CA3051293A1 - Peptide modulators of the interaction between human c-peptide and human elastin receptor for therapeutic use - Google Patents
Peptide modulators of the interaction between human c-peptide and human elastin receptor for therapeutic use Download PDFInfo
- Publication number
- CA3051293A1 CA3051293A1 CA3051293A CA3051293A CA3051293A1 CA 3051293 A1 CA3051293 A1 CA 3051293A1 CA 3051293 A CA3051293 A CA 3051293A CA 3051293 A CA3051293 A CA 3051293A CA 3051293 A1 CA3051293 A1 CA 3051293A1
- Authority
- CA
- Canada
- Prior art keywords
- peptide
- seq
- human
- elastin
- peptides
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Pending
Links
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 512
- VOUAQYXWVJDEQY-QENPJCQMSA-N 33017-11-7 Chemical compound OC(=O)CC[C@H](N)C(=O)N[C@@H](C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](C(C)C)C(=O)NCC(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)NCC(=O)NCC(=O)N1CCC[C@H]1C(=O)NCC(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N1[C@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(O)=O)CCC1 VOUAQYXWVJDEQY-QENPJCQMSA-N 0.000 title claims abstract description 343
- 101000851054 Homo sapiens Elastin Proteins 0.000 title claims description 47
- 102000054289 human ELN Human genes 0.000 title claims description 47
- 230000003993 interaction Effects 0.000 title abstract description 44
- 230000001225 therapeutic effect Effects 0.000 title description 3
- 150000001413 amino acids Chemical class 0.000 claims abstract description 145
- 206010061218 Inflammation Diseases 0.000 claims abstract description 79
- 230000004054 inflammatory process Effects 0.000 claims abstract description 79
- 241000282414 Homo sapiens Species 0.000 claims description 210
- 230000027455 binding Effects 0.000 claims description 124
- 208000001072 type 2 diabetes mellitus Diseases 0.000 claims description 92
- 102000005962 receptors Human genes 0.000 claims description 75
- 108020003175 receptors Proteins 0.000 claims description 75
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 claims description 58
- 206010067584 Type 1 diabetes mellitus Diseases 0.000 claims description 54
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 claims description 51
- 206010022489 Insulin Resistance Diseases 0.000 claims description 48
- 201000010099 disease Diseases 0.000 claims description 42
- 206010020772 Hypertension Diseases 0.000 claims description 29
- 239000004471 Glycine Substances 0.000 claims description 25
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 claims description 19
- 230000001766 physiological effect Effects 0.000 claims description 16
- 208000032928 Dyslipidaemia Diseases 0.000 claims description 13
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 claims description 11
- 101000976075 Homo sapiens Insulin Proteins 0.000 claims description 9
- 208000017170 Lipid metabolism disease Diseases 0.000 claims description 8
- PBGKTOXHQIOBKM-FHFVDXKLSA-N insulin (human) Chemical compound C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@H]1CSSC[C@H]2C(=O)N[C@H](C(=O)N[C@@H](CO)C(=O)N[C@H](C(=O)N[C@H](C(N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=3C=CC(O)=CC=3)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC=3C=CC(O)=CC=3)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=3C=CC(O)=CC=3)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=3NC=NC=3)NC(=O)[C@H](CO)NC(=O)CNC1=O)C(=O)NCC(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)NCC(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H]([C@@H](C)O)C(O)=O)C(=O)N[C@@H](CC(N)=O)C(O)=O)=O)CSSC[C@@H](C(N2)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C(C)C)NC(=O)[C@@H](NC(=O)CN)[C@@H](C)CC)[C@@H](C)CC)[C@@H](C)O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](NC(=O)[C@@H](N)CC=1C=CC=CC=1)C(C)C)C1=CN=CN1 PBGKTOXHQIOBKM-FHFVDXKLSA-N 0.000 claims description 8
- 230000000977 initiatory effect Effects 0.000 claims description 6
- 108010075254 C-Peptide Proteins 0.000 abstract description 253
- 108010064033 elastin-binding proteins Proteins 0.000 abstract description 201
- 102000004196 processed proteins & peptides Human genes 0.000 abstract description 170
- NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical compound N1C(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(NC(=O)CN)C(C)CC)CSSCC(C(NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CCC(N)=O)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CSSCC(NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2C=CC(O)=CC=2)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2NC=NC=2)NC(=O)C(CO)NC(=O)CNC2=O)C(=O)NCC(=O)NC(CCC(O)=O)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC(O)=CC=3)C(=O)NC(C(C)O)C(=O)N3C(CCC3)C(=O)NC(CCCCN)C(=O)NC(C)C(O)=O)C(=O)NC(CC(N)=O)C(O)=O)=O)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(C(C)O)NC(=O)C1CSSCC2NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(N)CC=1C=CC=CC=1)C(C)C)CC1=CN=CN1 NOESYZHRGYRDHS-UHFFFAOYSA-N 0.000 abstract description 169
- 239000012634 fragment Substances 0.000 abstract description 126
- 108090001061 Insulin Proteins 0.000 abstract description 86
- 102000004877 Insulin Human genes 0.000 abstract description 85
- 229940125396 insulin Drugs 0.000 abstract description 84
- 108010014258 Elastin Proteins 0.000 abstract description 77
- 229920002549 elastin Polymers 0.000 abstract description 75
- 102000016942 Elastin Human genes 0.000 abstract description 74
- 208000001145 Metabolic Syndrome Diseases 0.000 abstract description 51
- 201000000690 abdominal obesity-metabolic syndrome Diseases 0.000 abstract description 51
- 108090000623 proteins and genes Proteins 0.000 abstract description 36
- 102000004169 proteins and genes Human genes 0.000 abstract description 35
- 230000004913 activation Effects 0.000 abstract description 20
- 230000002792 vascular Effects 0.000 abstract description 18
- 210000004204 blood vessel Anatomy 0.000 abstract description 17
- 239000008103 glucose Substances 0.000 abstract description 14
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 abstract description 13
- 230000015556 catabolic process Effects 0.000 abstract description 12
- 238000011161 development Methods 0.000 abstract description 12
- 210000004369 blood Anatomy 0.000 abstract description 11
- 239000008280 blood Substances 0.000 abstract description 11
- 230000008439 repair process Effects 0.000 abstract description 11
- 230000003190 augmentative effect Effects 0.000 abstract description 3
- 235000012054 meals Nutrition 0.000 abstract description 3
- 229940024606 amino acid Drugs 0.000 description 132
- 235000001014 amino acid Nutrition 0.000 description 129
- 102100026189 Beta-galactosidase Human genes 0.000 description 89
- 238000000034 method Methods 0.000 description 50
- 206010012601 diabetes mellitus Diseases 0.000 description 47
- 239000005557 antagonist Substances 0.000 description 44
- 239000003814 drug Substances 0.000 description 41
- 210000004027 cell Anatomy 0.000 description 38
- BJLPWUCPFAJINB-UAQSTNRTSA-N sn-3-O-(geranylgeranyl)glycerol 1-phosphate Chemical compound CC(C)=CCC\C(C)=C\CC\C(C)=C\CC\C(C)=C\COC[C@H](O)COP(O)(O)=O BJLPWUCPFAJINB-UAQSTNRTSA-N 0.000 description 36
- 201000001320 Atherosclerosis Diseases 0.000 description 33
- 235000018102 proteins Nutrition 0.000 description 32
- 230000017423 tissue regeneration Effects 0.000 description 32
- 108010033276 Peptide Fragments Proteins 0.000 description 31
- 102000007079 Peptide Fragments Human genes 0.000 description 31
- 230000001105 regulatory effect Effects 0.000 description 30
- 239000003446 ligand Substances 0.000 description 29
- 125000003275 alpha amino acid group Chemical group 0.000 description 24
- 239000000556 agonist Substances 0.000 description 23
- 230000001404 mediated effect Effects 0.000 description 23
- 208000002249 Diabetes Complications Diseases 0.000 description 22
- 210000000227 basophil cell of anterior lobe of hypophysis Anatomy 0.000 description 21
- RLCSROTYKMPBDL-USJZOSNVSA-N 2-[[(2s)-1-[(2s)-2-[[(2s)-2-[[2-[[(2s)-2-amino-3-methylbutanoyl]amino]acetyl]amino]-3-methylbutanoyl]amino]propanoyl]pyrrolidine-2-carbonyl]amino]acetic acid Chemical compound CC(C)[C@H](N)C(=O)NCC(=O)N[C@@H](C(C)C)C(=O)N[C@@H](C)C(=O)N1CCC[C@H]1C(=O)NCC(O)=O RLCSROTYKMPBDL-USJZOSNVSA-N 0.000 description 20
- 230000000694 effects Effects 0.000 description 20
- 108010011876 valyl-glycyl-valyl-alanyl-prolyl-glycine Proteins 0.000 description 20
- 208000019553 vascular disease Diseases 0.000 description 19
- 210000002744 extracellular matrix Anatomy 0.000 description 17
- 230000001965 increasing effect Effects 0.000 description 17
