQTLMGRLEDGSPRTGQAFKQTYAKFDANSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF-(SSSSKAPPPSLPSPSRLPGPSDTPILPQSSSSKAPPPSLPSPSRLPGPSDTPILPQ
MOD-4023275CTP fused to hGH2 CTP fusedLinearLNoneSyntheticTreatment of GHDDay 263.6 mg/kg6.6Rats serum proteaseSandwich ELISARats serumIn Vivohttps://pmc.ncbi.nlm.nih.gov/articles/PMC3159989/, PDB id: 1HGUNoneEC50 = 15.8 ± 2.0 ng/ml (Proliferation of BAFB2B2 cells)
6206
267138392016
SSSSKAPPPSLPSPSRLPGPSDTPILPQFPTIPLSRLFQNAMLRAHRLHQLAFDTYEEFEEAYIPKEQKYSFLQAPQASLCFSESIPTPSNREQAQQKSNLQLLRISLLLIQSWLEPVGFLRSVFANSLVYGASDSDVYDLLKDLEEGIQTLMGRLEDGSPRTGQAFKQTYAKFDANSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF-(SSSSKAPPPSLPSPSRLPGPSDTPILPQSSSSKAPPPSLPSPSRLPGPSDTPILPQ
MOD-4023275CTP fused to hGH2 CTP fusedLinearLNoneSyntheticTreatment of GHDDay 263.6 mg/kg7.75Rats serum proteaseSandwich ELISARats serumIn Vivohttps://pmc.ncbi.nlm.nih.gov/articles/PMC3159989/, PDB id: 1HGUNoneEC50 = 15.8 ± 2.0 ng/ml (Proliferation of BAFB2B2 cells)
6207
267138392016
SSSSKAPPPSLPSPSRLPGPSDTPILPQFPTIPLSRLFQNAMLRAHRLHQLAFDTYEEFEEAYIPKEQKYSFLQAPQASLCFSESIPTPSNREQAQQKSNLQLLRISLLLIQSWLEPVGFLRSVFANSLVYGASDSDVYDLLKDLEEGIQTLMGRLEDGSPRTGQAFKQTYAKFDANSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF-(SSSSKAPPPSLPSPSRLPGPSDTPILPQSSSSKAPPPSLPSPSRLPGPSDTPILPQ
MOD-4023275CTP fused to hGH2 CTP fusedLinearLNoneSyntheticTreatment of GHDDay 2636 mg/kg3.71Rats serum proteaseSandwich ELISARats serumIn Vivohttps://pmc.ncbi.nlm.nih.gov/articles/PMC3159989/, PDB id: 1HGUNoneEC50 = 15.8 ± 2.0 ng/ml (Proliferation of BAFB2B2 cells)
6208
267138392016
SSSSKAPPPSLPSPSRLPGPSDTPILPQFPTIPLSRLFQNAMLRAHRLHQLAFDTYEEFEEAYIPKEQKYSFLQAPQASLCFSESIPTPSNREQAQQKSNLQLLRISLLLIQSWLEPVGFLRSVFANSLVYGASDSDVYDLLKDLEEGIQTLMGRLEDGSPRTGQAFKQTYAKFDANSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF-(SSSSKAPPPSLPSPSRLPGPSDTPILPQSSSSKAPPPSLPSPSRLPGPSDTPILPQ
MOD-4023275CTP fused to hGH2 CTP fusedLinearLNoneSyntheticTreatment of GHDDay 2636 mg/kg5.36Rats serum proteaseSandwich ELISARats serumIn Vivohttps://pmc.ncbi.nlm.nih.gov/articles/PMC3159989/, PDB id: 1HGUNoneEC50 = 15.8 ± 2.0 ng/ml (Proliferation of BAFB2B2 cells)
6209
267138392016
SSSSKAPPPSLPSPSRLPGPSDTPILPQFPTIPLSRLFQNAMLRAHRLHQLAFDTYEEFEEAYIPKEQKYSFLQAPQASLCFSESIPTPSNREQAQQKSNLQLLRISLLLIQSWLEPVGFLRSVFANSLVYGASDSDVYDLLKDLEEGIQTLMGRLEDGSPRTGQAFKQTYAKFDANSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF-(SSSSKAPPPSLPSPSRLPGPSDTPILPQSSSSKAPPPSLPSPSRLPGPSDTPILPQ
MOD-4023275CTP fused to hGH2 CTP fusedLinearLNoneSyntheticTreatment of GHDDay 26180 mg/kg6.24Rats serum proteaseSandwich ELISARats serumIn Vivohttps://pmc.ncbi.nlm.nih.gov/articles/PMC3159989/, PDB id: 1HGUNoneEC50 = 15.8 ± 2.0 ng/ml (Proliferation of BAFB2B2 cells)
6210
267138392016
