CA2361612A1 - Activites de modulation des peptides de l'heparine, et d'autres glycosaminoglycanes ou proteoglycanes - Google Patents
Activites de modulation des peptides de l'heparine, et d'autres glycosaminoglycanes ou proteoglycanes Download PDFInfo
- Publication number
- CA2361612A1 CA2361612A1 CA002361612A CA2361612A CA2361612A1 CA 2361612 A1 CA2361612 A1 CA 2361612A1 CA 002361612 A CA002361612 A CA 002361612A CA 2361612 A CA2361612 A CA 2361612A CA 2361612 A1 CA2361612 A1 CA 2361612A1
- Authority
- CA
- Canada
- Prior art keywords
- mammal
- peptide
- effective amount
- heparin
- administered
- 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.)
- Abandoned
Links
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 330
- HTTJABKRGRZYRN-UHFFFAOYSA-N Heparin Chemical compound OC1C(NC(=O)C)C(O)OC(COS(O)(=O)=O)C1OC1C(OS(O)(=O)=O)C(O)C(OC2C(C(OS(O)(=O)=O)C(OC3C(C(O)C(O)C(O3)C(O)=O)OS(O)(=O)=O)C(CO)O2)NS(O)(=O)=O)C(C(O)=O)O1 HTTJABKRGRZYRN-UHFFFAOYSA-N 0.000 title claims abstract description 291
- 229920000669 heparin Polymers 0.000 title claims abstract description 277
- 229960002897 heparin Drugs 0.000 title claims abstract description 274
- 229920002683 Glycosaminoglycan Polymers 0.000 title claims abstract description 83
- 102000016611 Proteoglycans Human genes 0.000 title claims abstract description 82
- 108010067787 Proteoglycans Proteins 0.000 title claims abstract description 82
- 102000004196 processed proteins & peptides Human genes 0.000 title abstract description 159
- 230000000694 effects Effects 0.000 title description 60
- 238000000034 method Methods 0.000 claims abstract description 72
- 210000004027 cell Anatomy 0.000 claims description 78
- 235000001014 amino acid Nutrition 0.000 claims description 51
- 150000001413 amino acids Chemical class 0.000 claims description 50
- 210000002889 endothelial cell Anatomy 0.000 claims description 34
- 229940079593 drug Drugs 0.000 claims description 23
- 239000003814 drug Substances 0.000 claims description 23
- 239000004475 Arginine Substances 0.000 claims description 21
- 102000004190 Enzymes Human genes 0.000 claims description 21
- 108090000790 Enzymes Proteins 0.000 claims description 21
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 claims description 21
- 238000000338 in vitro Methods 0.000 claims description 21
- 210000001519 tissue Anatomy 0.000 claims description 19
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 claims description 17
- 239000004472 Lysine Substances 0.000 claims description 17
- 239000003146 anticoagulant agent Substances 0.000 claims description 15
- 210000003462 vein Anatomy 0.000 claims description 15
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical group NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 claims description 13
- 229940127219 anticoagulant drug Drugs 0.000 claims description 13
- 230000012010 growth Effects 0.000 claims description 13
- 238000001727 in vivo Methods 0.000 claims description 13
- 230000001737 promoting effect Effects 0.000 claims description 13
- 230000004087 circulation Effects 0.000 claims description 12
- 235000004279 alanine Nutrition 0.000 claims description 11
- 210000000845 cartilage Anatomy 0.000 claims description 11
- 210000003038 endothelium Anatomy 0.000 claims description 10
- 239000000758 substrate Substances 0.000 claims description 10
- 206010027476 Metastases Diseases 0.000 claims description 9
- 230000000975 bioactive effect Effects 0.000 claims description 9
- 230000009401 metastasis Effects 0.000 claims description 9
- 210000004881 tumor cell Anatomy 0.000 claims description 9
- 125000003295 alanine group Chemical group N[C@@H](C)C(=O)* 0.000 claims description 8
- 230000000903 blocking effect Effects 0.000 claims description 8
- 230000014508 negative regulation of coagulation Effects 0.000 claims description 8
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 claims description 7
- 230000004069 differentiation Effects 0.000 claims description 7
- 230000001404 mediated effect Effects 0.000 claims description 7
- 229920005615 natural polymer Polymers 0.000 claims description 7
- 239000003805 procoagulant Substances 0.000 claims description 7
- 230000008685 targeting Effects 0.000 claims description 7
- 230000029663 wound healing Effects 0.000 claims description 7
- 102000015340 serglycin Human genes 0.000 claims description 6
- 108010050065 serglycin Proteins 0.000 claims description 6
- 241000124008 Mammalia Species 0.000 claims 120
- DPXJVFZANSGRMM-UHFFFAOYSA-N acetic acid;2,3,4,5,6-pentahydroxyhexanal;sodium Chemical compound [Na].CC(O)=O.OCC(O)C(O)C(O)C(O)C=O DPXJVFZANSGRMM-UHFFFAOYSA-N 0.000 claims 6
- 238000001261 affinity purification Methods 0.000 claims 6
- 238000002513 implantation Methods 0.000 claims 6
- 229920001059 synthetic polymer Polymers 0.000 claims 6
- 241001529936 Murinae Species 0.000 claims 1
- 230000027455 binding Effects 0.000 description 169
- 235000018102 proteins Nutrition 0.000 description 44
- 102000004169 proteins and genes Human genes 0.000 description 44
- 108090000623 proteins and genes Proteins 0.000 description 44
- 229920002971 Heparan sulfate Polymers 0.000 description 37
- 230000003993 interaction Effects 0.000 description 25
- 229940118179 lovenox Drugs 0.000 description 24
- 108091035707 Consensus sequence Proteins 0.000 description 22
- 108090000190 Thrombin Proteins 0.000 description 17
- 229960004072 thrombin Drugs 0.000 description 16
- 229940088598 enzyme Drugs 0.000 description 15
- 108010074860 Factor Xa Proteins 0.000 description 13
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 12
- 150000002500 ions Chemical class 0.000 description 11
- 230000002792 vascular Effects 0.000 description 11