- 102000010834 Extracellular Matrix Proteins Human genes 0.000 description 16
- 108010037362 Extracellular Matrix Proteins Proteins 0.000 description 16
- 230000004071 biological effect Effects 0.000 description 16
- 208000035475 disorder Diseases 0.000 description 16
- 210000002950 fibroblast Anatomy 0.000 description 16
- 230000002757 inflammatory effect Effects 0.000 description 16
- 230000003405 preventing effect Effects 0.000 description 16
- 230000002265 prevention Effects 0.000 description 15
- 206010012655 Diabetic complications Diseases 0.000 description 14
- 102000003777 Interleukin-1 beta Human genes 0.000 description 14
- 108090000193 Interleukin-1 beta Proteins 0.000 description 14
- 230000004968 inflammatory condition Effects 0.000 description 14
- 230000000391 smoking effect Effects 0.000 description 14
- 210000000329 smooth muscle myocyte Anatomy 0.000 description 14
- 102000000802 Galectin 3 Human genes 0.000 description 13
- 239000000203 mixture Substances 0.000 description 13
- 108010001517 Galectin 3 Proteins 0.000 description 12
- 230000006378 damage Effects 0.000 description 12
- 230000002209 hydrophobic effect Effects 0.000 description 12
- 210000002865 immune cell Anatomy 0.000 description 12
- 238000003032 molecular docking Methods 0.000 description 12
- 108010008064 pro-brain natriuretic peptide (1-76) Proteins 0.000 description 12
- 230000035755 proliferation Effects 0.000 description 12
- 241000282412 Homo Species 0.000 description 11
- 102000051628 Interleukin-1 receptor antagonist Human genes 0.000 description 11
- 241000700159 Rattus Species 0.000 description 11
- 230000018109 developmental process Effects 0.000 description 11
- 235000005911 diet Nutrition 0.000 description 11
- 230000002401 inhibitory effect Effects 0.000 description 11
- 239000000047 product Substances 0.000 description 11
- LOGFVTREOLYCPF-KXNHARMFSA-N (2s,3r)-2-[[(2r)-1-[(2s)-2,6-diaminohexanoyl]pyrrolidine-2-carbonyl]amino]-3-hydroxybutanoic acid Chemical compound C[C@@H](O)[C@@H](C(O)=O)NC(=O)[C@H]1CCCN1C(=O)[C@@H](N)CCCCN LOGFVTREOLYCPF-KXNHARMFSA-N 0.000 description 10
- 206010003210 Arteriosclerosis Diseases 0.000 description 10
- 208000024172 Cardiovascular disease Diseases 0.000 description 10
- 101001076407 Homo sapiens Interleukin-1 receptor antagonist protein Proteins 0.000 description 10
- 229940119178 Interleukin 1 receptor antagonist Drugs 0.000 description 10
- 239000013543 active substance Substances 0.000 description 10
- 239000003407 interleukin 1 receptor blocking agent Substances 0.000 description 10
- 208000017169 kidney disease Diseases 0.000 description 10
- 201000001119 neuropathy Diseases 0.000 description 10
- 230000007823 neuropathy Effects 0.000 description 10
- CWCXERYKLSEGEZ-KDKHKZEGSA-N procalcitonin Chemical group C([C@@H](C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@H](C(=O)N[C@@H](C)C(=O)N[C@@H]([C@@H](C)CC)C(=O)NCC(=O)N[C@@H](C(C)C)C(=O)NCC(=O)N[C@@H](C)C(=O)N1[C@@H](CCC1)C(=O)NCC(O)=O)[C@@H](C)O)NC(=O)[C@@H](NC(=O)[C@H](CC=1NC=NC=1)NC(=O)[C@H](CC=1C=CC=CC=1)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC=1C=CC=CC=1)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@@H](NC(=O)CNC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCSC)NC(=O)[C@H]1NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CO)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(N)=O)NC(=O)CNC(=O)[C@@H](N)CSSC1)[C@@H](C)O)[C@@H](C)O)[C@@H](C)O)C1=CC=CC=C1 CWCXERYKLSEGEZ-KDKHKZEGSA-N 0.000 description 10
- 238000012360 testing method Methods 0.000 description 10
- 230000006492 vascular dysfunction Effects 0.000 description 10
- 206010051379 Systemic Inflammatory Response Syndrome Diseases 0.000 description 9
- 208000011775 arteriosclerosis disease Diseases 0.000 description 9
- 108010005774 beta-Galactosidase Proteins 0.000 description 9
- 210000004899 c-terminal region Anatomy 0.000 description 9
- 230000035605 chemotaxis Effects 0.000 description 9
- 210000002966 serum Anatomy 0.000 description 9
- 102100038910 Alpha-enolase Human genes 0.000 description 8
- 241000699670 Mus sp. Species 0.000 description 8
- 108010022181 Phosphopyruvate Hydratase Proteins 0.000 description 8
- 102000001708 Protein Isoforms Human genes 0.000 description 8
- 108010029485 Protein Isoforms Proteins 0.000 description 8
- 208000037976 chronic inflammation Diseases 0.000 description 8
- 229940079593 drug Drugs 0.000 description 8
- 230000003203 everyday effect Effects 0.000 description 8
- 230000017854 proteolysis Effects 0.000 description 8
- 210000001519 tissue Anatomy 0.000 description 8
- 108010030229 Fibrillin-1 Proteins 0.000 description 7
- 102100031509 Fibrillin-1 Human genes 0.000 description 7
- 102000000589 Interleukin-1 Human genes 0.000 description 7
- 108010002352 Interleukin-1 Proteins 0.000 description 7
- 208000005764 Peripheral Arterial Disease Diseases 0.000 description 7
- 208000030831 Peripheral arterial occlusive disease Diseases 0.000 description 7
- 230000003399 chemotactic effect Effects 0.000 description 7
- 210000000265 leukocyte Anatomy 0.000 description 7
- 238000004519 manufacturing process Methods 0.000 description 7
- 210000001616 monocyte Anatomy 0.000 description 7
- 239000000546 pharmaceutical excipient Substances 0.000 description 7
- 239000012071 phase Substances 0.000 description 7
- 102100022166 E3 ubiquitin-protein ligase NEURL1 Human genes 0.000 description 6
- 206010019280 Heart failures Diseases 0.000 description 6
- 101000909506 Homo sapiens Collagen alpha-3(VI) chain Proteins 0.000 description 6
- 101000973232 Homo sapiens E3 ubiquitin-protein ligase NEURL1 Proteins 0.000 description 6
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 6
- 102000007547 Laminin Human genes 0.000 description 6
- 108010085895 Laminin Proteins 0.000 description 6
- 102100028524 Lysosomal protective protein Human genes 0.000 description 6
- IQFYYKKMVGJFEH-XLPZGREQSA-N Thymidine Chemical compound O=C1NC(=O)C(C)=CN1[C@@H]1O[C@H](CO)[C@@H](O)C1 IQFYYKKMVGJFEH-XLPZGREQSA-N 0.000 description 6
- 230000032683 aging Effects 0.000 description 6
- 230000033115 angiogenesis Effects 0.000 description 6
- 239000003472 antidiabetic agent Substances 0.000 description 6
- 230000000903 blocking effect Effects 0.000 description 6
- 230000007812 deficiency Effects 0.000 description 6
- 238000006731 degradation reaction Methods 0.000 description 6
- 230000037213 diet Effects 0.000 description 6
- 230000006870 function Effects 0.000 description 6
- 102000057000 human COL6A3 Human genes 0.000 description 6
- 230000002519 immonomodulatory effect Effects 0.000 description 6
- 238000000338 in vitro Methods 0.000 description 6
- 210000004153 islets of langerhan Anatomy 0.000 description 6
- 208000030159 metabolic disease Diseases 0.000 description 6
- 210000000496 pancreas Anatomy 0.000 description 6
- 208000033808 peripheral neuropathy Diseases 0.000 description 6
- 239000008194 pharmaceutical composition Substances 0.000 description 6
- 230000002441 reversible effect Effects 0.000 description 6
- GRPMKDCBBAUSQM-GMHRPJKWSA-N 2-[[(2s)-1-[(2s,3s)-3-methyl-2-[[(2s)-2-[[2-[[(2s)-pyrrolidine-2-carbonyl]amino]acetyl]amino]propanoyl]amino]pentanoyl]pyrrolidine-2-carbonyl]amino]acetic acid Chemical compound N([C@@H](C)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N1[C@@H](CCC1)C(=O)NCC(O)=O)C(=O)CNC(=O)[C@@H]1CCCN1 GRPMKDCBBAUSQM-GMHRPJKWSA-N 0.000 description 5
- 208000006545 Chronic Obstructive Pulmonary Disease Diseases 0.000 description 5
- 102000008186 Collagen Human genes 0.000 description 5
- 108010035532 Collagen Proteins 0.000 description 5
- 101000725565 Homo sapiens Pro-opiomelanocortin Proteins 0.000 description 5
- 101000962053 Homo sapiens Pyrin Proteins 0.000 description 5
- 206010054805 Macroangiopathy Diseases 0.000 description 5
- 108010048233 Procalcitonin Proteins 0.000 description 5
- 210000000577 adipose tissue Anatomy 0.000 description 5
- 239000000090 biomarker Substances 0.000 description 5
- 230000001364 causal effect Effects 0.000 description 5
- 239000003795 chemical substances by application Substances 0.000 description 5
- 229920001436 collagen Polymers 0.000 description 5
- 230000000378 dietary effect Effects 0.000 description 5
- 230000002526 effect on cardiovascular system Effects 0.000 description 5
- 102000051001 human MEFV Human genes 0.000 description 5
- 230000006759 inflammatory activation Effects 0.000 description 5
- 230000003902 lesion Effects 0.000 description 5
- 230000022275 macrophage chemotaxis Effects 0.000 description 5
- 210000000056 organ Anatomy 0.000 description 5
- 210000003668 pericyte Anatomy 0.000 description 5
- 238000002360 preparation method Methods 0.000 description 5
