AU728480B2 - Self-aligning peptides derived from elastin and other fibrous proteins - Google Patents
Self-aligning peptides derived from elastin and other fibrous proteins Download PDFInfo
- Publication number
- AU728480B2 AU728480B2 AU38438/97A AU3843897A AU728480B2 AU 728480 B2 AU728480 B2 AU 728480B2 AU 38438/97 A AU38438/97 A AU 38438/97A AU 3843897 A AU3843897 A AU 3843897A AU 728480 B2 AU728480 B2 AU 728480B2
- Authority
- AU
- Australia
- Prior art keywords
- polypeptide
- amino acid
- beta
- elastin
- acid sequence
- 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.)
- Ceased
Links
- 108090000765 processed proteins & peptides Proteins 0.000 title claims description 145
- 102000004196 processed proteins & peptides Human genes 0.000 title claims description 132
- 108010014258 Elastin Proteins 0.000 title claims description 101
- 102000016942 Elastin Human genes 0.000 title claims description 86
- 229920002549 elastin Polymers 0.000 title claims description 81
- 102000034240 fibrous proteins Human genes 0.000 title claims description 24
- 108091005899 fibrous proteins Proteins 0.000 title claims description 24
- 229920001184 polypeptide Polymers 0.000 claims description 114
- 239000000463 material Substances 0.000 claims description 91
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 54
- 108090000623 proteins and genes Proteins 0.000 claims description 48
- 102000004169 proteins and genes Human genes 0.000 claims description 48
- 125000000539 amino acid group Chemical group 0.000 claims description 46
- 241001465754 Metazoa Species 0.000 claims description 37
- 238000004132 cross linking Methods 0.000 claims description 33
- 108010062713 lamprin Proteins 0.000 claims description 28
- 229920001872 Spider silk Polymers 0.000 claims description 14
- 238000006467 substitution reaction Methods 0.000 claims description 12
- 150000001413 amino acids Chemical class 0.000 claims description 11
- 238000007792 addition Methods 0.000 claims description 10
- 210000004204 blood vessel Anatomy 0.000 claims description 10
- 238000012217 deletion Methods 0.000 claims description 10
- 230000037430 deletion Effects 0.000 claims description 10
- 239000000203 mixture Substances 0.000 claims description 10
- 229910052751 metal Inorganic materials 0.000 claims description 9
- 239000002184 metal Substances 0.000 claims description 9
- 241000894007 species Species 0.000 claims description 9
- 229920002994 synthetic fiber Polymers 0.000 claims description 6
- 102000037865 fusion proteins Human genes 0.000 claims description 5
- 108020001507 fusion proteins Proteins 0.000 claims description 5
- 238000002513 implantation Methods 0.000 claims description 5
- 239000013013 elastic material Substances 0.000 claims description 4
- 206010052428 Wound Diseases 0.000 claims description 3
- 208000027418 Wounds and injury Diseases 0.000 claims description 3
- 239000002537 cosmetic Substances 0.000 claims description 3
- 210000003709 heart valve Anatomy 0.000 claims description 2
- 101000851054 Homo sapiens Elastin Proteins 0.000 description 58
- 102000054289 human ELN Human genes 0.000 description 55
- 235000018102 proteins Nutrition 0.000 description 45
- 230000002209 hydrophobic effect Effects 0.000 description 41
- 238000000034 method Methods 0.000 description 19
- 102100033167 Elastin Human genes 0.000 description 15
- 238000004220 aggregation Methods 0.000 description 15
- 239000000835 fiber Substances 0.000 description 15
- 239000011159 matrix material Substances 0.000 description 14
- 238000005354 coacervation Methods 0.000 description 13
- 235000001014 amino acid Nutrition 0.000 description 12
- 238000000576 coating method Methods 0.000 description 12
- 230000015572 biosynthetic process Effects 0.000 description 11
- 239000011248 coating agent Substances 0.000 description 11
- 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 11
- 229940024606 amino acid Drugs 0.000 description 10
- 210000004027 cell Anatomy 0.000 description 10