- QAOWNCQODCNURD-UHFFFAOYSA-L Sulfate Chemical compound [O-]S([O-])(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-L 0.000 description 10
- 230000009471 action Effects 0.000 description 10
- 238000004458 analytical method Methods 0.000 description 10
- 239000000499 gel Substances 0.000 description 10
- 108090000935 Antithrombin III Proteins 0.000 description 9
- 102000007327 Protamines Human genes 0.000 description 9
- 108010007568 Protamines Proteins 0.000 description 9
- 206010028980 Neoplasm Diseases 0.000 description 8
- 230000015572 biosynthetic process Effects 0.000 description 8
- 239000000969 carrier Substances 0.000 description 8
- 102000022382 heparin binding proteins Human genes 0.000 description 8
- 108091012216 heparin binding proteins Proteins 0.000 description 8
- 229940048914 protamine Drugs 0.000 description 8
- 241001465754 Metazoa Species 0.000 description 7
- 238000013459 approach Methods 0.000 description 7
- 210000004369 blood Anatomy 0.000 description 7
- 239000008280 blood Substances 0.000 description 7
- 239000003795 chemical substances by application Substances 0.000 description 7
- 239000000463 material Substances 0.000 description 7
- 239000000523 sample Substances 0.000 description 7
- 210000000329 smooth muscle myocyte Anatomy 0.000 description 7
- 239000000243 solution Substances 0.000 description 7
- 101710132601 Capsid protein Proteins 0.000 description 6
- 102000003974 Fibroblast growth factor 2 Human genes 0.000 description 6
- 108090000379 Fibroblast growth factor 2 Proteins 0.000 description 6
- 241000699666 Mus <mouse, genus> Species 0.000 description 6
- 239000002253 acid Substances 0.000 description 6
- 235000009697 arginine Nutrition 0.000 description 6
- 239000004202 carbamide Substances 0.000 description 6
- 230000015556 catabolic process Effects 0.000 description 6
- 230000010261 cell growth Effects 0.000 description 6
- 230000035602 clotting Effects 0.000 description 6
- 235000018417 cysteine Nutrition 0.000 description 6
- 239000003102 growth factor Substances 0.000 description 6
- 238000002347 injection Methods 0.000 description 6
- 239000007924 injection Substances 0.000 description 6
- 239000000203 mixture Substances 0.000 description 6
- 230000037361 pathway Effects 0.000 description 6
- 238000002360 preparation method Methods 0.000 description 6
- 238000001228 spectrum Methods 0.000 description 6
- 102000004411 Antithrombin III Human genes 0.000 description 5
- 206010053567 Coagulopathies Diseases 0.000 description 5
- 108010035532 Collagen Proteins 0.000 description 5
- 102000008186 Collagen Human genes 0.000 description 5
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 5
- 229960005348 antithrombin iii Drugs 0.000 description 5
- 238000003556 assay Methods 0.000 description 5
- 239000000872 buffer Substances 0.000 description 5
- 230000008859 change Effects 0.000 description 5
- 238000001142 circular dichroism spectrum Methods 0.000 description 5
- 229920001436 collagen Polymers 0.000 description 5
- 230000003511 endothelial effect Effects 0.000 description 5
- 210000004379 membrane Anatomy 0.000 description 5
- 239000012528 membrane Substances 0.000 description 5
- 229920000642 polymer Polymers 0.000 description 5
- 235000013930 proline Nutrition 0.000 description 5
- OVXIMRGEBNSORH-UHFFFAOYSA-N 2-[[2-[2-[[2-[[1-[1-[5-amino-2-[[2-amino-3-(1h-indol-3-yl)propanoyl]amino]-5-oxopentanoyl]pyrrolidine-2-carbonyl]pyrrolidine-2-carbonyl]amino]-5-(diaminomethylideneamino)pentanoyl]amino]propanoylamino]-5-(diaminomethylideneamino)pentanoyl]amino]-3-methylp Chemical compound CCC(C)C(C(O)=O)NC(=O)C(CCCN=C(N)N)NC(=O)C(C)NC(=O)C(CCCN=C(N)N)NC(=O)C1CCCN1C(=O)C1N(C(=O)C(CCC(N)=O)NC(=O)C(N)CC=2C3=CC=CC=C3NC=2)CCC1 OVXIMRGEBNSORH-UHFFFAOYSA-N 0.000 description 4
- 102100022977 Antithrombin-III Human genes 0.000 description 4
- 206010003210 Arteriosclerosis Diseases 0.000 description 4
- 239000004471 Glycine Substances 0.000 description 4
- IOVCWXUNBOPUCH-UHFFFAOYSA-N Nitrous acid Chemical compound ON=O IOVCWXUNBOPUCH-UHFFFAOYSA-N 0.000 description 4
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 4
- 208000007536 Thrombosis Diseases 0.000 description 4
- 230000010100 anticoagulation Effects 0.000 description 4
- 208000011775 arteriosclerosis disease Diseases 0.000 description 4
- 239000012867 bioactive agent Substances 0.000 description 4
- 230000024245 cell differentiation Effects 0.000 description 4
- 230000004663 cell proliferation Effects 0.000 description 4
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 4
- 201000010099 disease Diseases 0.000 description 4
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 4
- 230000002708 enhancing effect Effects 0.000 description 4
- 239000003112 inhibitor Substances 0.000 description 4
- 239000003055 low molecular weight heparin Substances 0.000 description 4
- 229940127215 low-molecular weight heparin Drugs 0.000 description 4
- 230000005012 migration Effects 0.000 description 4
- 238000013508 migration Methods 0.000 description 4
- 230000036961 partial effect Effects 0.000 description 4
- YBYRMVIVWMBXKQ-UHFFFAOYSA-N phenylmethanesulfonyl fluoride Chemical compound FS(=O)(=O)CC1=CC=CC=C1 YBYRMVIVWMBXKQ-UHFFFAOYSA-N 0.000 description 4
- 230000003389 potentiating effect Effects 0.000 description 4
- 125000001500 prolyl group Chemical class [H]N1C([H])(C(=O)[*])C([H])([H])C([H])([H])C1([H])[H] 0.000 description 4
- 230000002441 reversible effect Effects 0.000 description 4
- 150000003839 salts Chemical class 0.000 description 4
- 239000011780 sodium chloride Substances 0.000 description 4
- 150000003467 sulfuric acid derivatives Chemical class 0.000 description 4