- 230000000770 proinflammatory effect Effects 0.000 description 5
- 108010092728 prolyl-glycyl-alanyl-isoleucyl-prolyl-glycine Proteins 0.000 description 5
- 238000011160 research Methods 0.000 description 5
- 241000894007 species Species 0.000 description 5
- 230000002194 synthesizing effect Effects 0.000 description 5
- LFTRJWKKLPVMNE-RCBQFDQVSA-N 2-[[(2s)-2-[[2-[[(2s)-1-[(2s)-2-amino-3-methylbutanoyl]pyrrolidine-2-carbonyl]amino]acetyl]amino]-3-methylbutanoyl]amino]acetic acid Chemical compound CC(C)[C@H](N)C(=O)N1CCC[C@H]1C(=O)NCC(=O)N[C@@H](C(C)C)C(=O)NCC(O)=O LFTRJWKKLPVMNE-RCBQFDQVSA-N 0.000 description 4
- 102400000686 Endothelin-1 Human genes 0.000 description 4
- 101800004490 Endothelin-1 Proteins 0.000 description 4
- 102000001824 GPR146 Human genes 0.000 description 4
- 108050009062 GPR146 Proteins 0.000 description 4
- 208000019451 Gillespie syndrome Diseases 0.000 description 4
- 108060003393 Granulin Proteins 0.000 description 4
- 206010020710 Hyperphagia Diseases 0.000 description 4
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 4
- 102000002274 Matrix Metalloproteinases Human genes 0.000 description 4
- 108010000684 Matrix Metalloproteinases Proteins 0.000 description 4
- 102000005583 Pyrin Human genes 0.000 description 4
- 108010059278 Pyrin Proteins 0.000 description 4
- 102100021025 Regulator of G-protein signaling 19 Human genes 0.000 description 4
- 101710148108 Regulator of G-protein signaling 19 Proteins 0.000 description 4
- 208000017442 Retinal disease Diseases 0.000 description 4
- 206010038923 Retinopathy Diseases 0.000 description 4
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 4
- YWPHLSNIBNZPMN-GILQHPPASA-N [(2r,3r,4s,6s)-3-acetamido-6-(hydroxymethyl)-2-[(2s,3r,4s,5r,6r)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-4-[(2r,3s,4r,5s,6s)-3,4,5-trihydroxy-6-methyloxan-2-yl]oxyoxan-2-yl] dihydrogen phosphate Chemical compound O[C@H]1[C@H](O)[C@H](O)[C@H](C)O[C@H]1O[C@@H]1[C@@H](NC(C)=O)[C@@](O[C@H]2[C@@H]([C@@H](O)[C@@H](O)[C@@H](CO)O2)O)(OP(O)(O)=O)O[C@H](CO)C1 YWPHLSNIBNZPMN-GILQHPPASA-N 0.000 description 4
- 238000004458 analytical method Methods 0.000 description 4
- 230000001413 cellular effect Effects 0.000 description 4
- 230000006020 chronic inflammation Effects 0.000 description 4
- 208000037893 chronic inflammatory disorder Diseases 0.000 description 4
- 208000020832 chronic kidney disease Diseases 0.000 description 4
- 238000003776 cleavage reaction Methods 0.000 description 4
- 230000034994 death Effects 0.000 description 4
- 210000004177 elastic tissue Anatomy 0.000 description 4
- 235000013305 food Nutrition 0.000 description 4
- 230000037406 food intake Effects 0.000 description 4
- 235000012631 food intake Nutrition 0.000 description 4
- 108010038088 glutamyl-glycyl-seryl-leucyl-glutamine Proteins 0.000 description 4
- 238000000126 in silico method Methods 0.000 description 4
- 230000003914 insulin secretion Effects 0.000 description 4
- 239000003550 marker Substances 0.000 description 4
- 208000010125 myocardial infarction Diseases 0.000 description 4
- 235000020830 overeating Nutrition 0.000 description 4
- 230000007170 pathology Effects 0.000 description 4
- 230000002093 peripheral effect Effects 0.000 description 4
- 208000028241 peripheral precocious puberty Diseases 0.000 description 4
- 230000002062 proliferating effect Effects 0.000 description 4
- 230000002797 proteolythic effect Effects 0.000 description 4
- 108010054022 valyl-prolyl-glycyl-valyl-glycine Proteins 0.000 description 4
- 230000003966 vascular damage Effects 0.000 description 4
- 210000005166 vasculature Anatomy 0.000 description 4
- 208000009304 Acute Kidney Injury Diseases 0.000 description 3
- 210000002237 B-cell of pancreatic islet Anatomy 0.000 description 3
- DWRXFEITVBNRMK-UHFFFAOYSA-N Beta-D-1-Arabinofuranosylthymine Natural products O=C1NC(=O)C(C)=CN1C1C(O)C(O)C(CO)O1 DWRXFEITVBNRMK-UHFFFAOYSA-N 0.000 description 3
- 102000005572 Cathepsin A Human genes 0.000 description 3
- 108010059081 Cathepsin A Proteins 0.000 description 3
- 150000008574 D-amino acids Chemical class 0.000 description 3
- 102100033167 Elastin Human genes 0.000 description 3
- 206010063560 Excessive granulation tissue Diseases 0.000 description 3
- 108010030242 Fibrillin-2 Proteins 0.000 description 3
- 102100031510 Fibrillin-2 Human genes 0.000 description 3
- 206010060378 Hyperinsulinaemia Diseases 0.000 description 3
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 3
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 3
- 208000008589 Obesity Diseases 0.000 description 3
- 206010053159 Organ failure Diseases 0.000 description 3
- 108010076181 Proinsulin Proteins 0.000 description 3
- 208000033626 Renal failure acute Diseases 0.000 description 3
- 206010053879 Sepsis syndrome Diseases 0.000 description 3
- 102100028760 Sialidase-1 Human genes 0.000 description 3
- 241000282898 Sus scrofa Species 0.000 description 3
- 208000002223 abdominal aortic aneurysm Diseases 0.000 description 3
- 230000001154 acute effect Effects 0.000 description 3
- 201000011040 acute kidney failure Diseases 0.000 description 3
- 125000003295 alanine group Chemical group N[C@@H](C)C(=O)* 0.000 description 3
- 125000000539 amino acid group Chemical group 0.000 description 3
- 230000003178 anti-diabetic effect Effects 0.000 description 3
- 229940125708 antidiabetic agent Drugs 0.000 description 3
- 230000003143 atherosclerotic effect Effects 0.000 description 3
- IQFYYKKMVGJFEH-UHFFFAOYSA-N beta-L-thymidine Natural products O=C1NC(=O)C(C)=CN1C1OC(CO)C(O)C1 IQFYYKKMVGJFEH-UHFFFAOYSA-N 0.000 description 3
- 230000000975 bioactive effect Effects 0.000 description 3
- 239000002775 capsule Substances 0.000 description 3
- 238000006243 chemical reaction Methods 0.000 description 3
- 230000001684 chronic effect Effects 0.000 description 3
- 239000007857 degradation product Substances 0.000 description 3
- DVSDDICSXBCMQJ-UHFFFAOYSA-N diethyl 2-acetylbutanedioate Chemical compound CCOC(=O)CC(C(C)=O)C(=O)OCC DVSDDICSXBCMQJ-UHFFFAOYSA-N 0.000 description 3
- 239000003937 drug carrier Substances 0.000 description 3
- 210000002889 endothelial cell Anatomy 0.000 description 3
- 210000001126 granulation tissue Anatomy 0.000 description 3
- 210000002216 heart Anatomy 0.000 description 3
- 230000035879 hyperinsulinaemia Effects 0.000 description 3
- 208000027866 inflammatory disease Diseases 0.000 description 3
- 102000006495 integrins Human genes 0.000 description 3
- 108010044426 integrins Proteins 0.000 description 3
- 210000003734 kidney Anatomy 0.000 description 3
- 230000011268 leukocyte chemotaxis Effects 0.000 description 3
- 210000004185 liver Anatomy 0.000 description 3
- XZWYZXLIPXDOLR-UHFFFAOYSA-N metformin Chemical compound CN(C)C(=N)NC(N)=N XZWYZXLIPXDOLR-UHFFFAOYSA-N 0.000 description 3
- 229960003105 metformin Drugs 0.000 description 3
- 230000004048 modification Effects 0.000 description 3
- 238000012986 modification Methods 0.000 description 3
- 235000020824 obesity Nutrition 0.000 description 3
- 238000012261 overproduction Methods 0.000 description 3
- 210000002705 pancreatic stellate cell Anatomy 0.000 description 3
- 229920001184 polypeptide Polymers 0.000 description 3
- 230000008569 process Effects 0.000 description 3
- 230000001681 protective effect Effects 0.000 description 3
- 230000006916 protein interaction Effects 0.000 description 3
- 206010039073 rheumatoid arthritis Diseases 0.000 description 3
- 230000007017 scission Effects 0.000 description 3
- 230000000276 sedentary effect Effects 0.000 description 3
- 230000009885 systemic effect Effects 0.000 description 3
- 229940104230 thymidine Drugs 0.000 description 3
- 210000004881 tumor cell Anatomy 0.000 description 3
- 210000004509 vascular smooth muscle cell Anatomy 0.000 description 3
- HFOXKFUFXCZIKS-HOTWGDJZSA-N (2s,3r,4s,5r,6r)-2-[(2r,3r,4s,5r,6r)-4,5-dihydroxy-6-(hydroxymethyl)-2-propyl-2-[(2s,3r,4s,5r,6r)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxyoxan-3-yl]oxy-6-(hydroxymethyl)oxane-3,4,5-triol Chemical compound O([C@]1(CCC)[C@@H]([C@@H](O)[C@@H](O)[C@@H](CO)O1)O[C@H]1[C@@H]([C@@H](O)[C@@H](O)[C@@H](CO)O1)O)[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O HFOXKFUFXCZIKS-HOTWGDJZSA-N 0.000 description 2
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 description 2
- 241000283690 Bos taurus Species 0.000 description 2
- 206010012289 Dementia Diseases 0.000 description 2
- 101710175017 Fibrillin-3 Proteins 0.000 description 2
- 102100031387 Fibrillin-3 Human genes 0.000 description 2
- 108010067306 Fibronectins Proteins 0.000 description 2
- 102000016359 Fibronectins Human genes 0.000 description 2