- 210000001519 tissue Anatomy 0.000 description 10
- 108010035532 Collagen Proteins 0.000 description 9
- 102000008186 Collagen Human genes 0.000 description 9
- 101000851055 Gallus gallus Elastin Proteins 0.000 description 9
- 229920001436 collagen Polymers 0.000 description 9
- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 9
- 239000002953 phosphate buffered saline Substances 0.000 description 9
- 239000000047 product Substances 0.000 description 9
- 108700024394 Exon Proteins 0.000 description 7
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 7
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 7
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 7
- 239000000243 solution Substances 0.000 description 7
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 6
- 229920004934 Dacron® Polymers 0.000 description 6
- 241000282412 Homo Species 0.000 description 6
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 6
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 6
- 238000003776 cleavage reaction Methods 0.000 description 6
- 229960000310 isoleucine Drugs 0.000 description 6
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 6
- 239000010410 layer Substances 0.000 description 6
- 230000004048 modification Effects 0.000 description 6
- 238000012986 modification Methods 0.000 description 6
- 239000005020 polyethylene terephthalate Substances 0.000 description 6
- 238000002360 preparation method Methods 0.000 description 6
- 230000007017 scission Effects 0.000 description 6
- 239000004474 valine Substances 0.000 description 6
- 102000009123 Fibrin Human genes 0.000 description 5
- 108010073385 Fibrin Proteins 0.000 description 5
- BWGVNKXGVNDBDI-UHFFFAOYSA-N Fibrin monomer Chemical compound CNC(=O)CNC(=O)CN BWGVNKXGVNDBDI-UHFFFAOYSA-N 0.000 description 5
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 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
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 5
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 5
- 235000004279 alanine Nutrition 0.000 description 5
- 230000008901 benefit Effects 0.000 description 5
- 239000012620 biological material Substances 0.000 description 5
- ATDGTVJJHBUTRL-UHFFFAOYSA-N cyanogen bromide Chemical compound BrC#N ATDGTVJJHBUTRL-UHFFFAOYSA-N 0.000 description 5
- 229950003499 fibrin Drugs 0.000 description 5
- 230000001965 increasing effect Effects 0.000 description 5
- 235000018977 lysine Nutrition 0.000 description 5
- 235000006109 methionine Nutrition 0.000 description 5
- 239000004814 polyurethane Substances 0.000 description 5
- 229920002635 polyurethane Polymers 0.000 description 5
- 230000008569 process Effects 0.000 description 5
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 5
- 108020004414 DNA Proteins 0.000 description 4
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 4
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 4
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 4
- 239000004472 Lysine Substances 0.000 description 4
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 4
- 239000004809 Teflon Substances 0.000 description 4
- 229920006362 Teflon® Polymers 0.000 description 4
- 210000001367 artery Anatomy 0.000 description 4
- 238000010382 chemical cross-linking Methods 0.000 description 4
- 238000004587 chromatography analysis Methods 0.000 description 4
- 229920000295 expanded polytetrafluoroethylene Polymers 0.000 description 4
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 4
- 230000008595 infiltration Effects 0.000 description 4
- 238000001764 infiltration Methods 0.000 description 4
- 229930182817 methionine Natural products 0.000 description 4
- 239000000178 monomer Substances 0.000 description 4
- 230000001453 nonthrombogenic effect Effects 0.000 description 4
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 4
- 229920000642 polymer Polymers 0.000 description 4
- 238000001338 self-assembly Methods 0.000 description 4
- 238000001262 western blot Methods 0.000 description 4