SSSSKAPPPSLPSPSRLPGPSDTPILPQFPTIPLSRLFQNAMLRAHRLHQLAFDTYEEFEEAYIPKEQKYSFLQAPQASLCFSESIPTPSNREQAQQKSNLQLLRISLLLIQSWLEPVGFLRSVFANSLVYGASDSDVYDLLKDLEEGIQTLMGRLEDGSPRTGQAFKQTYAKFDANSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF-(SSSSKAPPPSLPSPSRLPGPSDTPILPQSSSSKAPPPSLPSPSRLPGPSDTPILPQ
MOD-4023275CTP fused to hGH2 CTP fusedLinearLNoneSyntheticTreatment of GHDDay 26180 mg/kg6.2Rats serum proteaseSandwich ELISARats serumIn Vivohttps://pmc.ncbi.nlm.nih.gov/articles/PMC3159989/, PDB id: 1HGUNoneEC50 = 15.8 ± 2.0 ng/ml (Proliferation of BAFB2B2 cells)
6211
267138392016
SSSSKAPPPSLPSPSRLPGPSDTPILPQFPTIPLSRLFQNAMLRAHRLHQLAFDTYEEFEEAYIPKEQKYSFLQAPQASLCFSESIPTPSNREQAQQKSNLQLLRISLLLIQSWLEPVGFLRSVFANSLVYGASDSDVYDLLKDLEEGIQTLMGRLEDGSPRTGQAFKQTYAKFDANSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF-(SSSSKAPPPSLPSPSRLPGPSDTPILPQSSSSKAPPPSLPSPSRLPGPSDTPILPQ
MOD-4023275CTP fused to hGH2 CTP fusedLinearLNoneSyntheticTreatment of GHDDay 11.5 mg/kg12.76 ± 2.06Monkeys serum proteaseSandwich ELISAMonkeys serumIn Vivohttps://pmc.ncbi.nlm.nih.gov/articles/PMC3159989/, PDB id: 1HGUNoneEC50 = 15.8 ± 2.0 ng/ml (Proliferation of BAFB2B2 cells)
6212
267138392016
SSSSKAPPPSLPSPSRLPGPSDTPILPQFPTIPLSRLFQNAMLRAHRLHQLAFDTYEEFEEAYIPKEQKYSFLQAPQASLCFSESIPTPSNREQAQQKSNLQLLRISLLLIQSWLEPVGFLRSVFANSLVYGASDSDVYDLLKDLEEGIQTLMGRLEDGSPRTGQAFKQTYAKFDANSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF-(SSSSKAPPPSLPSPSRLPGPSDTPILPQSSSSKAPPPSLPSPSRLPGPSDTPILPQ
MOD-4023275CTP fused to hGH2 CTP fusedLinearLNoneSyntheticTreatment of GHDDay 11.5 mg/kg16.17 ± 2.30Monkeys serum proteaseSandwich ELISAMonkeys serumIn Vivohttps://pmc.ncbi.nlm.nih.gov/articles/PMC3159989/, PDB id: 1HGUNoneEC50 = 15.8 ± 2.0 ng/ml (Proliferation of BAFB2B2 cells)
6213
267138392016
SSSSKAPPPSLPSPSRLPGPSDTPILPQFPTIPLSRLFQNAMLRAHRLHQLAFDTYEEFEEAYIPKEQKYSFLQAPQASLCFSESIPTPSNREQAQQKSNLQLLRISLLLIQSWLEPVGFLRSVFANSLVYGASDSDVYDLLKDLEEGIQTLMGRLEDGSPRTGQAFKQTYAKFDANSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF-(SSSSKAPPPSLPSPSRLPGPSDTPILPQSSSSKAPPPSLPSPSRLPGPSDTPILPQ
MOD-4023275CTP fused to hGH2 CTP fusedLinearLNoneSyntheticTreatment of GHDDay 115 mg/kg15.88 ± 0.98Monkeys serum proteaseSandwich ELISAMonkeys serumIn Vivohttps://pmc.ncbi.nlm.nih.gov/articles/PMC3159989/, PDB id: 1HGUNoneEC50 = 15.8 ± 2.0 ng/ml (Proliferation of BAFB2B2 cells)
6214
267138392016
SSSSKAPPPSLPSPSRLPGPSDTPILPQFPTIPLSRLFQNAMLRAHRLHQLAFDTYEEFEEAYIPKEQKYSFLQAPQASLCFSESIPTPSNREQAQQKSNLQLLRISLLLIQSWLEPVGFLRSVFANSLVYGASDSDVYDLLKDLEEGIQTLMGRLEDGSPRTGQAFKQTYAKFDANSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF-(SSSSKAPPPSLPSPSRLPGPSDTPILPQSSSSKAPPPSLPSPSRLPGPSDTPILPQ