- 108010093031 Galactosidases Proteins 0.000 description 2
- 102000002464 Galactosidases Human genes 0.000 description 2
- 102000007563 Galectins Human genes 0.000 description 2
- 108010046569 Galectins Proteins 0.000 description 2
- 241000282575 Gorilla Species 0.000 description 2
- 101000765010 Homo sapiens Beta-galactosidase Proteins 0.000 description 2
- 101001123859 Homo sapiens Sialidase-1 Proteins 0.000 description 2
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 2
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 2
- 241000699660 Mus musculus Species 0.000 description 2
- 206010052904 Musculoskeletal stiffness Diseases 0.000 description 2
- 102400001263 NT-proBNP Human genes 0.000 description 2
- 206010028980 Neoplasm Diseases 0.000 description 2
- 108010006232 Neuraminidase Proteins 0.000 description 2
- 102000005348 Neuraminidase Human genes 0.000 description 2
- 201000009859 Osteochondrosis Diseases 0.000 description 2
- 241000282405 Pongo abelii Species 0.000 description 2
- 241000288906 Primates Species 0.000 description 2
- 108010026552 Proteome Proteins 0.000 description 2
- 230000010799 Receptor Interactions Effects 0.000 description 2
- 229920002472 Starch Polymers 0.000 description 2
- 208000006011 Stroke Diseases 0.000 description 2
- 208000032109 Transient ischaemic attack Diseases 0.000 description 2
- 238000009825 accumulation Methods 0.000 description 2
- 230000021736 acetylation Effects 0.000 description 2
- 238000006640 acetylation reaction Methods 0.000 description 2
- 230000009471 action Effects 0.000 description 2
- 230000003213 activating effect Effects 0.000 description 2
- 206010000891 acute myocardial infarction Diseases 0.000 description 2
- 210000001789 adipocyte Anatomy 0.000 description 2
- 235000004279 alanine Nutrition 0.000 description 2
- 230000009435 amidation Effects 0.000 description 2
- 238000007112 amidation reaction Methods 0.000 description 2
- 230000003110 anti-inflammatory effect Effects 0.000 description 2
- 238000003556 assay Methods 0.000 description 2
- 230000001363 autoimmune Effects 0.000 description 2
- WQZGKKKJIJFFOK-FPRJBGLDSA-N beta-D-galactose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@H]1O WQZGKKKJIJFFOK-FPRJBGLDSA-N 0.000 description 2
- 230000015572 biosynthetic process Effects 0.000 description 2
- 201000011510 cancer Diseases 0.000 description 2
- 230000008859 change Effects 0.000 description 2
- 239000002131 composite material Substances 0.000 description 2
- 238000012790 confirmation Methods 0.000 description 2
- 210000001608 connective tissue cell Anatomy 0.000 description 2
- 230000007423 decrease Effects 0.000 description 2
- 230000003247 decreasing effect Effects 0.000 description 2
- 238000009509 drug development Methods 0.000 description 2
- 230000004064 dysfunction Effects 0.000 description 2
- 230000010595 endothelial cell migration Effects 0.000 description 2
- 230000007071 enzymatic hydrolysis Effects 0.000 description 2
- 238000006047 enzymatic hydrolysis reaction Methods 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- 239000000284 extract Substances 0.000 description 2
- 150000008195 galaktosides Chemical class 0.000 description 2
- WHUUTDBJXJRKMK-VKHMYHEASA-L glutamate group Chemical group N[C@@H](CCC(=O)[O-])C(=O)[O-] WHUUTDBJXJRKMK-VKHMYHEASA-L 0.000 description 2
- 230000036541 health Effects 0.000 description 2
- 210000005260 human cell Anatomy 0.000 description 2
- 208000026278 immune system disease Diseases 0.000 description 2
- 239000002955 immunomodulating agent Substances 0.000 description 2
- 229940121354 immunomodulator Drugs 0.000 description 2
- 230000001771 impaired effect Effects 0.000 description 2
- 238000001727 in vivo Methods 0.000 description 2
- 230000006698 induction Effects 0.000 description 2
- 230000003834 intracellular effect Effects 0.000 description 2
- 229960000310 isoleucine Drugs 0.000 description 2
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 2
- -1 laminins Proteins 0.000 description 2
- 230000000670 limiting effect Effects 0.000 description 2
- 230000007774 longterm Effects 0.000 description 2
- 210000004072 lung Anatomy 0.000 description 2
- 210000002540 macrophage Anatomy 0.000 description 2
- 239000011159 matrix material Substances 0.000 description 2
- 238000005259 measurement Methods 0.000 description 2
- 239000012528 membrane Substances 0.000 description 2
- 230000002503 metabolic effect Effects 0.000 description 2
- 238000013508 migration Methods 0.000 description 2
- 230000003278 mimic effect Effects 0.000 description 2
- 238000010172 mouse model Methods 0.000 description 2
- 230000001537 neural effect Effects 0.000 description 2
- 238000010606 normalization Methods 0.000 description 2
- 239000000816 peptidomimetic Substances 0.000 description 2
- 230000003389 potentiating effect Effects 0.000 description 2
- 230000035935 pregnancy Effects 0.000 description 2
- 108010066381 preproinsulin Proteins 0.000 description 2
- 229940076372 protein antagonist Drugs 0.000 description 2
- 229940044551 receptor antagonist Drugs 0.000 description 2
- 239000002464 receptor antagonist Substances 0.000 description 2
- 230000000979 retarding effect Effects 0.000 description 2
- 230000011664 signaling Effects 0.000 description 2
- 210000003491 skin Anatomy 0.000 description 2
- 238000010532 solid phase synthesis reaction Methods 0.000 description 2
- 235000019698 starch Nutrition 0.000 description 2
- 230000000707 stereoselective effect Effects 0.000 description 2
- 230000004936 stimulating effect Effects 0.000 description 2
- 208000011580 syndromic disease Diseases 0.000 description 2
- 238000002560 therapeutic procedure Methods 0.000 description 2
- 230000008719 thickening Effects 0.000 description 2
- 238000013334 tissue model Methods 0.000 description 2
- 201000010875 transient cerebral ischemia Diseases 0.000 description 2
- 239000004474 valine Substances 0.000 description 2
- 210000005167 vascular cell Anatomy 0.000 description 2
- 230000004218 vascular function Effects 0.000 description 2
- DXRXYJYFADHAPA-AUTRQRHGSA-N (2s)-2-[[2-[[(2s)-5-amino-2-[[(2s)-2-aminopropanoyl]amino]-5-oxopentanoyl]amino]acetyl]amino]-3-methylbutanoic acid Chemical compound CC(C)[C@@H](C(O)=O)NC(=O)CNC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](C)N DXRXYJYFADHAPA-AUTRQRHGSA-N 0.000 description 1
- IVWWFWFVSWOTLP-YVZVNANGSA-N (3'as,4r,7'as)-2,2,2',2'-tetramethylspiro[1,3-dioxolane-4,6'-4,7a-dihydro-3ah-[1,3]dioxolo[4,5-c]pyran]-7'-one Chemical compound C([C@@H]1OC(O[C@@H]1C1=O)(C)C)O[C@]21COC(C)(C)O2 IVWWFWFVSWOTLP-YVZVNANGSA-N 0.000 description 1
- MZOFCQQQCNRIBI-VMXHOPILSA-N (3s)-4-[[(2s)-1-[[(2s)-1-[[(1s)-1-carboxy-2-hydroxyethyl]amino]-4-methyl-1-oxopentan-2-yl]amino]-5-(diaminomethylideneamino)-1-oxopentan-2-yl]amino]-3-[[2-[[(2s)-2,6-diaminohexanoyl]amino]acetyl]amino]-4-oxobutanoic acid Chemical compound OC[C@@H](C(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCN=C(N)N)NC(=O)[C@H](CC(O)=O)NC(=O)CNC(=O)[C@@H](N)CCCCN MZOFCQQQCNRIBI-VMXHOPILSA-N 0.000 description 1
- HMLGSIZOMSVISS-ONJSNURVSA-N (7r)-7-[[(2z)-2-(2-amino-1,3-thiazol-4-yl)-2-(2,2-dimethylpropanoyloxymethoxyimino)acetyl]amino]-3-ethenyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid Chemical compound N([C@@H]1C(N2C(=C(C=C)CSC21)C(O)=O)=O)C(=O)\C(=N/OCOC(=O)C(C)(C)C)C1=CSC(N)=N1 HMLGSIZOMSVISS-ONJSNURVSA-N 0.000 description 1
- SWLAMJPTOQZTAE-UHFFFAOYSA-N 4-[2-[(5-chloro-2-methoxybenzoyl)amino]ethyl]benzoic acid Chemical compound COC1=CC=C(Cl)C=C1C(=O)NCCC1=CC=C(C(O)=O)C=C1 SWLAMJPTOQZTAE-UHFFFAOYSA-N 0.000 description 1
- 108091006112 ATPases Proteins 0.000 description 1
- 102000057290 Adenosine Triphosphatases Human genes 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- 101100180402 Caenorhabditis elegans jun-1 gene Proteins 0.000 description 1
- 206010007558 Cardiac failure chronic Diseases 0.000 description 1
- 102000014914 Carrier Proteins Human genes 0.000 description 1
- 241000700199 Cavia porcellus Species 0.000 description 1
- 102000000844 Cell Surface Receptors Human genes 0.000 description 1
- 108010001857 Cell Surface Receptors Proteins 0.000 description 1
- 241000700112 Chinchilla Species 0.000 description 1
- 241000867607 Chlorocebus sabaeus Species 0.000 description 1
- 102000011022 Chorionic Gonadotropin Human genes 0.000 description 1
- 108010062540 Chorionic Gonadotropin Proteins 0.000 description 1
- 102000004266 Collagen Type IV Human genes 0.000 description 1
- 108010042086 Collagen Type IV Proteins 0.000 description 1
- 108091035707 Consensus sequence Proteins 0.000 description 1
- 208000011231 Crohn disease Diseases 0.000 description 1
- 102000004127 Cytokines Human genes 0.000 description 1