- VEVRNHHLCPGNDU-MUGJNUQGSA-N (2s)-2-amino-5-[1-[(5s)-5-amino-5-carboxypentyl]-3,5-bis[(3s)-3-amino-3-carboxypropyl]pyridin-1-ium-4-yl]pentanoate Chemical compound OC(=O)[C@@H](N)CCCC[N+]1=CC(CC[C@H](N)C(O)=O)=C(CCC[C@H](N)C([O-])=O)C(CC[C@H](N)C(O)=O)=C1 VEVRNHHLCPGNDU-MUGJNUQGSA-N 0.000 description 3
- 239000004475 Arginine Substances 0.000 description 3
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 3
- 108020004705 Codon Proteins 0.000 description 3
- 102000010834 Extracellular Matrix Proteins Human genes 0.000 description 3
- 108010037362 Extracellular Matrix Proteins Proteins 0.000 description 3
- 241000287828 Gallus gallus Species 0.000 description 3
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 3
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 3
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 3
- 108010003894 Protein-Lysine 6-Oxidase Proteins 0.000 description 3
- 102100026858 Protein-lysine 6-oxidase Human genes 0.000 description 3
- 108091081062 Repeated sequence (DNA) Proteins 0.000 description 3
- 239000002253 acid Substances 0.000 description 3
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 3
- 235000009697 arginine Nutrition 0.000 description 3
- 235000009582 asparagine Nutrition 0.000 description 3
- 229960001230 asparagine Drugs 0.000 description 3
- 239000000560 biocompatible material Substances 0.000 description 3
- 239000002131 composite material Substances 0.000 description 3
- 239000012634 fragment Substances 0.000 description 3
- 230000004927 fusion Effects 0.000 description 3
- 229930195712 glutamate Natural products 0.000 description 3
- 230000002163 immunogen Effects 0.000 description 3
- 238000004519 manufacturing process Methods 0.000 description 3
- 230000000704 physical effect Effects 0.000 description 3
- 210000003491 skin Anatomy 0.000 description 3
- 108010054022 valyl-prolyl-glycyl-valyl-glycine Proteins 0.000 description 3
- 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 2
- 241000588724 Escherichia coli Species 0.000 description 2
- 239000004471 Glycine Substances 0.000 description 2
- 229920000544 Gore-Tex Polymers 0.000 description 2
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 description 2
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 2
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 2
- 239000004473 Threonine Substances 0.000 description 2
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 2
- 150000007513 acids Chemical class 0.000 description 2
- 238000004458 analytical method Methods 0.000 description 2
- 229940009098 aspartate Drugs 0.000 description 2
- 239000002585 base Substances 0.000 description 2
- YCIMNLLNPGFGHC-UHFFFAOYSA-N catechol Chemical compound OC1=CC=CC=C1O YCIMNLLNPGFGHC-UHFFFAOYSA-N 0.000 description 2
- 239000003795 chemical substances by application Substances 0.000 description 2
- 239000003431 cross linking reagent Substances 0.000 description 2
- 230000001419 dependent effect Effects 0.000 description 2
- 238000010586 diagram Methods 0.000 description 2
- RWSXRVCMGQZWBV-WDSKDSINSA-N glutathione Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O RWSXRVCMGQZWBV-WDSKDSINSA-N 0.000 description 2
- 230000035876 healing Effects 0.000 description 2
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 2
- 230000003278 mimic effect Effects 0.000 description 2
- 150000003839 salts Chemical class 0.000 description 2
- 210000004872 soft tissue Anatomy 0.000 description 2
- 239000007787 solid Substances 0.000 description 2
- 238000003786 synthesis reaction Methods 0.000 description 2
- 108010003885 valyl-prolyl-glycyl-glycine Proteins 0.000 description 2
- 102100026189 Beta-galactosidase Human genes 0.000 description 1
- 241000255789 Bombyx mori Species 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- 101000575377 Bos taurus Microfibrillar-associated protein 2 Proteins 0.000 description 1
- 101100315624 Caenorhabditis elegans tyr-1 gene Proteins 0.000 description 1
- 102000030523 Catechol oxidase Human genes 0.000 description 1