MOD-4023275CTP fused to hGH2 CTP fusedLinearLNoneSyntheticTreatment of GHDDay 115 mg/kg15.47 ± 1.84Monkeys serum proteaseSandwich ELISAMonkeys serumIn Vivohttps://pmc.ncbi.nlm.nih.gov/articles/PMC3159989/, PDB id: 1HGUNoneEC50 = 15.8 ± 2.0 ng/ml (Proliferation of BAFB2B2 cells)
6215
267138392016
SSSSKAPPPSLPSPSRLPGPSDTPILPQFPTIPLSRLFQNAMLRAHRLHQLAFDTYEEFEEAYIPKEQKYSFLQAPQASLCFSESIPTPSNREQAQQKSNLQLLRISLLLIQSWLEPVGFLRSVFANSLVYGASDSDVYDLLKDLEEGIQTLMGRLEDGSPRTGQAFKQTYAKFDANSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF-(SSSSKAPPPSLPSPSRLPGPSDTPILPQSSSSKAPPPSLPSPSRLPGPSDTPILPQ
MOD-4023275CTP fused to hGH2 CTP fusedLinearLNoneSyntheticTreatment of GHDDay 130 mg/kg16.66 ± 2.41Monkeys serum proteaseSandwich ELISAMonkeys serumIn Vivohttps://pmc.ncbi.nlm.nih.gov/articles/PMC3159989/, PDB id: 1HGUNoneEC50 = 15.8 ± 2.0 ng/ml (Proliferation of BAFB2B2 cells)
6216
267138392016
SSSSKAPPPSLPSPSRLPGPSDTPILPQFPTIPLSRLFQNAMLRAHRLHQLAFDTYEEFEEAYIPKEQKYSFLQAPQASLCFSESIPTPSNREQAQQKSNLQLLRISLLLIQSWLEPVGFLRSVFANSLVYGASDSDVYDLLKDLEEGIQTLMGRLEDGSPRTGQAFKQTYAKFDANSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF-(SSSSKAPPPSLPSPSRLPGPSDTPILPQSSSSKAPPPSLPSPSRLPGPSDTPILPQ
MOD-4023275CTP fused to hGH2 CTP fusedLinearLNoneSyntheticTreatment of GHDDay 130 mg/kg16.93 ± 2.01Monkeys serum proteaseSandwich ELISAMonkeys serumIn Vivohttps://pmc.ncbi.nlm.nih.gov/articles/PMC3159989/, PDB id: 1HGUNoneEC50 = 15.8 ± 2.0 ng/ml (Proliferation of BAFB2B2 cells)
6217
267138392016
SSSSKAPPPSLPSPSRLPGPSDTPILPQFPTIPLSRLFQNAMLRAHRLHQLAFDTYEEFEEAYIPKEQKYSFLQAPQASLCFSESIPTPSNREQAQQKSNLQLLRISLLLIQSWLEPVGFLRSVFANSLVYGASDSDVYDLLKDLEEGIQTLMGRLEDGSPRTGQAFKQTYAKFDANSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF-(SSSSKAPPPSLPSPSRLPGPSDTPILPQSSSSKAPPPSLPSPSRLPGPSDTPILPQ
MOD-4023275CTP fused to hGH2 CTP fusedLinearLNoneSyntheticTreatment of GHDDay 1811.5 mg/kg15.40 ± 7.39Monkeys serum proteaseSandwich ELISAMonkeys serumIn Vivohttps://pmc.ncbi.nlm.nih.gov/articles/PMC3159989/, PDB id: 1HGUNoneEC50 = 15.8 ± 2.0 ng/ml (Proliferation of BAFB2B2 cells)
6218
267138392016
SSSSKAPPPSLPSPSRLPGPSDTPILPQFPTIPLSRLFQNAMLRAHRLHQLAFDTYEEFEEAYIPKEQKYSFLQAPQASLCFSESIPTPSNREQAQQKSNLQLLRISLLLIQSWLEPVGFLRSVFANSLVYGASDSDVYDLLKDLEEGIQTLMGRLEDGSPRTGQAFKQTYAKFDANSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF-(SSSSKAPPPSLPSPSRLPGPSDTPILPQSSSSKAPPPSLPSPSRLPGPSDTPILPQ
MOD-4023275CTP fused to hGH2 CTP fusedLinearLNoneSyntheticTreatment of GHDDay 1811.5 mg/kg17.01 ± 6.91Monkeys serum proteaseSandwich ELISAMonkeys serumIn Vivohttps://pmc.ncbi.nlm.nih.gov/articles/PMC3159989/, PDB id: 1HGUNoneEC50 = 15.8 ± 2.0 ng/ml (Proliferation of BAFB2B2 cells)
6219
267138392016
SSSSKAPPPSLPSPSRLPGPSDTPILPQFPTIPLSRLFQNAMLRAHRLHQLAFDTYEEFEEAYIPKEQKYSFLQAPQASLCFSESIPTPSNREQAQQKSNLQLLRISLLLIQSWLEPVGFLRSVFANSLVYGASDSDVYDLLKDLEEGIQTLMGRLEDGSPRTGQAFKQTYAKFDANSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF-(SSSSKAPPPSLPSPSRLPGPSDTPILPQSSSSKAPPPSLPSPSRLPGPSDTPILPQ