- 108090000695 Cytokines Proteins 0.000 description 1
- 108020004414 DNA Proteins 0.000 description 1
- 238000002965 ELISA Methods 0.000 description 1
- 206010014561 Emphysema Diseases 0.000 description 1
- 206010048554 Endothelial dysfunction Diseases 0.000 description 1
- 241000283086 Equidae Species 0.000 description 1
- 108700024394 Exon Proteins 0.000 description 1
- 101710145505 Fiber protein Proteins 0.000 description 1
- 102000003688 G-Protein-Coupled Receptors Human genes 0.000 description 1
- 108090000045 G-Protein-Coupled Receptors Proteins 0.000 description 1
- 101710197901 Galectin-3-binding protein Proteins 0.000 description 1
- 208000002705 Glucose Intolerance Diseases 0.000 description 1
- 102000003886 Glycoproteins Human genes 0.000 description 1
- 108090000288 Glycoproteins Proteins 0.000 description 1
- 229920002683 Glycosaminoglycan Polymers 0.000 description 1
- 241000212819 Hegeter glaber Species 0.000 description 1
- 101000866618 Homo sapiens 3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase Proteins 0.000 description 1
- 101000608757 Homo sapiens Galectin-3 Proteins 0.000 description 1
- 101000990902 Homo sapiens Matrix metalloproteinase-9 Proteins 0.000 description 1
- 102000003839 Human Proteins Human genes 0.000 description 1
- 108090000144 Human Proteins Proteins 0.000 description 1
- 241000282620 Hylobates sp. Species 0.000 description 1
- 102100023915 Insulin Human genes 0.000 description 1
- 108010073961 Insulin Aspart Proteins 0.000 description 1
- 108010057186 Insulin Glargine Proteins 0.000 description 1
- 108010065920 Insulin Lispro Proteins 0.000 description 1
- 102000003746 Insulin Receptor Human genes 0.000 description 1
- 108010001127 Insulin Receptor Proteins 0.000 description 1
- FYZPCMFQCNBYCY-WIWKJPBBSA-N Insulin degludec Chemical compound CC[C@H](C)[C@H](NC(=O)CN)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@H]1CSSC[C@@H]2NC(=O)[C@@H](NC(=O)[C@H](CO)NC(=O)[C@@H](NC(=O)[C@H](CSSC[C@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](Cc3c[nH]cn3)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](NC(=O)[C@@H](N)Cc3ccccc3)C(C)C)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](Cc3c[nH]cn3)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](Cc3ccc(O)cc3)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](Cc3ccc(O)cc3)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](Cc3ccc(O)cc3)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CO)NC2=O)C(=O)N[C@@H](CC(N)=O)C(O)=O)C(=O)NCC(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)NCC(=O)N[C@@H](Cc2ccccc2)C(=O)N[C@@H](Cc2ccccc2)C(=O)N[C@@H](Cc2ccc(O)cc2)C(=O)N[C@@H]([C@@H](C)O)C(=O)N2CCC[C@H]2C(=O)N[C@@H](CCCCNC(=O)CC[C@H](NC(=O)CCCCCCCCCCCCCCC(O)=O)C(O)=O)C(O)=O)NC1=O)[C@@H](C)O)[C@@H](C)CC FYZPCMFQCNBYCY-WIWKJPBBSA-N 0.000 description 1
- COCFEDIXXNGUNL-RFKWWTKHSA-N Insulin glargine Chemical compound C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@H]1CSSC[C@H]2C(=O)N[C@H](C(=O)N[C@@H](CO)C(=O)N[C@H](C(=O)N[C@H](C(N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=3C=CC(O)=CC=3)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC=3C=CC(O)=CC=3)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=3C=CC(O)=CC=3)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=3NC=NC=3)NC(=O)[C@H](CO)NC(=O)CNC1=O)C(=O)NCC(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)NCC(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O)C(=O)NCC(O)=O)=O)CSSC[C@@H](C(N2)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C(C)C)NC(=O)[C@@H](NC(=O)CN)[C@@H](C)CC)[C@@H](C)CC)[C@@H](C)O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](NC(=O)[C@@H](N)CC=1C=CC=CC=1)C(C)C)C1=CN=CN1 COCFEDIXXNGUNL-RFKWWTKHSA-N 0.000 description 1
- 108700021006 Interleukin-1 receptor antagonist Proteins 0.000 description 1
- 108090001005 Interleukin-6 Proteins 0.000 description 1
- 102000004889 Interleukin-6 Human genes 0.000 description 1
- 208000032382 Ischaemic stroke Diseases 0.000 description 1
- 150000008575 L-amino acids Chemical class 0.000 description 1
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 1
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 1
- 102000002297 Laminin Receptors Human genes 0.000 description 1
- 108010000851 Laminin Receptors Proteins 0.000 description 1
- 239000000232 Lipid Bilayer Substances 0.000 description 1
- 208000019693 Lung disease Diseases 0.000 description 1
- 239000004472 Lysine Substances 0.000 description 1
- 102000043136 MAP kinase family Human genes 0.000 description 1
- 108091054455 MAP kinase family Proteins 0.000 description 1
- 241000282553 Macaca Species 0.000 description 1
- 241000282560 Macaca mulatta Species 0.000 description 1
- 241000124008 Mammalia Species 0.000 description 1
- 208000001826 Marfan syndrome Diseases 0.000 description 1
- 108010076557 Matrix Metalloproteinase 14 Proteins 0.000 description 1
- 102100030216 Matrix metalloproteinase-14 Human genes 0.000 description 1
- 102100030412 Matrix metalloproteinase-9 Human genes 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 108010006519 Molecular Chaperones Proteins 0.000 description 1
- 102000005431 Molecular Chaperones Human genes 0.000 description 1
- 102000014962 Monocyte Chemoattractant Proteins Human genes 0.000 description 1
- 108010064136 Monocyte Chemoattractant Proteins Proteins 0.000 description 1
- 101000999002 Mus musculus Insulin-1 Proteins 0.000 description 1
- 101001012173 Mus musculus Insulin-2 Proteins 0.000 description 1
- DPUYCSDGMSDKKV-MKBYFEBXSA-N N-Acetyl-L-leucyl-L-isoleucylglycyl-L-valyl-N-methyl-L-prolinamide Chemical compound CC(C)C[C@H](NC(C)=O)C(=O)N[C@@H]([C@@H](C)CC)C(=O)NCC(=O)N[C@@H](C(C)C)C(=O)N1CCC[C@H]1C(=O)NC DPUYCSDGMSDKKV-MKBYFEBXSA-N 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- 206010033307 Overweight Diseases 0.000 description 1
- 241000282577 Pan troglodytes Species 0.000 description 1
- 102000016387 Pancreatic elastase Human genes 0.000 description 1
- 108010067372 Pancreatic elastase Proteins 0.000 description 1
- 241001494479 Pecora Species 0.000 description 1
- 208000018262 Peripheral vascular disease Diseases 0.000 description 1
- 102000013566 Plasminogen Human genes 0.000 description 1
- 108010051456 Plasminogen Proteins 0.000 description 1
- 241000036156 Pontogammarus obesus Species 0.000 description 1
- 241000077802 Procambarus troglodytes Species 0.000 description 1
- 102000006437 Proprotein Convertases Human genes 0.000 description 1
- 108010044159 Proprotein Convertases Proteins 0.000 description 1
- 241000700157 Rattus norvegicus Species 0.000 description 1
- 101000999001 Rattus norvegicus Insulin-1 Proteins 0.000 description 1
- 101001012176 Rattus norvegicus Insulin-2 Proteins 0.000 description 1
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 1
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 1
- 208000001647 Renal Insufficiency Diseases 0.000 description 1
- 108091081062 Repeated sequence (DNA) Proteins 0.000 description 1
- 206010040070 Septic Shock Diseases 0.000 description 1
- 101710128612 Sialidase-1 Proteins 0.000 description 1
- 208000007718 Stable Angina Diseases 0.000 description 1
- 229940100389 Sulfonylurea Drugs 0.000 description 1
- JLRGJRBPOGGCBT-UHFFFAOYSA-N Tolbutamide Chemical compound CCCCNC(=O)NS(=O)(=O)C1=CC=C(C)C=C1 JLRGJRBPOGGCBT-UHFFFAOYSA-N 0.000 description 1
- 108060008682 Tumor Necrosis Factor Proteins 0.000 description 1
- 102000000852 Tumor Necrosis Factor-alpha Human genes 0.000 description 1
- 201000004810 Vascular dementia Diseases 0.000 description 1
- 230000002159 abnormal effect Effects 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 230000003919 adipocyte function Effects 0.000 description 1
- 239000011543 agarose gel Substances 0.000 description 1
- 238000003915 air pollution Methods 0.000 description 1
- 229960004238 anakinra Drugs 0.000 description 1
- 238000002583 angiography Methods 0.000 description 1
- 238000000137 annealing Methods 0.000 description 1
- 230000003042 antagnostic effect Effects 0.000 description 1
- 208000007474 aortic aneurysm Diseases 0.000 description 1
- RCHHVVGSTHAVPF-ZPHPLDECSA-N apidra Chemical compound C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@H]1CSSC[C@H]2C(=O)N[C@H](C(=O)N[C@@H](CO)C(=O)N[C@H](C(=O)N[C@H](C(N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=3C=CC(O)=CC=3)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC=3C=CC(O)=CC=3)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=3C=CC(O)=CC=3)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=3N=CNC=3)NC(=O)[C@H](CO)NC(=O)CNC1=O)C(=O)NCC(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)NCC(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H]([C@@H](C)O)C(O)=O)C(=O)N[C@@H](CC(N)=O)C(O)=O)=O)CSSC[C@@H](C(N2)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C(C)C)NC(=O)[C@@H](NC(=O)CN)[C@@H](C)CC)[C@@H](C)CC)[C@@H](C)O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](NC(=O)[C@@H](N)CC=1C=CC=CC=1)C(C)C)C1=CNC=N1 RCHHVVGSTHAVPF-ZPHPLDECSA-N 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 125000000637 arginyl group Chemical group N[C@@H](CCCNC(N)=N)C(=O)* 0.000 description 1