- 238000003786 synthesis reaction Methods 0.000 description 4
- 230000004614 tumor growth Effects 0.000 description 4
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 4
- 102000004506 Blood Proteins Human genes 0.000 description 3
- 108010017384 Blood Proteins Proteins 0.000 description 3
- 102000012422 Collagen Type I Human genes 0.000 description 3
- 108010022452 Collagen Type I Proteins 0.000 description 3
- 102000008055 Heparan Sulfate Proteoglycans Human genes 0.000 description 3
- 241000282412 Homo Species 0.000 description 3
- 108090000054 Syndecan-2 Proteins 0.000 description 3
- 102100030951 Tissue factor pathway inhibitor Human genes 0.000 description 3
- 208000027418 Wounds and injury Diseases 0.000 description 3
- 210000003719 b-lymphocyte Anatomy 0.000 description 3
- 102000023732 binding proteins Human genes 0.000 description 3
- 108091008324 binding proteins Proteins 0.000 description 3
- 150000001720 carbohydrates Chemical class 0.000 description 3
- 101150087654 chrnd gene Proteins 0.000 description 3
- 230000015271 coagulation Effects 0.000 description 3
- 238000005345 coagulation Methods 0.000 description 3
- 238000006731 degradation reaction Methods 0.000 description 3
- 238000013461 design Methods 0.000 description 3
- 238000002474 experimental method Methods 0.000 description 3
- 125000000524 functional group Chemical group 0.000 description 3
- 230000036541 health Effects 0.000 description 3
- 230000002401 inhibitory effect Effects 0.000 description 3
- 230000005764 inhibitory process Effects 0.000 description 3
- 230000009545 invasion Effects 0.000 description 3
- 239000003446 ligand Substances 0.000 description 3
- 108010013555 lipoprotein-associated coagulation inhibitor Proteins 0.000 description 3
- 238000000302 molecular modelling Methods 0.000 description 3
- 238000006386 neutralization reaction Methods 0.000 description 3
- 230000001575 pathological effect Effects 0.000 description 3
- 230000012846 protein folding Effects 0.000 description 3
- 108020003175 receptors Proteins 0.000 description 3
- 230000009467 reduction Effects 0.000 description 3
- 230000000717 retained effect Effects 0.000 description 3
- 239000011734 sodium Substances 0.000 description 3
- 230000009885 systemic effect Effects 0.000 description 3
- 238000012360 testing method Methods 0.000 description 3
- 238000002560 therapeutic procedure Methods 0.000 description 3
- 208000019553 vascular disease Diseases 0.000 description 3
- BFSVOASYOCHEOV-UHFFFAOYSA-N 2-diethylaminoethanol Chemical compound CCN(CC)CCO BFSVOASYOCHEOV-UHFFFAOYSA-N 0.000 description 2
- TVZRAEYQIKYCPH-UHFFFAOYSA-N 3-(trimethylsilyl)propane-1-sulfonic acid Chemical compound C[Si](C)(C)CCCS(O)(=O)=O TVZRAEYQIKYCPH-UHFFFAOYSA-N 0.000 description 2
- SLXKOJJOQWFEFD-UHFFFAOYSA-N 6-aminohexanoic acid Chemical compound NCCCCCC(O)=O SLXKOJJOQWFEFD-UHFFFAOYSA-N 0.000 description 2
- 229920000936 Agarose Polymers 0.000 description 2
- 241000894006 Bacteria Species 0.000 description 2
- 108010023736 Chondroitinases and Chondroitin Lyases Proteins 0.000 description 2
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 2
- 101150021185 FGF gene Proteins 0.000 description 2
- 102000007547 Laminin Human genes 0.000 description 2
- 108010085895 Laminin Proteins 0.000 description 2
- 108010013563 Lipoprotein Lipase Proteins 0.000 description 2
- 102100022119 Lipoprotein lipase Human genes 0.000 description 2
- 241000357437 Mola Species 0.000 description 2
- 102100031688 N-acetylgalactosamine-6-sulfatase Human genes 0.000 description 2
- 238000005481 NMR spectroscopy Methods 0.000 description 2
- 241000700159 Rattus Species 0.000 description 2
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 2
- 102100035140 Vitronectin Human genes 0.000 description 2
- 108010031318 Vitronectin Proteins 0.000 description 2
- 206010052428 Wound Diseases 0.000 description 2
- 230000002378 acidificating effect Effects 0.000 description 2
- 150000007513 acids Chemical class 0.000 description 2
- 230000033115 angiogenesis Effects 0.000 description 2
- 230000001858 anti-Xa Effects 0.000 description 2
- 230000002668 anti-heparin effect Effects 0.000 description 2
- 230000002785 anti-thrombosis Effects 0.000 description 2
- 210000001367 artery Anatomy 0.000 description 2
- 210000002469 basement membrane Anatomy 0.000 description 2
- 239000011230 binding agent Substances 0.000 description 2
- 210000004204 blood vessel Anatomy 0.000 description 2
- 210000004899 c-terminal region Anatomy 0.000 description 2
- 235000014633 carbohydrates Nutrition 0.000 description 2
- 238000002144 chemical decomposition reaction Methods 0.000 description 2
- 238000006243 chemical reaction Methods 0.000 description 2
- 210000001612 chondrocyte Anatomy 0.000 description 2
- 238000000978 circular dichroism spectroscopy Methods 0.000 description 2
- 150000001945 cysteines Chemical class 0.000 description 2
- 230000003247 decreasing effect Effects 0.000 description 2
- 238000001212 derivatisation Methods 0.000 description 2
- 230000029087 digestion Effects 0.000 description 2
- 238000009826 distribution Methods 0.000 description 2
- 230000007515 enzymatic degradation Effects 0.000 description 2
- 239000000284 extract Substances 0.000 description 2
- 239000012091 fetal bovine serum Substances 0.000 description 2
- 230000020764 fibrinolysis Effects 0.000 description 2
- 239000012634 fragment Substances 0.000 description 2
- 239000001963 growth medium Substances 0.000 description 2
- 230000035876 healing Effects 0.000 description 2
- 108010021105 heparatinase I Proteins 0.000 description 2
- 238000011534 incubation Methods 0.000 description 2
- 230000008595 infiltration Effects 0.000 description 2