MOD-4023275CTP fused to hGH2 CTP fusedLinearLNoneSyntheticTreatment of GHDDay 18115 mg/kg16.57 ± 6.32Monkeys serum proteaseSandwich ELISAMonkeys serumIn Vivohttps://pmc.ncbi.nlm.nih.gov/articles/PMC3159989/, PDB id: 1HGUNoneEC50 = 15.8 ± 2.0 ng/ml (Proliferation of BAFB2B2 cells)
6220
267138392016
SSSSKAPPPSLPSPSRLPGPSDTPILPQFPTIPLSRLFQNAMLRAHRLHQLAFDTYEEFEEAYIPKEQKYSFLQAPQASLCFSESIPTPSNREQAQQKSNLQLLRISLLLIQSWLEPVGFLRSVFANSLVYGASDSDVYDLLKDLEEGIQTLMGRLEDGSPRTGQAFKQTYAKFDANSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF-(SSSSKAPPPSLPSPSRLPGPSDTPILPQSSSSKAPPPSLPSPSRLPGPSDTPILPQ
MOD-4023275CTP fused to hGH2 CTP fusedLinearLNoneSyntheticTreatment of GHDDay 18115 mg/kg19.94 ± 8.77Monkeys serum proteaseSandwich ELISAMonkeys serumIn Vivohttps://pmc.ncbi.nlm.nih.gov/articles/PMC3159989/, PDB id: 1HGUNoneEC50 = 15.8 ± 2.0 ng/ml (Proliferation of BAFB2B2 cells)
6221
267138392016
SSSSKAPPPSLPSPSRLPGPSDTPILPQFPTIPLSRLFQNAMLRAHRLHQLAFDTYEEFEEAYIPKEQKYSFLQAPQASLCFSESIPTPSNREQAQQKSNLQLLRISLLLIQSWLEPVGFLRSVFANSLVYGASDSDVYDLLKDLEEGIQTLMGRLEDGSPRTGQAFKQTYAKFDANSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF-(SSSSKAPPPSLPSPSRLPGPSDTPILPQSSSSKAPPPSLPSPSRLPGPSDTPILPQ
MOD-4023275CTP fused to hGH2 CTP fusedLinearLNoneSyntheticTreatment of GHDDay 18130 mg/kg22.44 ± 12.53Monkeys serum proteaseSandwich ELISAMonkeys serumIn Vivohttps://pmc.ncbi.nlm.nih.gov/articles/PMC3159989/, PDB id: 1HGUNoneEC50 = 15.8 ± 2.0 ng/ml (Proliferation of BAFB2B2 cells)
6222
267138392016
SSSSKAPPPSLPSPSRLPGPSDTPILPQFPTIPLSRLFQNAMLRAHRLHQLAFDTYEEFEEAYIPKEQKYSFLQAPQASLCFSESIPTPSNREQAQQKSNLQLLRISLLLIQSWLEPVGFLRSVFANSLVYGASDSDVYDLLKDLEEGIQTLMGRLEDGSPRTGQAFKQTYAKFDANSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF-(SSSSKAPPPSLPSPSRLPGPSDTPILPQSSSSKAPPPSLPSPSRLPGPSDTPILPQ
MOD-4023275CTP fused to hGH2 CTP fusedLinearLNoneSyntheticTreatment of GHDDay 18130 mg/kg22.54 ± 19.55Monkeys serum proteaseSandwich ELISAMonkeys serumIn Vivohttps://pmc.ncbi.nlm.nih.gov/articles/PMC3159989/, PDB id: 1HGUNoneEC50 = 15.8 ± 2.0 ng/ml (Proliferation of BAFB2B2 cells)
6229
265077212016
HGEGTFTSDVSSYLEEQAAKEFIAWLVKGGGGGGGSGGGGSGGGGSAESKYGPPCPPCPAPEAAGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSQEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKGLPSSIEKTISKAKGQPREPQVYTLPPSQEEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSRLTVDKSRWQEGNVFSCSVMHEALHNHYTQKSLSLSLG
Dulaglutide275FreeIgG4 Fc fused at C terminal using GS linker LinearLNoneGLP-1 analogsAntidiabetes4 to 6 weeks0.75 mg5.5 (GM)Human plasma proteaseRIAHuman plasma after multiple doses of dulaglutide once weekly, ranging from 4 to 6 weeksIn VivoDB id: DB09045NoneN.A.
