DE10025001A1 - Gewebekleber mit verbesserten anti-adhäsiven Eigenschaften - Google Patents
Gewebekleber mit verbesserten anti-adhäsiven EigenschaftenInfo
- Publication number
- DE10025001A1 DE10025001A1 DE10025001A DE10025001A DE10025001A1 DE 10025001 A1 DE10025001 A1 DE 10025001A1 DE 10025001 A DE10025001 A DE 10025001A DE 10025001 A DE10025001 A DE 10025001A DE 10025001 A1 DE10025001 A1 DE 10025001A1
- Authority
- DE
- Germany
- Prior art keywords
- tissue adhesive
- adhesive according
- tissue
- preparation
- acid
- 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
- 239000003106 tissue adhesive Substances 0.000 title claims abstract description 58
- 230000001976 improved effect Effects 0.000 title description 14
- 230000000181 anti-adherent effect Effects 0.000 title description 5
- 238000002360 preparation method Methods 0.000 claims abstract description 26
- 108010049003 Fibrinogen Proteins 0.000 claims abstract description 15
- 102000008946 Fibrinogen Human genes 0.000 claims abstract description 15
- 229940012952 fibrinogen Drugs 0.000 claims abstract description 15
- 108090000190 Thrombin Proteins 0.000 claims abstract description 14
- 229960004072 thrombin Drugs 0.000 claims abstract description 14
- 239000000126 substance Substances 0.000 claims abstract description 10
- 208000031737 Tissue Adhesions Diseases 0.000 claims abstract description 7
- 230000003196 chaotropic effect Effects 0.000 claims abstract description 6
- 239000007788 liquid Substances 0.000 claims abstract description 5
- 230000002980 postoperative effect Effects 0.000 claims abstract description 5
- 108010071289 Factor XIII Proteins 0.000 claims description 12
- KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 claims description 12
- 229940012444 factor xiii Drugs 0.000 claims description 11
- 150000003839 salts Chemical class 0.000 claims description 11
- 239000003381 stabilizer Substances 0.000 claims description 11
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 claims description 8
- 239000000203 mixture Substances 0.000 claims description 8
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 claims description 6
- 235000001014 amino acid Nutrition 0.000 claims description 6
- 150000001413 amino acids Chemical class 0.000 claims description 6
- 150000005846 sugar alcohols Chemical class 0.000 claims description 6
- 230000001567 anti-fibrinolytic effect Effects 0.000 claims description 5
- 238000000034 method Methods 0.000 claims description 5
- SLXKOJJOQWFEFD-UHFFFAOYSA-N 6-aminohexanoic acid Chemical compound NCCCCCC(O)=O SLXKOJJOQWFEFD-UHFFFAOYSA-N 0.000 claims description 4
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 claims description 4
- ZRALSGWEFCBTJO-UHFFFAOYSA-N Guanidine Chemical compound NC(N)=N ZRALSGWEFCBTJO-UHFFFAOYSA-N 0.000 claims description 4
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 claims description 4
- 239000002253 acid Substances 0.000 claims description 4
- 150000002016 disaccharides Chemical class 0.000 claims description 4
- YMAWOPBAYDPSLA-UHFFFAOYSA-N glycylglycine Chemical compound [NH3+]CC(=O)NCC([O-])=O YMAWOPBAYDPSLA-UHFFFAOYSA-N 0.000 claims description 4
- JVTAAEKCZFNVCJ-UHFFFAOYSA-N lactic acid Chemical compound CC(O)C(O)=O JVTAAEKCZFNVCJ-UHFFFAOYSA-N 0.000 claims description 4
- 150000002772 monosaccharides Chemical class 0.000 claims description 4
- 239000011780 sodium chloride Substances 0.000 claims description 4
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 claims description 3
- 229960002684 aminocaproic acid Drugs 0.000 claims description 3
- QCTBMLYLENLHLA-UHFFFAOYSA-N aminomethylbenzoic acid Chemical compound NCC1=CC=C(C(O)=O)C=C1 QCTBMLYLENLHLA-UHFFFAOYSA-N 0.000 claims description 3
- 229960003375 aminomethylbenzoic acid Drugs 0.000 claims description 3
- 235000004554 glutamine Nutrition 0.000 claims description 3
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 claims description 3