- 238000001764 infiltration Methods 0.000 description 2
- 238000005259 measurement Methods 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 210000000663 muscle cell Anatomy 0.000 description 2
- 229930014626 natural product Natural products 0.000 description 2
- 230000007935 neutral effect Effects 0.000 description 2
- 230000003472 neutralizing effect Effects 0.000 description 2
- 238000010899 nucleation Methods 0.000 description 2
- 210000000056 organ Anatomy 0.000 description 2
- 230000000399 orthopedic effect Effects 0.000 description 2
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 2
- 230000035755 proliferation Effects 0.000 description 2
- 238000000746 purification Methods 0.000 description 2
- 238000011160 research Methods 0.000 description 2
- 208000037803 restenosis Diseases 0.000 description 2
- 108010004093 retinal S antigen peptide M Proteins 0.000 description 2
- 239000012146 running buffer Substances 0.000 description 2
- 239000001632 sodium acetate Substances 0.000 description 2
- 235000017281 sodium acetate Nutrition 0.000 description 2
- 239000001509 sodium citrate Substances 0.000 description 2
- NLJMYIDDQXHKNR-UHFFFAOYSA-K sodium citrate Chemical compound O.O.[Na+].[Na+].[Na+].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O NLJMYIDDQXHKNR-UHFFFAOYSA-K 0.000 description 2
- 239000002904 solvent Substances 0.000 description 2
- 241000894007 species Species 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- 230000004083 survival effect Effects 0.000 description 2
- 230000000699 topical effect Effects 0.000 description 2
- DZGWFCGJZKJUFP-UHFFFAOYSA-N tyramine Chemical compound NCCC1=CC=C(O)C=C1 DZGWFCGJZKJUFP-UHFFFAOYSA-N 0.000 description 2
- -1 vitranectin Proteins 0.000 description 2
- GCSZJMUFYOAHFY-SDQBBNPISA-N (1z)-1-(3-ethyl-5-hydroxy-1,3-benzothiazol-2-ylidene)propan-2-one Chemical compound C1=C(O)C=C2N(CC)\C(=C\C(C)=O)SC2=C1 GCSZJMUFYOAHFY-SDQBBNPISA-N 0.000 description 1
- 125000003088 (fluoren-9-ylmethoxy)carbonyl group Chemical group 0.000 description 1
- MSWZFWKMSRAUBD-IVMDWMLBSA-N 2-amino-2-deoxy-D-glucopyranose Chemical compound N[C@H]1C(O)O[C@H](CO)[C@@H](O)[C@@H]1O MSWZFWKMSRAUBD-IVMDWMLBSA-N 0.000 description 1
- NUFBIAUZAMHTSP-UHFFFAOYSA-N 3-(n-morpholino)-2-hydroxypropanesulfonic acid Chemical compound OS(=O)(=O)CC(O)CN1CCOCC1 NUFBIAUZAMHTSP-UHFFFAOYSA-N 0.000 description 1
- UMCMPZBLKLEWAF-BCTGSCMUSA-N 3-[(3-cholamidopropyl)dimethylammonio]propane-1-sulfonate Chemical compound C([C@H]1C[C@H]2O)[C@H](O)CC[C@]1(C)[C@@H]1[C@@H]2[C@@H]2CC[C@H]([C@@H](CCC(=O)NCCC[N+](C)(C)CCCS([O-])(=O)=O)C)[C@@]2(C)[C@@H](O)C1 UMCMPZBLKLEWAF-BCTGSCMUSA-N 0.000 description 1
- SQDAZGGFXASXDW-UHFFFAOYSA-N 5-bromo-2-(trifluoromethoxy)pyridine Chemical compound FC(F)(F)OC1=CC=C(Br)C=N1 SQDAZGGFXASXDW-UHFFFAOYSA-N 0.000 description 1
- 241000251468 Actinopterygii Species 0.000 description 1
- 206010067484 Adverse reaction Diseases 0.000 description 1
- 241000935968 Alania Species 0.000 description 1
- 101100133992 Amycolatopsis sp Aaar gene Proteins 0.000 description 1
- 241000415078 Anemone hepatica Species 0.000 description 1
- 241001233887 Ania Species 0.000 description 1
- 102000006991 Apolipoprotein B-100 Human genes 0.000 description 1
- 108010008150 Apolipoprotein B-100 Proteins 0.000 description 1
- 108010071619 Apolipoproteins Proteins 0.000 description 1
- 102000007592 Apolipoproteins Human genes 0.000 description 1
- 101100207331 Arabidopsis thaliana TPPI gene Proteins 0.000 description 1
- 241000531806 Aramus guarauna Species 0.000 description 1
- 241000370685 Arge Species 0.000 description 1
- 241001133287 Artocarpus hirsutus Species 0.000 description 1
- 201000001320 Atherosclerosis Diseases 0.000 description 1
- 102100036597 Basement membrane-specific heparan sulfate proteoglycan core protein Human genes 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- 101150050114 CTL1 gene Proteins 0.000 description 1
- 241000282472 Canis lupus familiaris Species 0.000 description 1
- 241000282994 Cervidae Species 0.000 description 1
- 229920002567 Chondroitin Polymers 0.000 description 1
- 229920001287 Chondroitin sulfate Polymers 0.000 description 1
- 102000002734 Collagen Type VI Human genes 0.000 description 1
- 108010043741 Collagen Type VI Proteins 0.000 description 1
- 206010009944 Colon cancer Diseases 0.000 description 1
- 241001137251 Corvidae Species 0.000 description 1
- 241000699802 Cricetulus griseus Species 0.000 description 1
- 229920004934 Dacron® Polymers 0.000 description 1
- 206010011878 Deafness Diseases 0.000 description 1
- 241000922654 Deparia Species 0.000 description 1
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 1
- 230000010777 Disulfide Reduction Effects 0.000 description 1
- 101100285518 Drosophila melanogaster how gene Proteins 0.000 description 1
- 101710083262 Ectin Proteins 0.000 description 1
- 102400001047 Endostatin Human genes 0.000 description 1
- 108010079505 Endostatins Proteins 0.000 description 1
- 102000010834 Extracellular Matrix Proteins Human genes 0.000 description 1
- 108010037362 Extracellular Matrix Proteins Proteins 0.000 description 1
- 244000034902 Fevillea cordifolia Species 0.000 description 1
- 235000004863 Fevillea cordifolia Nutrition 0.000 description 1
- 102000018233 Fibroblast Growth Factor Human genes 0.000 description 1
- 108050007372 Fibroblast Growth Factor Proteins 0.000 description 1
- 102000003971 Fibroblast Growth Factor 1 Human genes 0.000 description 1
- 108090000386 Fibroblast Growth Factor 1 Proteins 0.000 description 1
- KRHYYFGTRYWZRS-UHFFFAOYSA-M Fluoride anion Chemical compound [F-] KRHYYFGTRYWZRS-UHFFFAOYSA-M 0.000 description 1
- 241001123946 Gaga Species 0.000 description 1