6230
265077212016
HGEGTFTSDVSSYLEEQAAKEFIAWLVKGGGGGGGSGGGGSGGGGSAESKYGPPCPPCPAPEAAGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSQEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKGLPSSIEKTISKAKGQPREPQVYTLPPSQEEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSRLTVDKSRWQEGNVFSCSVMHEALHNHYTQKSLSLSLG
Dulaglutide275FreeIgG4 Fc fused at C terminal using GS linker LinearLNoneGLP-1 analogsAntidiabetes4 to 6 weeks1.5 mg4.7 (GM)Human plasma proteaseRIAHuman plasma after multiple doses of dulaglutide once weekly, ranging from 4 to 6 weeksIn VivoDB id: DB09045NoneN.A.
6245
273936542016
CDLPQTHSLGSRRTLMLLAQMRKISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE
IFN-α165FreeFreeLinearLNoneHuman derivedAntiproliferative, immunoregulatory and antiviralAt desired time points (1, 5, 15, 30 min, 1, 3, 6, 24,48, 72 and 96 h)1 mg IFN-α equivalent/kg0.33 (T1/2a- Distribution Half Life)Mice plasma proteaseELISAMice plasmaIn VivoPDB id: 1ITFNoneIC50 = 10.77 pg/mL
6246
273936542016
CDLPQTHSLGSRRTLMLLAQMRKISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE-(PMPC)
IFN-PMPC165FreePoly(2-Methacryloyloxyethyl Phosphorylcholine)LinearLNoneHuman derivedAntiproliferative, immunoregulatory and antiviralAt desired time points (1, 5, 15, 30 min, 1, 3, 6, 24,48, 72 and 96 h)1 mg IFN-α equivalent/kg2 (T1/2a- Distribution Half Life)Mice plasma proteaseELISAMice plasmaIn VivoPDB id: 1ITFNoneIC50 = 20.02 pg/mL
6251
265529362016
AGLPTREPVRQASTAEPGAERIIVKYRAGTAAAGDRSAKLSTVQSALTRASLSGGTARASTLGPQVVRKLGVGADLIRLQGRLAPAELQRVLKELKADPAVQYAEADVKLRRTELRAGDVQPALAPNDPYYQQYQWHLHNATGGINAPSAWDVSQGEGVVVAVLDTGILPQHPDLVGNLLEGYDFISDAETSRRATNDRVPGAQDYGDWVENDNECYTGSVAEDSSWHGTHVAGTVAEQTNNGVGMAGVAHKAKVLPVRVLGKCGGYLSDIADAITWASGGTVAGVPANANPAEIINMSLGGSGSCDGTYQDAINGAISRGTTVVVAAGNETDNASKYRPASCDGVVTVGATRITGGITYYSNYGTRVDLSGPGGGGSVDGNPGGYVWQSGSDAATTPESGSYSYMGMGGTSMASPHVAAVAALVQSALIAKGKDPLAPAAMRTLLKETARPFPVSIPAATPIGTGIVDAKAALAKALEEPCTESCGPVATPLTNKAAVGGLNGTAGSSRLYSFEAAAGKQLSVITYGGTGNVSVYIAQGREPSASDNDGKSTRPGTSETVRVNKPVAGTYYIKVVGEAAYNGVSILATQH
DDD591FreeFreeLinearLHis-tagWild-type KerSMDKeratinase 60°CN.A.41 ± 15 (Activity Half Life)N.A.Enzyme activity assayDDDIn VitroNoneNoneActivity with Casein (U mg−1) = 3779 ± 20
6252
265529362016