- 108010031396 Catechol oxidase Proteins 0.000 description 1
- 108010067306 Fibronectins Proteins 0.000 description 1
- 102000016359 Fibronectins Human genes 0.000 description 1
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 1
- 108010024636 Glutathione Proteins 0.000 description 1
- 108060003393 Granulin Proteins 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 102000003839 Human Proteins Human genes 0.000 description 1
- 108090000144 Human Proteins Proteins 0.000 description 1
- 241000235789 Hyperoartia Species 0.000 description 1
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 description 1
- 101150118523 LYS4 gene Proteins 0.000 description 1
- 108010085895 Laminin Proteins 0.000 description 1
- 102000007547 Laminin Human genes 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
- 101100342977 Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) leu-1 gene Proteins 0.000 description 1
- 108091028043 Nucleic acid sequence Proteins 0.000 description 1
- 102000003992 Peroxidases Human genes 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- 108010076504 Protein Sorting Signals Proteins 0.000 description 1
- 108091006629 SLC13A2 Proteins 0.000 description 1
- 101710172711 Structural protein Proteins 0.000 description 1
- RTAQQCXQSZGOHL-UHFFFAOYSA-N Titanium Chemical compound [Ti] RTAQQCXQSZGOHL-UHFFFAOYSA-N 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 239000000654 additive Substances 0.000 description 1
- 230000002411 adverse Effects 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 125000003295 alanine group Chemical group N[C@@H](C)C(=O)* 0.000 description 1
- 150000001299 aldehydes Chemical class 0.000 description 1
- 239000003513 alkali Substances 0.000 description 1
- 230000004075 alteration Effects 0.000 description 1
- 125000003277 amino group Chemical group 0.000 description 1
- 235000003704 aspartic acid Nutrition 0.000 description 1
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 description 1
- 229920001222 biopolymer Polymers 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 238000004364 calculation method Methods 0.000 description 1
- 210000000845 cartilage Anatomy 0.000 description 1
- 230000021164 cell adhesion Effects 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 210000001136 chorion Anatomy 0.000 description 1
- 108010078300 chorion proteins Proteins 0.000 description 1
- 230000000295 complement effect Effects 0.000 description 1
- 239000002299 complementary DNA Substances 0.000 description 1
- 210000002808 connective tissue Anatomy 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 125000000798 desmosine group Chemical group 0.000 description 1
- 230000000694 effects Effects 0.000 description 1
- 108010064033 elastin-binding proteins Proteins 0.000 description 1
- 229920001198 elastomeric copolymer Polymers 0.000 description 1
- 230000003028 elevating effect Effects 0.000 description 1
- 210000002889 endothelial cell Anatomy 0.000 description 1
- 230000003511 endothelial effect Effects 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 210000002744 extracellular matrix Anatomy 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 238000001125 extrusion Methods 0.000 description 1
- 230000001605 fetal effect Effects 0.000 description 1
- 239000012530 fluid Substances 0.000 description 1
- 238000000799 fluorescence microscopy Methods 0.000 description 1
- 230000006870 function Effects 0.000 description 1
- 235000013922 glutamic acid Nutrition 0.000 description 1
- 239000004220 glutamic acid Substances 0.000 description 1
- 229960003180 glutathione Drugs 0.000 description 1
- 229910052739 hydrogen Inorganic materials 0.000 description 1
- 239000001257 hydrogen Substances 0.000 description 1
- 230000005847 immunogenicity Effects 0.000 description 1
- 239000007943 implant Substances 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- 210000003041 ligament Anatomy 0.000 description 1
- 230000007774 longterm Effects 0.000 description 1