- 244000287680 Garcinia dulcis Species 0.000 description 1
- 208000032843 Hemorrhage Diseases 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 102000004157 Hydrolases Human genes 0.000 description 1
- 108090000604 Hydrolases Proteins 0.000 description 1
- 241000257303 Hymenoptera Species 0.000 description 1
- DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 1
- 206010021703 Indifference Diseases 0.000 description 1
- 102000004856 Lectins Human genes 0.000 description 1
- 102000004882 Lipase Human genes 0.000 description 1
- 108090001060 Lipase Proteins 0.000 description 1
- 239000004367 Lipase Substances 0.000 description 1
- DIWRORZWFLOCLC-UHFFFAOYSA-N Lorazepam Chemical compound C12=CC(Cl)=CC=C2NC(=O)C(O)N=C1C1=CC=CC=C1Cl DIWRORZWFLOCLC-UHFFFAOYSA-N 0.000 description 1
- 241000699660 Mus musculus Species 0.000 description 1
- 101100166829 Mus musculus Cenpk gene Proteins 0.000 description 1
- 101100246029 Mus musculus Ptpn2 gene Proteins 0.000 description 1
- BKAYIFDRRZZKNF-VIFPVBQESA-N N-acetylcarnosine Chemical compound CC(=O)NCCC(=O)N[C@H](C(O)=O)CC1=CN=CN1 BKAYIFDRRZZKNF-VIFPVBQESA-N 0.000 description 1
- 102400000108 N-terminal peptide Human genes 0.000 description 1
- 101800000597 N-terminal peptide Proteins 0.000 description 1
- 238000012565 NMR experiment Methods 0.000 description 1
- 241000906034 Orthops Species 0.000 description 1
- 108091081548 Palindromic sequence Proteins 0.000 description 1
- 235000014676 Phragmites communis Nutrition 0.000 description 1
- 102000004211 Platelet factor 4 Human genes 0.000 description 1
- 108090000778 Platelet factor 4 Proteins 0.000 description 1
- 101710093543 Probable non-specific lipid-transfer protein Proteins 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- 241000271574 Rheiformes Species 0.000 description 1
- 241000283984 Rodentia Species 0.000 description 1
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 1
- 241000270295 Serpentes Species 0.000 description 1
- XUIMIQQOPSSXEZ-UHFFFAOYSA-N Silicon Chemical compound [Si] XUIMIQQOPSSXEZ-UHFFFAOYSA-N 0.000 description 1
- 206010041235 Snoring Diseases 0.000 description 1
- 229930006000 Sucrose Natural products 0.000 description 1
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 1
- 102000019361 Syndecan Human genes 0.000 description 1
- 108050006774 Syndecan Proteins 0.000 description 1
- 102100035721 Syndecan-1 Human genes 0.000 description 1
- 108090000058 Syndecan-1 Proteins 0.000 description 1
- 210000001744 T-lymphocyte Anatomy 0.000 description 1
- 102000002938 Thrombospondin Human genes 0.000 description 1
- 108060008245 Thrombospondin Proteins 0.000 description 1
- ATJFFYVFTNAWJD-UHFFFAOYSA-N Tin Chemical compound [Sn] ATJFFYVFTNAWJD-UHFFFAOYSA-N 0.000 description 1
- 206010060872 Transplant failure Diseases 0.000 description 1
- 229920004890 Triton X-100 Polymers 0.000 description 1
- 239000013504 Triton X-100 Substances 0.000 description 1
- 238000010306 acid treatment Methods 0.000 description 1
- 230000003213 activating effect Effects 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 230000006838 adverse reaction Effects 0.000 description 1
- 239000011543 agarose gel Substances 0.000 description 1
- 230000004931 aggregating effect Effects 0.000 description 1
- 230000002776 aggregation Effects 0.000 description 1
- 238000004220 aggregation Methods 0.000 description 1
- 150000001298 alcohols Chemical class 0.000 description 1
- 229910052783 alkali metal Inorganic materials 0.000 description 1
- 230000004075 alteration Effects 0.000 description 1
- 150000001412 amines Chemical class 0.000 description 1
- 125000000539 amino acid group Chemical group 0.000 description 1
- 229960002684 aminocaproic acid Drugs 0.000 description 1
- APKFDSVGJQXUKY-INPOYWNPSA-N amphotericin B Chemical compound O[C@H]1[C@@H](N)[C@H](O)[C@@H](C)O[C@H]1O[C@H]1/C=C/C=C/C=C/C=C/C=C/C=C/C=C/[C@H](C)[C@@H](O)[C@@H](C)[C@H](C)OC(=O)C[C@H](O)C[C@H](O)CC[C@@H](O)[C@H](O)C[C@H](O)C[C@](O)(C[C@H](O)[C@H]2C(O)=O)O[C@H]2C1 APKFDSVGJQXUKY-INPOYWNPSA-N 0.000 description 1
- 230000001028 anti-proliverative effect Effects 0.000 description 1
- 239000000729 antidote Substances 0.000 description 1
- 239000004019 antithrombin Substances 0.000 description 1
- 150000001484 arginines Chemical class 0.000 description 1
- 238000003491 array Methods 0.000 description 1
- 230000002917 arthritic effect Effects 0.000 description 1
- 230000004888 barrier function Effects 0.000 description 1
- 230000006399 behavior Effects 0.000 description 1
- PXXJHWLDUBFPOL-UHFFFAOYSA-N benzamidine Chemical compound NC(=N)C1=CC=CC=C1 PXXJHWLDUBFPOL-UHFFFAOYSA-N 0.000 description 1
- MSWZFWKMSRAUBD-UHFFFAOYSA-N beta-D-galactosamine Natural products NC1C(O)OC(CO)C(O)C1O MSWZFWKMSRAUBD-UHFFFAOYSA-N 0.000 description 1
- 210000000601 blood cell Anatomy 0.000 description 1
- 230000017531 blood circulation Effects 0.000 description 1
- 239000011575 calcium Substances 0.000 description 1
- VSGNNIFQASZAOI-UHFFFAOYSA-L calcium acetate Chemical compound [Ca+2].CC([O-])=O.CC([O-])=O VSGNNIFQASZAOI-UHFFFAOYSA-L 0.000 description 1
- 239000001639 calcium acetate Substances 0.000 description 1
- 229960005147 calcium acetate Drugs 0.000 description 1
- 235000011092 calcium acetate Nutrition 0.000 description 1
- 230000022159 cartilage development Effects 0.000 description 1
- 230000021164 cell adhesion Effects 0.000 description 1
- 230000004700 cellular uptake Effects 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- DLGJWSVWTWEWBJ-HGGSSLSASA-N chondroitin Chemical compound CC(O)=N[C@@H]1[C@H](O)O[C@H](CO)[C@H](O)[C@@H]1OC1[C@H](O)[C@H](O)C=C(C(O)=O)O1 DLGJWSVWTWEWBJ-HGGSSLSASA-N 0.000 description 1