AGLPTREPVRQASTAEPGAERIIVKYRAGTAAAGDRSAKLSTVQSALTRASLSGGTARASTLGPQVVRKLGVGADLIRLQGRLAPAELQRVLKELKADPAVQYAEADVKLRRTELRAGDVQPALAPNDPYYQQYQWHLHNATGGINAPSAWDVSQGEGVVVAVLDTGILPQHPDLVGNLLEGYDFISDAETSRRATNDRVPGAQDYGDWVENDNECYTGSVAEDSSWHGTHVAGTVAEQTNNGVGMAGVAHKAKVLPVRVLGKCGGYLSDIADAITWASGGTVAGVPANANPAEIINMSLGGSGSCDGTYQDAINGAISRGTTVVVAAGNETDNASKYRPASCDGVVTVGATRITGGITYYSNYGTRVDLSGPGGGGSVDGNPGGYVWQSGSDAATTPESGSYSYMGMGGTSMASPHVAAVAALVQSALIAKGKDPLAPAAMRTLLKETARPFPVSIPAATPIGTGIVDAKAALAKALEEPCTESPGGNVLQNNVPVTGLGAATGAELNYTVAVPAGSSQLRVTISGGSGDADLYVRQGSAPTDTSYTCRPYLSGNSETCTINSPAAGTWYVRVKAYSTFSGVTLNAQYH
DDF590FreeT1 From KERsmfLinearLHis-tagKerSMD mutantsKeratinase 60°CN.A.105.3 ± 5 (Activity Half Life)N.A.Enzyme activity assayDDFIn VitroNoneNoneActivity with Casein (U mg−1) = 4467 ± 14
6253
265529362016
GDVQLSGLQSAPTHQRFIVKYRDGSAPVANTTALASSLKSAAAGLASSQGRALGLQEVRKLAVGPTLVRTDRPLDQAESELLMRKLAADPNVEYVEVDQIMRATLAPNDPYYQQYQWHLHNATGGINAPSAWDVSQGEGVVVAVLDTGILPQHPDLVGNLLEGYDFISDAETSRRATNDRVPGAQDYGDWVENDNECYTGSVAEDSSWHGTHVAGTVAEQTNNGVGMAGVAHKAKVLPVRVLGKCGGYLSDIADAITWASGGTVAGVPANANPAEIINMSLGGSGSCDGTYQDAINGAISRGTTVVVAAGNETDNASKYRPASCDGVVTVGATRITGGITYYSNYGTRVDLSGPGGGGSVDGNPGGYVWQSGSDAATTPESGSYSYMGMGGTSMASPHVAAVAALVQSALIAKGKDPLAPAAMRTLLKETARPFPVSIPAATPIGTGIVDAKAALAKALEEPCTESCGPVATPLTNKAAVGGLNGTAGSSRLYSFEAAAGKQLSVITYGGTGNVSVYIAQGREPSASDNDGKSTRPGTSETVRVNKPVAGTYYIKVVGEAAYNGVSILATQH
FDD572P1 Substituitions From KersmfFreeLinearLHis-tagKerSMD mutantsKeratinase 60°CN.A.152.2 ± 2 (Activity Half Life)N.A.Enzyme activity assayFDDIn VitroNoneNoneActivity with Casein (U mg−1) =7844 ± 25
6254
265529362016
GDVQLSGLQSAPTHQRFIVKYRDGSAPVANTTALASSLKSAAAGLASSQGRALGLQEVRKLAVGPTLVRTDRPLDQAESELLMRKLAADPNVEYVEVDQIMRATLAPNDPYYQQYQWHLHNATGGINAPSAWDVSQGEGVVVAVLDTGILPQHPDLVGNLLEGYDFISDAETSRRATNDRVPGAQDYGDWVENDNECYTGSVAEDSSWHGTHVAGTVAEQTNNGVGMAGVAHKAKVLPVRVLGKCGGYLSDIADAITWASGGTVAGVPANANPAEIINMSLGGSGSCDGTYQDAINGAISRGTTVVVAAGNETDNASKYRPASCDGVVTVGATRITGGITYYSNYGTRVDLSGPGGGGSVDGNPGGYVWQSGSDAATTPESGSYSYMGMGGTSMASPHVAAVAALVQSALIAKGKDPLAPAAMRTLLKETARPFPVSIPAATPIGTGIVDAKAALAKALEEPCTESPGGNVLQNNVPVTGLGAATGAELNYTVAVPAGSSQLRVTISGGSGDADLYVRQGSAPTDTSYTCRPYLSGNSETCTINSPAAGTWYVRVKAYSTFSGVTLNAQYH
FDF571P1 Substituitions From KersmfT1 Substituitions From KersmfLinearLHis-tagKerSMD mutantsKeratinase 60°CN.A.244.6 ± 2 (Activity Half Life)N.A.Enzyme activity assayFDFIn VitroNoneNoneActivity with Casein (U mg−1) =8229 ± 50
6255
265529362016