- 210000004072 lung Anatomy 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 150000002739 metals Chemical class 0.000 description 1
- 150000002742 methionines Chemical class 0.000 description 1
- 239000005445 natural material Substances 0.000 description 1
- 238000007833 oxidative deamination reaction Methods 0.000 description 1
- 108040007629 peroxidase activity proteins Proteins 0.000 description 1
- 238000006552 photochemical reaction Methods 0.000 description 1
- 239000002243 precursor Substances 0.000 description 1
- 230000002028 premature Effects 0.000 description 1
- 239000012264 purified product Substances 0.000 description 1
- 230000004044 response Effects 0.000 description 1
- 230000028327 secretion 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
- 239000011343 solid material Substances 0.000 description 1
- 108010028203 spidroin 2 Proteins 0.000 description 1
- 230000002269 spontaneous effect Effects 0.000 description 1
- 229910001220 stainless steel Inorganic materials 0.000 description 1
- 239000010935 stainless steel Substances 0.000 description 1
- -1 stents Substances 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 239000002344 surface layer Substances 0.000 description 1
- 230000002885 thrombogenetic effect Effects 0.000 description 1
- 239000010936 titanium Substances 0.000 description 1
- 229910052719 titanium Inorganic materials 0.000 description 1
- 238000004627 transmission electron microscopy Methods 0.000 description 1
- 230000002792 vascular Effects 0.000 description 1
- 210000003556 vascular endothelial cell Anatomy 0.000 description 1
- 210000004509 vascular smooth muscle cell Anatomy 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
Classifications
-
- 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]
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K8/00—Cosmetics or similar toiletry preparations
- A61K8/18—Cosmetics or similar toiletry preparations characterised by the composition
- A61K8/30—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds
- A61K8/64—Proteins; Peptides; Derivatives or degradation products thereof
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61L—METHODS OR APPARATUS FOR STERILISING MATERIALS OR OBJECTS IN GENERAL; DISINFECTION, STERILISATION OR DEODORISATION OF AIR; CHEMICAL ASPECTS OF BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES; MATERIALS FOR BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES
- A61L27/00—Materials for grafts or prostheses or for coating grafts or prostheses
- A61L27/28—Materials for coating prostheses
- A61L27/34—Macromolecular materials
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61L—METHODS OR APPARATUS FOR STERILISING MATERIALS OR OBJECTS IN GENERAL; DISINFECTION, STERILISATION OR DEODORISATION OF AIR; CHEMICAL ASPECTS OF BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES; MATERIALS FOR BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES
- A61L31/00—Materials for other surgical articles, e.g. stents, stent-grafts, shunts, surgical drapes, guide wires, materials for adhesion prevention, occluding devices, surgical gloves, tissue fixation devices
- A61L31/08—Materials for coatings
- A61L31/10—Macromolecular materials
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
- A61Q19/00—Preparations for care of the skin
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K2800/00—Properties of cosmetic compositions or active ingredients thereof or formulation aids used therein and process related aspects
- A61K2800/70—Biological properties of the composition as a whole
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K2800/00—Properties of cosmetic compositions or active ingredients thereof or formulation aids used therein and process related aspects
- A61K2800/80—Process related aspects concerning the preparation of the cosmetic composition or the storage or application thereof
- A61K2800/86—Products or compounds obtained by genetic engineering
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S977/00—Nanotechnology