- 125000000613 asparagine group Chemical group N[C@@H](CC(N)=O)C(=O)* 0.000 description 1
- CKLJMWTZIZZHCS-REOHCLBHSA-L aspartate group Chemical group N[C@@H](CC(=O)[O-])C(=O)[O-] CKLJMWTZIZZHCS-REOHCLBHSA-L 0.000 description 1
- 230000036523 atherogenesis Effects 0.000 description 1
- 230000000923 atherogenic effect Effects 0.000 description 1
- 230000003305 autocrine Effects 0.000 description 1
- SQVRNKJHWKZAKO-UHFFFAOYSA-N beta-N-Acetyl-D-neuraminic acid Natural products CC(=O)NC1C(O)CC(O)(C(O)=O)OC1C(O)C(O)CO SQVRNKJHWKZAKO-UHFFFAOYSA-N 0.000 description 1
- 108091008324 binding proteins Proteins 0.000 description 1
- 230000008827 biological function Effects 0.000 description 1
- 230000008512 biological response Effects 0.000 description 1
- 229920001222 biopolymer Polymers 0.000 description 1
- 210000004556 brain Anatomy 0.000 description 1
- 230000015916 branching morphogenesis of a tube Effects 0.000 description 1
- 210000000692 cap cell Anatomy 0.000 description 1
- 210000004413 cardiac myocyte Anatomy 0.000 description 1
- 230000003197 catalytic effect Effects 0.000 description 1
- 150000001768 cations Chemical class 0.000 description 1
- 230000034196 cell chemotaxis Effects 0.000 description 1
- 210000000170 cell membrane Anatomy 0.000 description 1
- 230000004663 cell proliferation Effects 0.000 description 1
- 108091092328 cellular RNA Proteins 0.000 description 1
- 230000036755 cellular response Effects 0.000 description 1
- 125000003636 chemical group Chemical group 0.000 description 1
- 239000007795 chemical reaction product Substances 0.000 description 1
- 210000001612 chondrocyte Anatomy 0.000 description 1
- 229960004407 chorionic gonadotrophin Drugs 0.000 description 1
- 229940015047 chorionic gonadotropin Drugs 0.000 description 1
- 208000022831 chronic renal failure syndrome Diseases 0.000 description 1
- 239000002299 complementary DNA Substances 0.000 description 1
- 210000002808 connective tissue Anatomy 0.000 description 1
- 208000029078 coronary artery disease Diseases 0.000 description 1
- 210000004748 cultured cell Anatomy 0.000 description 1
- 230000001186 cumulative effect Effects 0.000 description 1
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 1
- 230000007850 degeneration Effects 0.000 description 1
- 238000004925 denaturation Methods 0.000 description 1
- 230000036425 denaturation Effects 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 238000000151 deposition Methods 0.000 description 1
- 230000008021 deposition Effects 0.000 description 1
- 230000003831 deregulation Effects 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 238000002405 diagnostic procedure Methods 0.000 description 1
- 230000003292 diminished effect Effects 0.000 description 1
- 238000013399 early diagnosis Methods 0.000 description 1
- 235000005686 eating Nutrition 0.000 description 1
- 230000012202 endocytosis Effects 0.000 description 1
- 210000002472 endoplasmic reticulum Anatomy 0.000 description 1
- 230000008694 endothelial dysfunction Effects 0.000 description 1
- 230000007613 environmental effect Effects 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 230000029142 excretion Effects 0.000 description 1
- 238000004992 fast atom bombardment mass spectroscopy Methods 0.000 description 1
- 102000013370 fibrillin Human genes 0.000 description 1
- 108060002895 fibrillin Proteins 0.000 description 1
- 238000013467 fragmentation Methods 0.000 description 1
- 238000006062 fragmentation reaction Methods 0.000 description 1
- 239000000446 fuel Substances 0.000 description 1
- 125000002519 galactosyl group Chemical group C1([C@H](O)[C@@H](O)[C@@H](O)[C@H](O1)CO)* 0.000 description 1
- 150000002270 gangliosides Chemical class 0.000 description 1
- 230000002496 gastric effect Effects 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 101150091511 glb-1 gene Proteins 0.000 description 1
- 229930195712 glutamate Natural products 0.000 description 1
- 125000000404 glutamine group Chemical group N[C@@H](CCC(N)=O)C(=O)* 0.000 description 1
- 230000002641 glycemic effect Effects 0.000 description 1
- 125000003630 glycyl group Chemical group [H]N([H])C([H])([H])C(*)=O 0.000 description 1
- 230000012010 growth Effects 0.000 description 1
- 210000000425 gut endothelial cell Anatomy 0.000 description 1
- 210000003494 hepatocyte Anatomy 0.000 description 1
- 125000000487 histidyl group Chemical group [H]N([H])C(C(=O)O*)C([H])([H])C1=C([H])N([H])C([H])=N1 0.000 description 1
- 230000003054 hormonal effect Effects 0.000 description 1
- WNRQPCUGRUFHED-DETKDSODSA-N humalog Chemical compound C([C@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CO)NC(=O)[C@H](CS)NC(=O)[C@H]([C@@H](C)CC)NC(=O)[C@H](CO)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CS)NC(=O)[C@H](CS)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C(C)C)NC(=O)[C@@H](NC(=O)CN)[C@@H](C)CC)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CS)C(=O)N[C@@H](CC(N)=O)C(O)=O)C1=CC=C(O)C=C1.C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@H](C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CS)C(=O)NCC(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)NCC(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCCCN)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H]([C@@H](C)O)C(O)=O)C(C)C)NC(=O)[C@H](CO)NC(=O)CNC(=O)[C@H](CS)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=1NC=NC=1)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](NC(=O)[C@@H](N)CC=1C=CC=CC=1)C(C)C)C1=CN=CN1 WNRQPCUGRUFHED-DETKDSODSA-N 0.000 description 1
- 102000054554 human EBP Human genes 0.000 description 1
- 102000048551 human LGALS3 Human genes 0.000 description 1
- 102000043827 human Smooth muscle Human genes 0.000 description 1
- 108700038605 human Smooth muscle Proteins 0.000 description 1
- 230000007062 hydrolysis Effects 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- 230000002779 inactivation Effects 0.000 description 1
- 238000010348 incorporation Methods 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 208000015181 infectious disease Diseases 0.000 description 1
- 210000004969 inflammatory cell Anatomy 0.000 description 1
- 230000005764 inhibitory process Effects 0.000 description 1
- 230000015788 innate immune response Effects 0.000 description 1
- 229960004717 insulin aspart Drugs 0.000 description 1
- 108010050259 insulin degludec Proteins 0.000 description 1
- 229960004225 insulin degludec Drugs 0.000 description 1
- 239000004026 insulin derivative Substances 0.000 description 1
- 229960002869 insulin glargine Drugs 0.000 description 1
- 108700039926 insulin glulisine Proteins 0.000 description 1
- 229960000696 insulin glulisine Drugs 0.000 description 1
- 229960002068 insulin lispro Drugs 0.000 description 1
- 230000002452 interceptive effect Effects 0.000 description 1
- 125000000741 isoleucyl group Chemical group [H]N([H])C(C(C([H])([H])[H])C([H])([H])C([H])([H])[H])C(=O)O* 0.000 description 1
- 201000006370 kidney failure Diseases 0.000 description 1
- 125000001909 leucine group Chemical group [H]N(*)C(C(*)=O)C([H])([H])C(C([H])([H])[H])C([H])([H])[H] 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 238000004811 liquid chromatography Methods 0.000 description 1
- 210000005229 liver cell Anatomy 0.000 description 1
- 230000033001 locomotion Effects 0.000 description 1
- 125000003588 lysine group Chemical group [H]N([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 1
- 230000002132 lysosomal effect Effects 0.000 description 1
- 210000003712 lysosome Anatomy 0.000 description 1
- 230000001868 lysosomic effect Effects 0.000 description 1
- 229950004994 meglitinide Drugs 0.000 description 1
- 238000010197 meta-analysis Methods 0.000 description 1
- 230000004060 metabolic process Effects 0.000 description 1
- 229930182817 methionine Natural products 0.000 description 1
- 230000005012 migration Effects 0.000 description 1
- 230000000116 mitigating effect Effects 0.000 description 1
- 230000028550 monocyte chemotaxis Effects 0.000 description 1
- 210000003205 muscle Anatomy 0.000 description 1
- 210000000663 muscle cell Anatomy 0.000 description 1
- 230000010807 negative regulation of binding Effects 0.000 description 1
- 210000005036 nerve Anatomy 0.000 description 1