AGLPTREPVRQASTAEPGAERIIVKYRAGTAAAGDRSAKLSTVQSALTRASLSGGTARASTLGPQVVRKLGVGADLIRLQGRLAPAELQRVLKELKADPAVQYAEADVKLRRTELRAGDVQPALAPNDPYYQQYQWHLHNATGGINAPSAWDVSQGEGVVVAVLDTGILPQHPDLVGNLLEGYDFISDAETSRRATNDRVPGAQDYGDWVENDNECYTGSVAEDSSWHGTHVAGTVAEQTNNGVGMAGVAHKAKVLPVRVLGKCGGYLSDIADAITWASGGTVAGVPANANPAEIINMSLGGSGSCDGTYQDAINGAISRGTTVVVAAGNETDNASKYRPASCDGVVTVGATRITGGITYYSNYGTRVDLSGPGGGGSVDGNPGGYVWQSGSDAATTPESGSYSYMGMGGTSMASPHVAAVAALVQSALIAKGKDPLAPAAMRTLLKETARPFPVSIPAATPIGTGIVDAKAALAKALEEPCTESH
DD486FreeT2 RemovedLinearLHis-tagKerSMD mutantsKeratinase 60°CN.A.5.6 ± 2 (Activity Half Life)N.A.Enzyme activity assayDDIn VitroNoneNoneActivity with Casein (U mg−1) = 4328 ± 18
6256
265529362016
GDVQLSGLQSAPTHQRFIVKYRDGSAPVANTTALASSLKSAAAGLASSQGRALGLQEVRKLAVGPTLVRTDRPLDQAESELLMRKLAADPNVEYVEVDQIMRATLAPNDPYYQQYQWHLHNATGGINAPSAWDVSQGEGVVVAVLDTGILPQHPDLVGNLLEGYDFISDAETSRRATNDRVPGAQDYGDWVENDNECYTGSVAEDSSWHGTHVAGTVAEQTNNGVGMAGVAHKAKVLPVRVLGKCGGYLSDIADAITWASGGTVAGVPANANPAEIINMSLGGSGSCDGTYQDAINGAISRGTTVVVAAGNETDNASKYRPASCDGVVTVGATRITGGITYYSNYGTRVDLSGPGGGGSVDGNPGGYVWQSGSDAATTPESGSYSYMGMGGTSMASPHVAAVAALVQSALIAKGKDPLAPAAMRTLLKETARPFPVSIPAATPIGTGIVDAKAALAKALEEPCTESH
FD467P1 From KERsmfT2 RemovedLinearLHis-tagKerSMD mutantsKeratinase 60°CN.A.36.5 ± 6 (Activity Half Life)N.A.Enzyme activity assayFDIn VitroNoneNoneActivity with Casein (U mg−1) = 9876 ± 50
6258
133-353-120-049-1212016
APPRLICDSRVLERYLLEAKEAENITTGCAEHCSLNENITVPDTKVNFYAWKRMEVGQQAVEVWQGLALLSEAVLRGQALLVNSSQPWEPLQLHVDKAVSGLRSLTTLLRALRAQKEAISPPDAASAAPLRTITADTFRKLFRVYSNFLRGKLKLYTGEACRTGDRVEPKSGDKTSTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGPFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK
rHuEPO-Fc399FreeFreeLinearLFusion with IgG Fc fragmentHuman erythropoietic protein Fusion with IgG Fc fragmentImmunogenicN.A.5 ug/kg 35.24+/-5.15Not mentionedELISABloodin vivohttps://lens.org/133-353-120-049-121US 9,375,487 B2N.A.
6268
043-207-181-799-34X2016
MVSQALRLLCLLLGLQGCLAAVFVTQEEAHGVLHRRRRANAFLEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYSDGDQCASSPCQNGGSCKDQLQSYICFCLPAFEGRNCETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSLLADGVSCTPTVEYPCGKIPILEKRNASKPQGRIVGGKVCPKGECPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIPSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPERTFSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCLQQSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQKLMRSEPRPGVLLRAPFPSSSSKAPPPSLPSPSRLPGPSDTPILPQSSSSKAPPPSLPSTSRLPGPSDTPILPQSSSSKAPPPSLPSPSRLPGP
Coagulation Factor VII444Free3CTPsLinearLCTPhepatocytes60 sec100 μl4.07serine proteaseELISABlood Streamin vivohttps://www.lens.org/lens/patent/043-207-181-799-34XUS 9458444 B2N.A.