- Y10S977/902—Specified use of nanostructure
- Y10S977/904—Specified use of nanostructure for medical, immunological, body treatment, or diagnosis
- Y10S977/92—Detection of biochemical
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Veterinary Medicine (AREA)
- Chemical & Material Sciences (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Epidemiology (AREA)
- Dermatology (AREA)
- Medicinal Chemistry (AREA)
- Organic Chemistry (AREA)
- Surgery (AREA)
- Biophysics (AREA)
- Heart & Thoracic Surgery (AREA)
- Transplantation (AREA)
- Vascular Medicine (AREA)
- Toxicology (AREA)
- Zoology (AREA)
- Gastroenterology & Hepatology (AREA)
- Biochemistry (AREA)
- Birds (AREA)
- Genetics & Genomics (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Oral & Maxillofacial Surgery (AREA)
- Materials For Medical Uses (AREA)
- Peptides Or Proteins (AREA)
- Cosmetics (AREA)
Applications Claiming Priority (5)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US2355296P | 1996-08-07 | 1996-08-07 | |
| US60/023552 | 1996-08-07 | ||
| US08/911364 | 1997-08-07 | ||
| PCT/CA1997/000560 WO1998005685A2 (en) | 1996-08-07 | 1997-08-07 | Self-aligning peptides derived from elastin and other fibrous proteins |
| US08/911,364 US5969106A (en) | 1996-08-07 | 1997-08-07 | Self-aligning peptides modeled on human elastin and other fibrous proteins |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| AU3843897A AU3843897A (en) | 1998-02-25 |
| AU728480B2 true AU728480B2 (en) | 2001-01-11 |
Family
ID=26697313
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| AU38438/97A Ceased AU728480B2 (en) | 1996-08-07 | 1997-08-07 | Self-aligning peptides derived from elastin and other fibrous proteins |
Country Status (6)
| Country | Link |
|---|---|
| US (1) | US5969106A (enExample) |
| EP (1) | EP0922058A2 (enExample) |
| JP (1) | JP2001505539A (enExample) |
| AU (1) | AU728480B2 (enExample) |
| CA (1) | CA2262446A1 (enExample) |
| WO (1) | WO1998005685A2 (enExample) |
Families Citing this family (24)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20030198956A1 (en) * | 2002-02-21 | 2003-10-23 | Lee Makowski | Staged assembly of nanostructures |
| US6489446B1 (en) | 1996-08-07 | 2002-12-03 | Hsc Research And Development Limited Partnership | Self-aligning peptides modeled on human elastin and other fibrous proteins |
| CA2262446A1 (en) * | 1996-08-07 | 1998-02-12 | Protein Specialties, Ltd. | Self-aligning peptides derived from elastin and other fibrous proteins |
| US6369626B1 (en) | 1997-03-21 | 2002-04-09 | Rambus Inc. | Low pass filter for a delay locked loop circuit |
| US20050204408A1 (en) * | 1998-07-17 | 2005-09-15 | Weiss Anthony S. | Tropoelastin derivatives |
| AUPO811797A0 (en) | 1997-07-18 | 1997-08-14 | University Of Sydney, The | Tropoelastin derivatives |
| US7193043B1 (en) * | 1998-07-17 | 2007-03-20 | Weiss Anthony S | Tropoelastin derivatives |
| AUPP472398A0 (en) | 1998-07-17 | 1998-08-13 | University Of Sydney, The | Protease susceptibility II |
| US6903244B1 (en) * | 1999-02-26 | 2005-06-07 | University Of Utah Research Foundation | Mice which are +/− or −/− for the elastin gene as models for vascular disease |
| US20010053931A1 (en) * | 1999-11-24 | 2001-12-20 | Salvatore J. Abbruzzese | Thin-layered, endovascular silk-covered stent device and method of manufacture thereof |
| US6808707B2 (en) * | 2000-02-04 | 2004-10-26 | Matrix Design | Wound healing compositions and methods using tropoelastin and lysyl oxidase |
| GB0108767D0 (en) * | 2001-04-07 | 2001-05-30 | Univ Leeds | Coatings |
| US6902932B2 (en) * | 2001-11-16 | 2005-06-07 | Tissue Regeneration, Inc. | Helically organized silk fibroin fiber bundles for matrices in tissue engineering |
| WO2003069033A1 (en) * | 2002-02-14 | 2003-08-21 | The University Of British Columbia | α-HELICAL PROTEIN BASED MATERIALS AND METHODS FOR MAKING SAME |
| AU2003902483A0 (en) * | 2003-05-21 | 2003-06-05 | Commonwealth Scientific And Industrial Research Organisation | A bioelastomer ii |