- 239000003112 inhibitor Substances 0.000 claims description 3
- 239000004475 Arginine Substances 0.000 claims description 2
- 239000004471 Glycine Substances 0.000 claims description 2
- 108010008488 Glycylglycine Proteins 0.000 claims description 2
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 claims description 2
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 claims description 2
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 claims description 2
- RHGKLRLOHDJJDR-BYPYZUCNSA-N L-citrulline Chemical compound NC(=O)NCCC[C@H]([NH3+])C([O-])=O RHGKLRLOHDJJDR-BYPYZUCNSA-N 0.000 claims description 2
- CHJJGSNFBQVOTG-UHFFFAOYSA-N N-methyl-guanidine Natural products CNC(N)=N CHJJGSNFBQVOTG-UHFFFAOYSA-N 0.000 claims description 2
- RHGKLRLOHDJJDR-UHFFFAOYSA-N Ndelta-carbamoyl-DL-ornithine Natural products OC(=O)C(N)CCCNC(N)=O RHGKLRLOHDJJDR-UHFFFAOYSA-N 0.000 claims description 2
- 241000700605 Viruses Species 0.000 claims description 2
- 235000004279 alanine Nutrition 0.000 claims description 2
- 239000003963 antioxidant agent Substances 0.000 claims description 2
- 230000003078 antioxidant effect Effects 0.000 claims description 2
- 235000009697 arginine Nutrition 0.000 claims description 2
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 claims description 2
- 159000000007 calcium salts Chemical class 0.000 claims description 2
- 239000004202 carbamide Substances 0.000 claims description 2
- 150000001735 carboxylic acids Chemical class 0.000 claims description 2
- 238000005277 cation exchange chromatography Methods 0.000 claims description 2
- 235000013477 citrulline Nutrition 0.000 claims description 2
- 229960002173 citrulline Drugs 0.000 claims description 2
- 235000018417 cysteine Nutrition 0.000 claims description 2
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 claims description 2
- SWSQBOPZIKWTGO-UHFFFAOYSA-N dimethylaminoamidine Natural products CN(C)C(N)=N SWSQBOPZIKWTGO-UHFFFAOYSA-N 0.000 claims description 2
- 229940043257 glycylglycine Drugs 0.000 claims description 2
- 235000014304 histidine Nutrition 0.000 claims description 2
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 claims description 2
- 238000004191 hydrophobic interaction chromatography Methods 0.000 claims description 2
- 229910017053 inorganic salt Inorganic materials 0.000 claims description 2
- 239000004310 lactic acid Substances 0.000 claims description 2
- 235000014655 lactic acid Nutrition 0.000 claims description 2
- 230000008569 process Effects 0.000 claims description 2
- 239000004094 surface-active agent Substances 0.000 claims description 2
- 150000000000 tetracarboxylic acids Chemical class 0.000 claims description 2
- 150000003628 tricarboxylic acids Chemical class 0.000 claims description 2
- OZDAOHVKBFBBMZ-UHFFFAOYSA-N 2-aminopentanedioic acid;hydrate Chemical compound O.OC(=O)C(N)CCC(O)=O OZDAOHVKBFBBMZ-UHFFFAOYSA-N 0.000 claims 1
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 claims 1
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 claims 1
- 235000003704 aspartic acid Nutrition 0.000 claims 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 claims 1
- 239000012928 buffer substance Substances 0.000 claims 1
- 235000013922 glutamic acid Nutrition 0.000 claims 1
- 229940075469 tissue adhesives Drugs 0.000 description 12
- 241000283973 Oryctolagus cuniculus Species 0.000 description 10
- 241001465754 Metazoa Species 0.000 description 8
- 108010080379 Fibrin Tissue Adhesive Proteins 0.000 description 7
- 230000002439 hemostatic effect Effects 0.000 description 7
- 230000002265 prevention Effects 0.000 description 6
- 206010052428 Wound Diseases 0.000 description 5
- 208000027418 Wounds and injury Diseases 0.000 description 5
- 230000001070 adhesive effect Effects 0.000 description 5
- 210000004185 liver Anatomy 0.000 description 5
- 230000009467 reduction Effects 0.000 description 5
- 108010073385 Fibrin Proteins 0.000 description 4