6273
130-503-305-403-5202016
APISSHCRLDKSNFQQPYITNRTFMLAKEASLADNNTDVRLIGEKLFHGV SMSERCYLMKQVLNFTLEEVLFPQSDRFQPYMQEVVPFLARLSNRLSTCH IEGDDLHIQRNVQKLKDTVKKLGESGEIKAIGELDLLFMSLRNACIGSGG GSGGGGSGGGGSAPISSHCRLDKSNFQQPYITNRTFMLAKEASLADNNTD VRLIGEKLFHGVSMSERCYLMKQVLNFTLEEVLFPQSDRFQPYMQEVVPF LARLSNRLSTCHIEGDDLHIQRNVQKLKDTVKKLGESGEIKAIGELDLLF MSLRNACI
IL-22 dimer308FreeFreeLinearLNoneHumanNA20-30 min100 μg/kg1.3NAMTTPC12 cellsin vitrohttps://lens.org/130-503-305-403-520US 9352024 B2NA
6274
033-015-326-560-8092016
QDSTSDLIPAPPLSKVPLQQNFQDNQFHGKWYVVGLAGNAILREDKDPQK MYATIYELKEDKSYNVTSVLFRKKKCDYWIRTFVPGSQPGEFTLGNIKSY PGLTSYLVRVVSTNYNQHAMVFFKKVSQNREYFKITLYGRTKELTSELKE NFIRFSKSLGLPENHIVFPVPIDQCIDG
Lipocalin 2 mutein178FreeFreeLinearLNoneHumanantagonist30 minNANAserine proteaseELISANAin vivohttps://lens.org/033-015-326-560-809US 9260492 B2NA
6285
138-792-131-275-4112017
MSDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSH EDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKE YKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSREEMTKNQVSLTCL VKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQ QGNVFSCSVMHEALHNHYTQKSLSLSPGKAERAALEELVKLQGERVRGLK QQKASAELIEEEVAKLLKLKAQLGPDESKQKFVLKTPK
Fc-HRS (2-60)293FcFreeLinearLNoneSyntheticTherapeutic1.5 hr8 mg/kg72NAELISAmicein vivohttps://lens.org/138-792-131-275-411US 9587235 B2NA
6286
138-792-131-275-4112017
MAERAALEELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQLGPDES KQKFVLKTPKSDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEV TCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVL HQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSREEMT KNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSK LTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK
HRS (1-60)-Fc293FreeFcLinearLNoneSyntheticTherapeutic1.5 hr8 mg/kg33NAELISAmicein vivohttps://lens.org/138-792-131-275-411US 9587235 B2NA
6288
138-792-131-275-4112017
MSDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSH EDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKE YKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSREEMTKNQVSLTCL VKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQ QGNVFSCSVMHEALHNHYTQKSLSLSPGKAERAALEELVKLQGERVRGLK QQKASAELIEEEVAKLLKLKAQLGPDESKQKFVLKTPK
Fc-HRS (2-60)293FcFreeLinearLNoneSyntheticTherapeutic1.5 hr8 mg/kg71NAELISAmicein vivohttps://lens.org/138-792-131-275-411US 9587235 B2NA
6289
138-792-131-275-4112017
MAERAALEELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQLGPDES KQKFVLKTPKSDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEV TCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVL HQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSREEMT KNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSK LTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK
HRS (1-60)-Fc293FreeFcLinearLNoneSyntheticTherapeutic1.5 hr8 mg/kg37NAELISAmicein vivohttps://lens.org/138-792-131-275-411US 9587235 B2NA
6291
013-179-165-807-0352017
MHRPRRRGTRPPPLALLAALLLAARGADARSTGSPGSGDKTHTCPPCPAP ELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGV EVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPI EKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWE SNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEAL HNHYTQKSLSLSPGKGGGGSGGGGSGGGGSQRPRLSHKGPMPF
hFc-Apelin13298hFCfreeLinearLNonehuman adrenomedullin peptidena2 HRS10 μg/mL01-OctNAELISAC57/Bl6 micein vivohttps://lens.org/038-310-729-099-192US 9789197 B2NA
6292
013-179-165-807-0352017
MHRPRRRGTRPPPLALLAALLLAARGADAQRPRLSHKGPMPFGGGGSGGG GSGGGGSDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVV VDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDW LNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQV SLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVD KSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK
Apelin13-hFc289freehFCLinearLNonehuman adrenomedullin peptidena2 HRS3 μg/mL01-OctNAELISAC57/Bl6 micein vivohttps://lens.org/038-310-729-099-192US 9789197 B2NA