| AU2003902474A0 (en) * | 2003-05-21 | 2003-06-05 | Commonwealth Scientific And Industrial Research Organisation | A bioelastomer i |
| CA2669114C (en) | 2006-11-13 | 2014-12-16 | The University Of Sydney | Use of tropoelastin for repair or restoration of tissue |
| CA2686895A1 (en) * | 2007-05-10 | 2008-11-20 | Elastin Specialties, Inc. | Synthetic peptide materials for joint reconstruction, repair and cushioning |
| US9308070B2 (en) | 2008-12-15 | 2016-04-12 | Allergan, Inc. | Pliable silk medical device |
| WO2010102337A1 (en) | 2009-03-10 | 2010-09-16 | The University Of Sydney | Injectable biomaterials |
| CN105530951B (zh) | 2013-08-13 | 2019-10-22 | 爱力根制药国际有限公司 | 受损组织的再生 |
| SG11202111349QA (en) * | 2019-04-12 | 2021-11-29 | Geltor Inc | Recombinant elastin and production thereof |
| WO2022038155A1 (en) * | 2020-08-18 | 2022-02-24 | Universität Basel | Hemostatic elastin-like polypeptides |
| CN112745394B (zh) * | 2020-12-09 | 2022-12-06 | 肽源（广州）生物科技有限公司 | 一种重组类人胶原蛋白及其制备方法和应用 |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO1991016919A1 (en) * | 1990-05-03 | 1991-11-14 | New England Deaconess Hospital Corporation | Synthetic peptides for arterial imaging |
| WO1994014598A1 (en) * | 1992-12-21 | 1994-07-07 | Anthony Joseph Cesaroni | Bonding of tubes to articles |
Family Cites Families (27)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4132746A (en) * | 1976-07-09 | 1979-01-02 | University Of Alabama, Birmingham Medical & Education Foundation | Synthetic elastomeric insoluble cross-linked polypentapeptide |
| NL7713618A (nl) * | 1976-12-11 | 1978-06-13 | Bayer Ag | Werkwijze voor de bereiding van een cosmetisch preparaat. |
| DE2705670C3 (de) * | 1977-02-11 | 1983-11-17 | Fa. Carl Freudenberg, 6940 Weinheim | Verfahren zur Herstellung von wasserlöslichen Elastin-Hydrolysaten |
| US4419288A (en) * | 1981-08-27 | 1983-12-06 | Seton Company | Elastin hydrolyzate |
| US4474851A (en) * | 1981-10-02 | 1984-10-02 | The University Of Alabama In Birmingham | Elastomeric composite material comprising a polypeptide |
| US4474763A (en) * | 1982-07-07 | 1984-10-02 | Lubowe Irwin I | Skin preparation |
| US4960423A (en) * | 1982-11-17 | 1990-10-02 | Smith Donald W | Method of enhancing the attachment of endothelial cells on a matrix and vascular prosthesis with enhanced anti-thrombogenic characteristics |
| US4589882A (en) * | 1983-09-19 | 1986-05-20 | Urry Dan W | Enzymatically crosslinked bioelastomers |
| US4659740A (en) * | 1985-02-14 | 1987-04-21 | Polydex Pharmaceuticals Ltd. | Cosmetic preparations comprising novel elastin derivatives |
| FR2598423B1 (fr) * | 1985-03-01 | 1989-03-17 | Inst Nat Sante Rech Med | Produit a base d'elastine, procede pour sa preparation et ses applications biologiques, en particulier en tant que biomateriaux et supports artificiels |
| US5223420A (en) * | 1985-03-01 | 1993-06-29 | Institut National De La Sante Et De La Recherche Medicale | Elastin-based product, a procedure for its preparation and its biological applications; in particular as biomaterials and artificial supports |
| US5336256A (en) * | 1986-04-17 | 1994-08-09 | Uab Research Foundation | Elastomeric polypeptides as vascular prosthetic materials |
| US4870055A (en) * | 1986-04-17 | 1989-09-26 | University Of Alabama At Birmingham | Segmented polypeptide bioelastomers to modulate elastic modulus |
| US4783523A (en) * | 1986-08-27 | 1988-11-08 | Urry Dan W | Temperature correlated force and structure development of elastin polytetrapeptides and polypentapeptides |
| US5250516A (en) * | 1986-04-17 | 1993-10-05 | Uab Research Foundation | Bioelastomeric materials suitable for the protection of burn areas or the protection of wound repair sites from the occurrence of adhesions |
| GB8618374D0 (en) * | 1986-07-28 | 1986-09-03 | Hsc Res Dev Corp | Biological vascular prostheses |
| US4979959A (en) * | 1986-10-17 | 1990-12-25 | Bio-Metric Systems, Inc. | Biocompatible coating for solid surfaces |