- 229940059329 chondroitin sulfate Drugs 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- GKTWGGQPFAXNFI-HNNXBMFYSA-N clopidogrel Chemical compound C1([C@H](N2CC=3C=CSC=3CC2)C(=O)OC)=CC=CC=C1Cl GKTWGGQPFAXNFI-HNNXBMFYSA-N 0.000 description 1
- 239000011248 coating agent Substances 0.000 description 1
- 238000000576 coating method Methods 0.000 description 1
- 239000012141 concentrate Substances 0.000 description 1
- 230000009146 cooperative binding Effects 0.000 description 1
- 238000004132 cross linking Methods 0.000 description 1
- 210000000805 cytoplasm Anatomy 0.000 description 1
- 230000006378 damage Effects 0.000 description 1
- 230000007547 defect Effects 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- JXSJBGJIGXNWCI-UHFFFAOYSA-N diethyl 2-[(dimethoxyphosphorothioyl)thio]succinate Chemical compound CCOC(=O)CC(SP(=S)(OC)OC)C(=O)OCC JXSJBGJIGXNWCI-UHFFFAOYSA-N 0.000 description 1
- RCKMWOKWVGPNJF-UHFFFAOYSA-N diethylcarbamazine Chemical compound CCN(CC)C(=O)N1CCN(C)CC1 RCKMWOKWVGPNJF-UHFFFAOYSA-N 0.000 description 1
- 238000009792 diffusion process Methods 0.000 description 1
- 239000003085 diluting agent Substances 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- 238000006471 dimerization reaction Methods 0.000 description 1
- 230000003292 diminished effect Effects 0.000 description 1
- 229940042399 direct acting antivirals protease inhibitors Drugs 0.000 description 1
- 238000006073 displacement reaction Methods 0.000 description 1
- 239000012153 distilled water Substances 0.000 description 1
- JOSBTZULDGZZRE-UHFFFAOYSA-N elanine Natural products CCC(C)C(=O)OC1C2CC3C1C(O)(CC2OC)C4(O)C(OC)C5C6(COC(=O)c7ccccc7N8C(=O)CC(C)C8=O)CCC(OC)C35C4N(CC)C6 JOSBTZULDGZZRE-UHFFFAOYSA-N 0.000 description 1
- 229940082150 encore Drugs 0.000 description 1
- 210000003743 erythrocyte Anatomy 0.000 description 1
- 150000002170 ethers Chemical class 0.000 description 1
- 239000013604 expression vector Substances 0.000 description 1
- 210000002744 extracellular matrix Anatomy 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 230000002349 favourable effect Effects 0.000 description 1
- 210000003191 femoral vein Anatomy 0.000 description 1
- 230000035557 fibrillogenesis Effects 0.000 description 1
- 210000002950 fibroblast Anatomy 0.000 description 1
- 230000003328 fibroblastic effect Effects 0.000 description 1
- 239000000945 filler Substances 0.000 description 1
- 235000019688 fish Nutrition 0.000 description 1
- 238000009472 formulation Methods 0.000 description 1
- 239000007789 gas Substances 0.000 description 1
- 229960002442 glucosamine Drugs 0.000 description 1
- 150000004676 glycans Chemical class 0.000 description 1
- 238000003306 harvesting Methods 0.000 description 1
- 238000010438 heat treatment Methods 0.000 description 1
- 230000023597 hemostasis Effects 0.000 description 1
- 239000002634 heparin fragment Substances 0.000 description 1
- 108010083213 heparitinsulfate lyase Proteins 0.000 description 1
- 230000002440 hepatic effect Effects 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- 239000012145 high-salt buffer Substances 0.000 description 1
- 210000003630 histaminocyte Anatomy 0.000 description 1
- 210000005260 human cell Anatomy 0.000 description 1
- 229910052739 hydrogen Inorganic materials 0.000 description 1
- 239000001257 hydrogen Substances 0.000 description 1
- 206010020718 hyperplasia Diseases 0.000 description 1
- 230000028993 immune response Effects 0.000 description 1
- 230000002779 inactivation Effects 0.000 description 1
- 238000013383 initial experiment Methods 0.000 description 1
- 208000014674 injury Diseases 0.000 description 1
- 239000002198 insoluble material Substances 0.000 description 1
- 230000000968 intestinal effect Effects 0.000 description 1
- 210000004347 intestinal mucosa Anatomy 0.000 description 1
- 210000004731 jugular vein Anatomy 0.000 description 1
- 235000019421 lipase Nutrition 0.000 description 1
- 230000007774 longterm Effects 0.000 description 1
- 210000004072 lung Anatomy 0.000 description 1
- 230000003211 malignant effect Effects 0.000 description 1
- 210000004962 mammalian cell Anatomy 0.000 description 1
- 238000004949 mass spectrometry Methods 0.000 description 1
- 239000011159 matrix material Substances 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 239000002609 medium Substances 0.000 description 1
- 201000001441 melanoma Diseases 0.000 description 1
- 230000004060 metabolic process Effects 0.000 description 1
- 230000003278 mimic effect Effects 0.000 description 1
- 150000007522 mineralic acids Chemical class 0.000 description 1
- 238000003032 molecular docking Methods 0.000 description 1
- 238000000329 molecular dynamics simulation Methods 0.000 description 1
- 238000011580 nude mouse model Methods 0.000 description 1
- 210000001672 ovary Anatomy 0.000 description 1
- 230000009589 pathological growth Effects 0.000 description 1
- 230000007170 pathology Effects 0.000 description 1
- 108010091212 pepstatin Proteins 0.000 description 1
- FAXGPCHRFPCXOO-LXTPJMTPSA-N pepstatin A Chemical compound OC(=O)C[C@H](O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)C[C@H](O)[C@H](CC(C)C)NC(=O)[C@H](C(C)C)NC(=O)[C@H](C(C)C)NC(=O)CC(C)C FAXGPCHRFPCXOO-LXTPJMTPSA-N 0.000 description 1
- 239000000137 peptide hydrolase inhibitor Substances 0.000 description 1
- 108010049224 perlecan Proteins 0.000 description 1
- 238000002823 phage display Methods 0.000 description 1
- 235000015108 pies Nutrition 0.000 description 1
- 239000006187 pill Substances 0.000 description 1
- 235000021018 plums Nutrition 0.000 description 1
- 231100000614 poison Toxicity 0.000 description 1
- 230000007096 poisonous effect Effects 0.000 description 1
- 229920000724 poly(L-arginine) polymer Polymers 0.000 description 1