- VOMXSOIBEJBQNF-UTTRGDHVSA-N novorapid Chemical compound C([C@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CO)NC(=O)[C@H](CS)NC(=O)[C@H]([C@@H](C)CC)NC(=O)[C@H](CO)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CS)NC(=O)[C@H](CS)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C(C)C)NC(=O)[C@@H](NC(=O)CN)[C@@H](C)CC)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CS)C(=O)N[C@@H](CC(N)=O)C(O)=O)C1=CC=C(O)C=C1.C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@H](C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CS)C(=O)NCC(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)NCC(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H]([C@@H](C)O)C(O)=O)C(C)C)NC(=O)[C@H](CO)NC(=O)CNC(=O)[C@H](CS)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=1NC=NC=1)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](NC(=O)[C@@H](N)CC=1C=CC=CC=1)C(C)C)C1=CN=CN1 VOMXSOIBEJBQNF-UTTRGDHVSA-N 0.000 description 1
- 238000005457 optimization Methods 0.000 description 1
- 239000006186 oral dosage form Substances 0.000 description 1
- 230000008520 organization Effects 0.000 description 1
- 230000003076 paracrine Effects 0.000 description 1
- 239000013618 particulate matter Substances 0.000 description 1
- 230000008506 pathogenesis Effects 0.000 description 1
- 230000001575 pathological effect Effects 0.000 description 1
- 230000001991 pathophysiological effect Effects 0.000 description 1
- 230000006995 pathophysiological pathway Effects 0.000 description 1
- 230000037361 pathway Effects 0.000 description 1
- 108010011903 peptide receptors Proteins 0.000 description 1
- 238000010647 peptide synthesis reaction Methods 0.000 description 1
- COLNVLDHVKWLRT-QMMMGPOBSA-N phenylalanine group Chemical group N[C@@H](CC1=CC=CC=C1)C(=O)O COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 1
- 230000004962 physiological condition Effects 0.000 description 1
- 230000035479 physiological effects, processes and functions Effects 0.000 description 1
- 230000036470 plasma concentration Effects 0.000 description 1
- 238000003752 polymerase chain reaction Methods 0.000 description 1
- 239000002243 precursor Substances 0.000 description 1
- 201000009104 prediabetes syndrome Diseases 0.000 description 1
- 235000020991 processed meat Nutrition 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 230000000750 progressive effect Effects 0.000 description 1
- 125000001500 prolyl group Chemical group [H]N1C([H])(C(=O)[*])C([H])([H])C([H])([H])C1([H])[H] 0.000 description 1
- 230000001737 promoting effect Effects 0.000 description 1
- 229940076376 protein agonist Drugs 0.000 description 1
- 230000005855 radiation Effects 0.000 description 1
- 238000004064 recycling Methods 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 230000002829 reductive effect Effects 0.000 description 1
- 230000008929 regeneration Effects 0.000 description 1
- 238000011069 regeneration method Methods 0.000 description 1
- 230000029556 regulation of feeding behavior Effects 0.000 description 1
- 238000007634 remodeling Methods 0.000 description 1
- 210000001525 retina Anatomy 0.000 description 1
- 238000010839 reverse transcription Methods 0.000 description 1
- 238000004007 reversed phase HPLC Methods 0.000 description 1
- 238000012552 review Methods 0.000 description 1
- 102200026932 rs121908274 Human genes 0.000 description 1
- 102200026933 rs121908279 Human genes 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 230000036303 septic shock Effects 0.000 description 1
- 125000003607 serino group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(O[H])([H])[H] 0.000 description 1
- SQVRNKJHWKZAKO-OQPLDHBCSA-N sialic acid Chemical compound CC(=O)N[C@@H]1[C@@H](O)C[C@@](O)(C(O)=O)OC1[C@H](O)[C@H](O)CO SQVRNKJHWKZAKO-OQPLDHBCSA-N 0.000 description 1
- 230000019491 signal transduction Effects 0.000 description 1
- 210000002027 skeletal muscle Anatomy 0.000 description 1
- 210000001626 skin fibroblast Anatomy 0.000 description 1
- 239000000779 smoke Substances 0.000 description 1
- 239000008107 starch Substances 0.000 description 1
- 230000035882 stress Effects 0.000 description 1
- 238000012916 structural analysis Methods 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- YROXIXLRRCOBKF-UHFFFAOYSA-N sulfonylurea Chemical class OC(=N)N=S(=O)=O YROXIXLRRCOBKF-UHFFFAOYSA-N 0.000 description 1
- 125000000341 threoninyl group Chemical group [H]OC([H])(C([H])([H])[H])C([H])(N([H])[H])C(*)=O 0.000 description 1
- 208000037816 tissue injury Diseases 0.000 description 1
- 125000000430 tryptophan group Chemical group [H]N([H])C(C(=O)O*)C([H])([H])C1=C([H])N([H])C2=C([H])C([H])=C([H])C([H])=C12 0.000 description 1
- 210000005233 tubule cell Anatomy 0.000 description 1
- 125000001493 tyrosinyl group Chemical group [H]OC1=C([H])C([H])=C(C([H])=C1[H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 1
- 230000003827 upregulation Effects 0.000 description 1
- 238000011144 upstream manufacturing Methods 0.000 description 1
- 210000002700 urine Anatomy 0.000 description 1
- 125000002987 valine group Chemical group [H]N([H])C([H])(C(*)=O)C([H])(C([H])([H])[H])C([H])([H])[H] 0.000 description 1
- 230000029663 wound healing Effects 0.000 description 1
Classifications
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/575—Hormones
- C07K14/62—Insulins
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/705—Receptors; Cell surface antigens; Cell surface determinants
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
- G01N33/564—Immunoassay; Biospecific binding assay; Materials therefor for pre-existing immune complex or autoimmune disease, i.e. systemic lupus erythematosus, rheumatoid arthritis, multiple sclerosis, rheumatoid factors or complement components C1-C9
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
- G01N33/566—Immunoassay; Biospecific binding assay; Materials therefor using specific carrier or receptor proteins as ligand binding reagents where possible specific carrier or receptor proteins are classified with their target compounds
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
- G01N33/577—Immunoassay; Biospecific binding assay; Materials therefor involving monoclonal antibodies binding reaction mechanisms characterised by the use of monoclonal antibodies; monoclonal antibodies per se are classified with their corresponding antigens
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/78—Connective tissue peptides, e.g. collagen, elastin, laminin, fibronectin, vitronectin or cold insoluble globulin [CIG]
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2333/00—Assays involving biological materials from specific organisms or of a specific nature
- G01N2333/435—Assays involving biological materials from specific organisms or of a specific nature from animals; from humans
- G01N2333/575—Hormones
- G01N2333/62—Insulins
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2333/00—Assays involving biological materials from specific organisms or of a specific nature
- G01N2333/435—Assays involving biological materials from specific organisms or of a specific nature from animals; from humans
- G01N2333/78—Connective tissue peptides, e.g. collagen, elastin, laminin, fibronectin, vitronectin, cold insoluble globulin [CIG]
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2500/00—Screening for compounds of potential therapeutic value
- G01N2500/02—Screening involving studying the effect of compounds C on the interaction between interacting molecules A and B (e.g. A = enzyme and B = substrate for A, or A = receptor and B = ligand for the receptor)
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2800/00—Detection or diagnosis of diseases
- G01N2800/04—Endocrine or metabolic disorders
- G01N2800/042—Disorders of carbohydrate metabolism, e.g. diabetes, glucose metabolism
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2800/00—Detection or diagnosis of diseases
- G01N2800/32—Cardiovascular disorders
- G01N2800/323—Arteriosclerosis, Stenosis
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Immunology (AREA)
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Molecular Biology (AREA)
- Hematology (AREA)
- Urology & Nephrology (AREA)
- Biomedical Technology (AREA)
- Medicinal Chemistry (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- Cell Biology (AREA)
- Analytical Chemistry (AREA)
- General Physics & Mathematics (AREA)
- Pathology (AREA)
- Physics & Mathematics (AREA)
- Food Science & Technology (AREA)
- Biotechnology (AREA)
- Microbiology (AREA)
- Organic Chemistry (AREA)
- Gastroenterology & Hepatology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Zoology (AREA)