| US5243038A (en) * | 1986-11-04 | 1993-09-07 | Protein Polymer Technologies, Inc. | Construction of synthetic DNA and its use in large polypeptide synthesis |
| JPH01501755A (ja) * | 1986-11-04 | 1989-06-22 | シントロ コーポレイション | 合成ｄｎａの構成および大ポリペプチドの合成におけるその使用 |
| JP2549118B2 (ja) * | 1987-05-30 | 1996-10-30 | 三省製薬株式会社 | 乳化組成物 |
| US5606019A (en) * | 1987-10-29 | 1997-02-25 | Protien Polymer Technologies, Inc. | Synthetic protein as implantables |
| KR0176966B1 (ko) * | 1988-11-09 | 1999-04-01 | 제니스 케이. 맥밀리언 | 재조합 방법으로 제조한 기능적 합성 단백질 폴리머 |
| FR2649982B1 (fr) * | 1989-07-20 | 1991-09-27 | Inst Nat Sante Rech Med | Membrane biologique artificielle |
| WO1992009695A1 (en) * | 1990-11-28 | 1992-06-11 | E.I. Du Pont De Nemours And Company | Structural proteins from artificial genes |
| JP3474190B2 (ja) * | 1992-12-22 | 2003-12-08 | ザ ユニバーシテイ オブ シドニイ | 合成ポリヌクレオチド |
| US5527610A (en) * | 1994-05-20 | 1996-06-18 | The Uab Research Foundation | Elastomeric polypeptide matrices for preventing adhesion of biological materials |
| CA2262446A1 (en) * | 1996-08-07 | 1998-02-12 | Protein Specialties, Ltd. | Self-aligning peptides derived from elastin and other fibrous proteins |
-
1997
- 1997-08-07 CA CA002262446A patent/CA2262446A1/en not_active Abandoned
- 1997-08-07 EP EP97935396A patent/EP0922058A2/en not_active Withdrawn
- 1997-08-07 JP JP50741998A patent/JP2001505539A/ja not_active Withdrawn
- 1997-08-07 US US08/911,364 patent/US5969106A/en not_active Expired - Lifetime
- 1997-08-07 WO PCT/CA1997/000560 patent/WO1998005685A2/en not_active Ceased
- 1997-08-07 AU AU38438/97A patent/AU728480B2/en not_active Ceased
Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO1991016919A1 (en) * | 1990-05-03 | 1991-11-14 | New England Deaconess Hospital Corporation | Synthetic peptides for arterial imaging |
| WO1994014598A1 (en) * | 1992-12-21 | 1994-07-07 | Anthony Joseph Cesaroni | Bonding of tubes to articles |
Non-Patent Citations (1)
| Title |
|---|
| SCIENCE VOL. 271, 1996, PP. 84-87 * |
Also Published As
| Publication number | Publication date |
|---|---|
| AU3843897A (en) | 1998-02-25 |
| EP0922058A2 (en) | 1999-06-16 |
| WO1998005685A3 (en) | 1998-04-30 |
| CA2262446A1 (en) | 1998-02-12 |
| US5969106A (en) | 1999-10-19 |
| JP2001505539A (ja) | 2001-04-24 |
| WO1998005685A2 (en) | 1998-02-12 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US6489446B1 (en) | Self-aligning peptides modeled on human elastin and other fibrous proteins | |
| AU728480B2 (en) | Self-aligning peptides derived from elastin and other fibrous proteins | |
| CA2124583C (en) | Synthetic compounds and compositions with enhanced cell binding | |
| El Blidi et al. | Extraction methods, characterization and biomedical applications of collagen: A review | |
| US7700126B2 (en) | Tropoelastin-based protoelastin biomaterials | |
| US4589882A (en) | Enzymatically crosslinked bioelastomers | |
| CA2476656C (en) | Immobilized bioactive hydrogel matrices as surface coatings | |
| US5162430A (en) | Collagen-polymer conjugates | |
| US5304595A (en) | Collagen-polymer conjugates | |
| US5306500A (en) | Method of augmenting tissue with collagen-polymer conjugates | |
| Girotti et al. | Recombinant technology in the development of materials and systems for soft‐tissue repair | |
| CA2066213A1 (en) | Surfaces having desirable cell adhesive effects | |
| WO2008150101A2 (en) | Chimeric polypeptide including a mussel adheisve protein and extracellular matrix | |
| Del Prado Audelo et al. | Recent advances in elastin-based biomaterials | |
| EP1945144A2 (en) | Method of using and producing tropoelastin and tropoelastin biomaterials | |
| Ramshaw et al. | Applications of collagen in medical devices | |
| US8119598B2 (en) | Synthetic peptide materials for joint reconstruction, repair and cushioning | |
| EP4392231A1 (en) | Collagen biomaterial derived from abalone | |
| CN111961137B (zh) | 仿生内皮细胞功能的融合蛋白及其应用 |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| FGA | Letters patent sealed or granted (standard patent) |