- 229920000729 poly(L-lysine) polymer Polymers 0.000 description 1
- 229920001223 polyethylene glycol Polymers 0.000 description 1
- 239000005020 polyethylene terephthalate Substances 0.000 description 1
- 229920001184 polypeptide Polymers 0.000 description 1
- 239000013641 positive control Substances 0.000 description 1
- MFDFERRIHVXMIY-UHFFFAOYSA-N procaine Chemical compound CCN(CC)CCOC(=O)C1=CC=C(N)C=C1 MFDFERRIHVXMIY-UHFFFAOYSA-N 0.000 description 1
- 229960004919 procaine Drugs 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 229940070353 protamines Drugs 0.000 description 1
- 230000017854 proteolysis Effects 0.000 description 1
- 230000002685 pulmonary effect Effects 0.000 description 1
- 238000000163 radioactive labelling Methods 0.000 description 1
- 230000002829 reductive effect Effects 0.000 description 1
- 230000008458 response to injury Effects 0.000 description 1
- 238000012552 review Methods 0.000 description 1
- 239000004576 sand Substances 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 108010080511 serum sodium transport inhibitor Proteins 0.000 description 1
- 229910052710 silicon Inorganic materials 0.000 description 1
- 239000010703 silicon Substances 0.000 description 1
- 239000002893 slag Substances 0.000 description 1
- 101150052401 slc44a1 gene Proteins 0.000 description 1
- 229910052708 sodium Inorganic materials 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 230000009870 specific binding Effects 0.000 description 1
- 230000000087 stabilizing effect Effects 0.000 description 1
- 229960005322 streptomycin Drugs 0.000 description 1
- 238000007920 subcutaneous administration Methods 0.000 description 1
- 238000006467 substitution reaction Methods 0.000 description 1
- 239000005720 sucrose Substances 0.000 description 1
- 238000005670 sulfation reaction Methods 0.000 description 1
- 150000003460 sulfonic acids Chemical class 0.000 description 1
- 238000001356 surgical procedure Methods 0.000 description 1
- 238000004114 suspension culture Methods 0.000 description 1
- 230000001225 therapeutic effect Effects 0.000 description 1
- 230000001732 thrombotic effect Effects 0.000 description 1
- 238000004324 time-proportional phase incrementation Methods 0.000 description 1
- 239000002407 tissue scaffold Substances 0.000 description 1
- 238000012582 total correlation spectroscopy experiment Methods 0.000 description 1
- 231100000331 toxic Toxicity 0.000 description 1
- 230000002588 toxic effect Effects 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 238000002054 transplantation Methods 0.000 description 1
- 229960003732 tyramine Drugs 0.000 description 1
- 210000003606 umbilical vein Anatomy 0.000 description 1
- 210000003556 vascular endothelial cell Anatomy 0.000 description 1
- 231100000216 vascular lesion Toxicity 0.000 description 1
- 239000002435 venom Substances 0.000 description 1
- 231100000611 venom Toxicity 0.000 description 1
- 210000001048 venom Anatomy 0.000 description 1
- 108010047303 von Willebrand Factor Proteins 0.000 description 1
- 102100036537 von Willebrand factor Human genes 0.000 description 1
- 229960001134 von willebrand factor Drugs 0.000 description 1
- 238000002424 x-ray crystallography Methods 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K7/00—Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
- C07K7/04—Linear peptides containing only normal peptide links
- C07K7/08—Linear peptides containing only normal peptide links having 12 to 20 amino acids
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/001—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof by chemical synthesis
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
Landscapes
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Health & Medical Sciences (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Life Sciences & Earth Sciences (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Gastroenterology & Hepatology (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
Abstract
L'invention concerne des peptides de différentes séquences et tailles, et des techniques d'utilisation de ces peptides qui présentent une forte affinité pour les glycosaminoglycanes et les protéoglycanes, ces peptides réagissant fortement avec l'héparine, et d'autres glycosaminoglycanes, ou protéoglycanes (PG).
Applications Claiming Priority (3)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
US11827699P | 1999-02-02 | 1999-02-02 | |
US60/118,276 | 1999-02-02 | ||
PCT/US2000/002853 WO2000045831A1 (fr) | 1999-02-02 | 2000-02-02 | Activites de modulation des peptides de l'heparine, et d'autres glycosaminoglycanes ou proteoglycanes |
Publications (1)
Publication Number | Publication Date |
---|---|
CA2361612A1 true CA2361612A1 (fr) | 2000-08-10 |
Family
ID=22377591
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
CA002361612A Abandoned CA2361612A1 (fr) | 1999-02-02 | 2000-02-02 | Activites de modulation des peptides de l'heparine, et d'autres glycosaminoglycanes ou proteoglycanes |
Country Status (3)
Country | Link |
---|---|
EP (1) | EP1156816A4 (fr) |
CA (1) | CA2361612A1 (fr) |
WO (1) | WO2000045831A1 (fr) |
Families Citing this family (21)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US8003595B2 (en) | 2000-03-01 | 2011-08-23 | Cellectis | Amino acid sequences facilitating penetration of a substance of interest into cells and/or cell nuclei |
US20040097586A1 (en) * | 2001-01-30 | 2004-05-20 | Andre Trouet | Anti-tumor compounds |
US7049286B2 (en) | 2001-08-30 | 2006-05-23 | Diatos, S.A. | Insulin conjugates and methods of use thereof |
WO2003054146A2 (fr) | 2001-11-14 | 2003-07-03 | Northwestern University | Auto-assemblage et mineralisation de nanofibres de peptide amphiphile |