- Genetics & Genomics (AREA)
- Biophysics (AREA)
- Toxicology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Endocrinology (AREA)
- Diabetes (AREA)
- Rehabilitation Therapy (AREA)
- Rheumatology (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| EP17154889.4 | 2017-02-06 | ||
| EP17154889 | 2017-02-06 | ||
| PCT/EP2018/052822 WO2018141969A1 (en) | 2017-02-06 | 2018-02-05 | Peptide modulators of the interaction between human c-peptide and human elastin receptor for therapeutic use |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA3051293A1 true CA3051293A1 (en) | 2018-08-09 |
Family
ID=57995050
Family Applications (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA3051293A Pending CA3051293A1 (en) | 2017-02-06 | 2018-02-05 | Peptide modulators of the interaction between human c-peptide and human elastin receptor for therapeutic use |
| CA3049738A Pending CA3049738A1 (en) | 2017-02-06 | 2018-02-05 | Interaction between c-peptides and elastin receptor, a model for understanding vascular disease |
Family Applications After (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA3049738A Pending CA3049738A1 (en) | 2017-02-06 | 2018-02-05 | Interaction between c-peptides and elastin receptor, a model for understanding vascular disease |
Country Status (8)
| Country | Link |
|---|---|
| US (4) | US20200087374A1 (cg-RX-API-DMAC7.html) |
| EP (3) | EP3577462B1 (cg-RX-API-DMAC7.html) |
| JP (2) | JP7438757B2 (cg-RX-API-DMAC7.html) |
| AU (2) | AU2018215245B2 (cg-RX-API-DMAC7.html) |
| CA (2) | CA3051293A1 (cg-RX-API-DMAC7.html) |
| ES (1) | ES2927977T3 (cg-RX-API-DMAC7.html) |
| SG (2) | SG11201906939XA (cg-RX-API-DMAC7.html) |
| WO (2) | WO2018141969A1 (cg-RX-API-DMAC7.html) |
Families Citing this family (10)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP6982395B2 (ja) * | 2017-03-16 | 2021-12-17 | 三洋化成工業株式会社 | インターロイキン１０の産生量増加剤 |
| WO2019104391A1 (en) * | 2017-12-01 | 2019-06-06 | St Vincent's Institute Of Medical Research | Type 1 diabetes treatment |
| AU2020337111A1 (en) * | 2019-08-30 | 2022-03-31 | Biotempt B.V. | Q-ER peptide |
| JP6895148B1 (ja) * | 2020-03-31 | 2021-06-30 | クラシエホールディングス株式会社 | 冷え保有者における冷えの原因が、腎機能低下、水分代謝異常又は副腎疲労にあることを判定する判定用マーカー、冷え保有者における冷えの原因が、腎機能低下、水分代謝異常又は副腎疲労にあることを判定する判定方法、及び冷え保有者における冷えの原因が、腎機能低下、水分代謝異常又は副腎疲労にあることを判定するための判定用キット |
| CN117106029A (zh) * | 2020-06-08 | 2023-11-24 | 深圳市图微安创科技开发有限公司 | 靶向于纤连蛋白衍生肽的抑制剂多肽化合物及其用途 |
| JP2023544832A (ja) * | 2020-10-08 | 2023-10-25 | ドクター メアリー モリス アンド アソシエイツ リミテッド ライアビリティ カンパニー | １型糖尿病の治療および予防のための方法および組成物 |
| CN112345770A (zh) * | 2020-11-06 | 2021-02-09 | 苏州大学附属第一医院 | 弹性蛋白降解肽作为腹膜透析患者血管钙化标志物的应用 |
| KR102718109B1 (ko) * | 2021-10-01 | 2024-10-17 | (주)케어젠 | 탈모 방지 또는 발모 촉진 활성을 갖는 펩타이드와 이의 용도 |
| AU2022359382A1 (en) * | 2021-10-05 | 2024-05-02 | Biotempt B.V. | Angiogenic control, preferably combined with glycaemic control. |
| EP4554672A1 (en) | 2022-07-12 | 2025-05-21 | Resiliun B.V. | Treating conditions with hypoglycemia associated with hyperinsulinemia |
Family Cites Families (16)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| SE520392C2 (sv) | 1996-09-27 | 2003-07-01 | Creative Peptides Sweden Ab C | Specifika peptider för behandling av diabetes mellitus |
| US6734289B2 (en) * | 2001-03-29 | 2004-05-11 | The University Of Chicago | Gastrokines and derived peptides including inhibitors |
| EP1578352A2 (en) * | 2002-03-27 | 2005-09-28 | University of Utah Research Foundation | Elastin prevents occlusion of body vessels by vascular smooth muscle cells |
| GB0218970D0 (en) | 2002-08-14 | 2002-09-25 | Creative Peptides Sweden Ab | Fragments of Insulin c-peptide |
| GB0323979D0 (en) * | 2003-10-13 | 2003-11-19 | Creative Peptides Sweden Ab | Therapeutic applications for c-peptide |
| GB0412174D0 (en) * | 2004-06-01 | 2004-06-30 | Creative Peptides Sweden Ab | Degradation-resistant analogues of pro-insulin c-peptide |
| WO2008118387A2 (en) * | 2007-03-23 | 2008-10-02 | Wayne State University | Erythrocyte atp-release modulators |
| EP2480888B1 (en) * | 2009-09-25 | 2016-11-30 | XOMA Technology Ltd. | Screening methods |
| CN104105966B (zh) * | 2012-02-01 | 2016-10-26 | 弗·哈夫曼-拉罗切有限公司 | 用于检测多特异性结合物的结合搭档的方法 |
| EP2626704B1 (en) * | 2012-02-08 | 2015-11-18 | Mehmet Ali Soylemez | Diagnosis of pancreatic diabetes in patients with normal blood leucocyte counts using procalcitonin |
| BR112014025189B1 (pt) * | 2012-04-12 | 2020-04-07 | Brahms Gmbh | métodos de predizer o risco de adquirir um evento adverso e de orientação de tratamento com antibióticos em um paciente com insuficiência cardíaca crônica estável |
| WO2014028776A1 (en) * | 2012-08-15 | 2014-02-20 | Zyngenia, Inc. | Monovalent and multivalent multispecific complexes and uses thereof |
| JP6430962B2 (ja) * | 2013-01-08 | 2018-11-28 | シュピーンゴテック ゲゼルシャフト ミット ベシュレンクテル ハフツング | 心血管系疾患発症リスクの予測的マーカーとしての成長ホルモンの空腹時レベル |
| EP2972339A1 (en) * | 2013-03-15 | 2016-01-20 | Health Diagnostic Laboratory, Inc. | Method of generating an index score for mbl deficiency to predict cardiodiabetes risk |
| CN104371003B (zh) * | 2013-08-15 | 2025-09-02 | 上海市第一人民医院 | 预防和治疗炎症的小分子多肽及其应用 |
| US20170138961A1 (en) * | 2014-03-21 | 2017-05-18 | Sanofi-Aventis Deutschland Gmbh | New markers for the assessment of the risk for development of a cardiovascular disorder |
-
2018
- 2018-02-05 SG SG11201906939XA patent/SG11201906939XA/en unknown
- 2018-02-05 EP EP18705844.1A patent/EP3577462B1/en active Active
- 2018-02-05 EP EP24170487.3A patent/EP4421088A3/en not_active Withdrawn
- 2018-02-05 US US16/483,717 patent/US20200087374A1/en not_active Abandoned
- 2018-02-05 AU AU2018215245A patent/AU2018215245B2/en active Active
- 2018-02-05 AU AU2018216033A patent/AU2018216033B2/en active Active
- 2018-02-05 CA CA3051293A patent/CA3051293A1/en active Pending
- 2018-02-05 CA CA3049738A patent/CA3049738A1/en active Pending
- 2018-02-05 EP EP18705843.3A patent/EP3570875B1/en active Active
- 2018-02-05 ES ES18705843T patent/ES2927977T3/es active Active
- 2018-02-05 WO PCT/EP2018/052822 patent/WO2018141969A1/en not_active Ceased
- 2018-02-05 JP JP2019563680A patent/JP7438757B2/ja active Active
- 2018-02-05 US US16/483,317 patent/US20220009988A1/en not_active Abandoned
- 2018-02-05 WO PCT/EP2018/052824 patent/WO2018141970A1/en not_active Ceased
- 2018-02-05 SG SG11201906943VA patent/SG11201906943VA/en unknown
-
2023
- 2023-05-01 US US18/310,188 patent/US20240027431A1/en not_active Abandoned
-
2024
- 2024-02-13 JP JP2024019238A patent/JP2024056838A/ja active Pending
- 2024-11-26 US US18/960,532 patent/US20250123275A1/en active Pending
Also Published As
| Publication number | Publication date |
|---|---|
| US20240027431A1 (en) | 2024-01-25 |
| JP7438757B2 (ja) | 2024-02-27 |
| SG11201906939XA (en) | 2019-08-27 |
| US20250123275A1 (en) | 2025-04-17 |
| JP2024056838A (ja) | 2024-04-23 |
| CA3049738A1 (en) | 2018-08-09 |
| JP2020507623A (ja) | 2020-03-12 |
| EP4421088A2 (en) | 2024-08-28 |
| AU2018216033B2 (en) | 2021-10-07 |
| US20200087374A1 (en) | 2020-03-19 |
| WO2018141970A1 (en) | 2018-08-09 |
| EP3577462C0 (en) | 2024-04-17 |
| EP3570875A1 (en) | 2019-11-27 |
| ES2927977T3 (es) | 2022-11-14 |
| WO2018141969A1 (en) | 2018-08-09 |
| EP3577462A1 (en) | 2019-12-11 |
| EP4421088A3 (en) | 2024-12-04 |
| EP3570875B1 (en) | 2022-07-06 |
| AU2018215245B2 (en) | 2024-07-11 |
| US20220009988A1 (en) | 2022-01-13 |
| AU2018215245A1 (en) | 2019-07-25 |
| SG11201906943VA (en) | 2019-08-27 |
| AU2018216033A1 (en) | 2019-08-15 |
| EP3577462B1 (en) | 2024-04-17 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US20250123275A1 (en) | Peptide modulators of the interaction between human c-peptide and human elastin receptor for therapeutic use | |
| CN102459348A (zh) | 用于将gdnf和bdnf递送至中枢神经系统的融合蛋白 | |
| EP3826662B9 (en) | Method of using a gip/glp1 co-agonist for diabetes | |
| US20210340211A1 (en) | Gip peptide analogues | |
| KR20220109384A (ko) | Q-er 펩타이드 | |
| KR20160098406A (ko) | 프로테아제 내성 펩티드 | |
| AU2019386379B2 (en) | DPEP-1 binding agents and methods of use | |
| JP2011525895A (ja) | アミリン及びサケカルシトニンの誘導体化ハイブリッドペプチド | |
| EP2252314B1 (en) | Leptin agonist and methods of use | |
| Straus et al. | ROSALYN S. YALOW | |
| US20090197800A1 (en) | Insulin Receptor Binding Peptides with Non-Insulin Gene Activation Profiles and Uses Thereof | |
| KR101156992B1 (ko) | 혈압 강하 활성을 가지는 펩티드 | |
| HK40042746B (en) | Method of using a gip/glp1 co-agonist for diabetes |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| EEER | Examination request |
Effective date: 20220929 |
|
| EEER | Examination request |
Effective date: 20220929 |
|
| EEER | Examination request |
Effective date: 20220929 |
|
| EEER | Examination request |
Effective date: 20220929 |