US7371719B2 (en) | 2002-02-15 | 2008-05-13 | Northwestern University | Self-assembly of peptide-amphiphile nanofibers under physiological conditions |
WO2004018628A2 (fr) | 2002-08-21 | 2004-03-04 | Northwestern University | Solutions chargees de peptides amphiphiles, et reseaux auto-assembles de nanofibres de peptides en etant faits |
US7554021B2 (en) | 2002-11-12 | 2009-06-30 | Northwestern University | Composition and method for self-assembly and mineralization of peptide amphiphiles |
WO2004046167A2 (fr) | 2002-11-14 | 2004-06-03 | Northwestern University | Synthese et auto-ssemblage du peptide bola tribloc abc |
IL153762A0 (en) * | 2002-12-31 | 2003-07-06 | Rimonyx Pharmaceuticals Ltd | Methods of screening for anti-inflammatory drugs and use thereof |
WO2005014619A2 (fr) | 2003-03-28 | 2005-02-17 | Thomas Jefferson University | Peptides de liaison a l'heparine et leur utilisation |
WO2005018650A2 (fr) | 2003-08-14 | 2005-03-03 | Diatos | Composition anti-bacterienne plus particulierement contre les bacteries gram negatif comprenent un peptide et un agent anti-bacterien avantageusement hydrophobe |
NZ547671A (en) | 2003-12-05 | 2009-10-30 | Univ Northwestern | Self-assembling peptide amphiphiles and related methods for growth factor delivery |
CN1905893A (zh) | 2003-12-05 | 2007-01-31 | 西北大学 | 分支的肽两亲物、相关的表位组合物和其自组装的结构 |
EP1853917A4 (fr) * | 2005-03-04 | 2008-09-10 | Univ Northwestern | Epitopes angiogéniques de liaison a l'héparine, amphiphiles peptidiques, compositions auto-assemblées et procédés d'utilisation associés |
EP1797901A1 (fr) | 2005-12-16 | 2007-06-20 | Diatos | Conjugués peptidiques pénétrant dans les cellules en tant que vecteurs pour l'administration d'acides nucléiques |
EP1818395A1 (fr) | 2006-02-08 | 2007-08-15 | Diatos | Compositions et méthodes pour le traitement de maladies lysosomales |
KR101394768B1 (ko) | 2006-03-30 | 2014-05-21 | 드라이스 파마슈티컬스 아이엔씨 | 캄토테신-세포 투과 펩티드 결합체 및 이를 포함하는 약학 조성물 |
US8076295B2 (en) | 2007-04-17 | 2011-12-13 | Nanotope, Inc. | Peptide amphiphiles having improved solubility and methods of using same |
US8450271B2 (en) | 2009-04-13 | 2013-05-28 | Northwestern University | Peptide-based scaffolds for cartilage regeneration and methods for their use |
US10222410B2 (en) * | 2013-02-12 | 2019-03-05 | Headsight, Inc. | Diagnostic system for a controller |
WO2024261742A1 (fr) | 2023-06-21 | 2024-12-26 | Nano Ghost Ltd | Compositions comprenant des médicaments insolubles dans l'eau et leurs procédés de production et d'utilisation |
Family Cites Families (3)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US5770563A (en) * | 1991-12-06 | 1998-06-23 | The United States Of America As Represented By The Department Of Health And Human Services | Heparin- and sulfatide binding peptides from the type I repeats of human thrombospondin and conjugates thereof |
US5614494A (en) * | 1993-11-12 | 1997-03-25 | University Of Michigan, The Board Of Regents Acting For And On Behalf Of | Peptides for heparin and low molecular weight heparin anticoagulation reversal |
US5877153A (en) * | 1996-06-11 | 1999-03-02 | Commonwealth Biotechnologies Inc. | Heparin-binding peptides |
-
2000
- 2000-02-02 CA CA002361612A patent/CA2361612A1/fr not_active Abandoned
- 2000-02-02 EP EP00905964A patent/EP1156816A4/fr not_active Withdrawn
- 2000-02-02 WO PCT/US2000/002853 patent/WO2000045831A1/fr not_active Application Discontinuation
Also Published As
Publication number | Publication date |
---|---|
EP1156816A4 (fr) | 2004-12-29 |
EP1156816A1 (fr) | 2001-11-28 |
WO2000045831A1 (fr) | 2000-08-10 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
CA2361612A1 (fr) | Activites de modulation des peptides de l'heparine, et d'autres glycosaminoglycanes ou proteoglycanes | |
US6319897B1 (en) | Peptides which inhibit complement activation | |
Brown et al. | Histidine-rich glycoprotein and platelet factor 4 mask heparan sulfate proteoglycans recognized by acidic and basic fibroblast growth factor | |
US5654273A (en) | Synducin mediated modulation of tissue repair | |
ES2259816T3 (es) | Codificacion polinucleotida de un polipeptido con actividad heparanasa y expresion del mismo en celulas transducidas. | |
EP2877248B1 (fr) | Variants de hmgb1 et leurs utilisations | |
EP0333356A2 (fr) | Peptides de hirudine | |
Sahni et al. | Fibrinogen and fibrin protect fibroblast growth factor-2 from proteolytic degradation | |
McLane et al. | Disintegrins in health and disease | |
JP2004043507A (ja) | 細胞外マトリックスの蓄積を防止するためのトランスフォーミング増殖因子βの阻害 | |
JPH06510989A (ja) | 組織形成因子誘導による炎症反応の調節 | |
JP2011121956A (ja) | ヘパリン様化合物、その製造並びに血管傷害および介入に伴う動脈血栓を阻止するための使用 | |
EP0278781B1 (fr) | Peptides à activité de laminine | |
EP0372670A2 (fr) | Peptides analogues de l'hirudine pour l'empêchement de l'agrégation des thrombocytes | |
US6855801B1 (en) | Peptides modulating activities of heparin other glycosaminoglycans or proteoglycans | |
Bittner et al. | Modulation of collagen gel contraction by decorin | |
US5618917A (en) | Methods and compositions for detecting and treating kidney diseases associated with adhesion of crystals to kidney cells | |
CZ20012916A3 (cs) | Farmaceutický prostředek | |
CA2227972A1 (fr) | Une protease du venin du cobra, la mocarhagine, et ses utilisations therapeutiques | |
JP2002512018A (ja) | マトリックス結合因子 | |
US20060252692A1 (en) | Inhibitors for use in hemostasis | |
US8106002B2 (en) | Anti-cancer agent comprising protein C inhibitor | |
JP2003530841A (ja) | 治療的化合物および方法 | |
US20080293628A1 (en) | Methods and Compositions for the Inhibition of Thrombus Formation | |
TW200529870A (en) | Therapeutic use of factor XI |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
FZDE | Discontinued |