- 102000009123 Fibrin Human genes 0.000 description 4
- BWGVNKXGVNDBDI-UHFFFAOYSA-N Fibrin monomer Chemical compound CNC(=O)CNC(=O)CN BWGVNKXGVNDBDI-UHFFFAOYSA-N 0.000 description 4
- 210000000683 abdominal cavity Anatomy 0.000 description 4
- 239000000853 adhesive Substances 0.000 description 4
- 230000000694 effects Effects 0.000 description 4
- 229950003499 fibrin Drugs 0.000 description 4
- 230000023597 hemostasis Effects 0.000 description 4
- 229940024606 amino acid Drugs 0.000 description 3
- 229960002885 histidine Drugs 0.000 description 3
- 239000012141 concentrate Substances 0.000 description 2
- 239000003292 glue Substances 0.000 description 2
- 239000000463 material Substances 0.000 description 2
- 238000002271 resection Methods 0.000 description 2
- 239000011734 sodium Substances 0.000 description 2
- PGOHTUIFYSHAQG-LJSDBVFPSA-N (2S)-6-amino-2-[[(2S)-5-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-4-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-5-amino-2-[[(2S)-5-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S,3R)-2-[[(2S)-5-amino-2-[[(2S)-2-[[(2S)-2-[[(2S,3R)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-5-amino-2-[[(2S)-1-[(2S,3R)-2-[[(2S)-2-[[(2S)-2-[[(2R)-2-[[(2S)-2-[[(2S)-2-[[2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-1-[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-amino-4-methylsulfanylbutanoyl]amino]-3-(1H-indol-3-yl)propanoyl]amino]-5-carbamimidamidopentanoyl]amino]propanoyl]pyrrolidine-2-carbonyl]amino]-3-methylbutanoyl]amino]-4-methylpentanoyl]amino]-4-methylpentanoyl]amino]acetyl]amino]-3-hydroxypropanoyl]amino]-4-methylpentanoyl]amino]-3-sulfanylpropanoyl]amino]-4-methylsulfanylbutanoyl]amino]-5-carbamimidamidopentanoyl]amino]-3-hydroxybutanoyl]pyrrolidine-2-carbonyl]amino]-5-oxopentanoyl]amino]-3-hydroxypropanoyl]amino]-3-hydroxypropanoyl]amino]-3-(1H-imidazol-5-yl)propanoyl]amino]-4-methylpentanoyl]amino]-3-hydroxybutanoyl]amino]-3-(1H-indol-3-yl)propanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-oxopentanoyl]amino]-3-hydroxybutanoyl]amino]-3-hydroxypropanoyl]amino]-3-carboxypropanoyl]amino]-3-hydroxypropanoyl]amino]-5-oxopentanoyl]amino]-5-oxopentanoyl]amino]-3-phenylpropanoyl]amino]-5-carbamimidamidopentanoyl]amino]-3-methylbutanoyl]amino]-4-methylpentanoyl]amino]-4-oxobutanoyl]amino]-5-carbamimidamidopentanoyl]amino]-3-(1H-indol-3-yl)propanoyl]amino]-4-carboxybutanoyl]amino]-5-oxopentanoyl]amino]hexanoic acid Chemical compound CSCC[C@H](N)C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](C)C(=O)N1CCC[C@H]1C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CO)C(=O)N[C@@H](Cc1cnc[nH]1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCCCN)C(O)=O PGOHTUIFYSHAQG-LJSDBVFPSA-N 0.000 description 1
- WPANETAWYGDRLL-UHFFFAOYSA-N 4-aminobenzenecarboximidamide Chemical compound NC(=N)C1=CC=C(N)C=C1 WPANETAWYGDRLL-UHFFFAOYSA-N 0.000 description 1
- 206010002091 Anaesthesia Diseases 0.000 description 1
- 108010039627 Aprotinin Proteins 0.000 description 1
- FBPFZTCFMRRESA-KVTDHHQDSA-N D-Mannitol Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-KVTDHHQDSA-N 0.000 description 1
- ODKSFYDXXFIFQN-BYPYZUCNSA-N L-arginine Chemical compound OC(=O)[C@@H](N)CCCN=C(N)N ODKSFYDXXFIFQN-BYPYZUCNSA-N 0.000 description 1
- 229930064664 L-arginine Natural products 0.000 description 1
- 235000014852 L-arginine Nutrition 0.000 description 1
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 1
- 229930195725 Mannitol Natural products 0.000 description 1
- 206010034650 Peritoneal adhesions Diseases 0.000 description 1
- 108010094028 Prothrombin Proteins 0.000 description 1
- 102100027378 Prothrombin Human genes 0.000 description 1
- 108010000499 Thromboplastin Proteins 0.000 description 1
- 102000002262 Thromboplastin Human genes 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 230000037005 anaesthesia Effects 0.000 description 1
- 238000010171 animal model Methods 0.000 description 1
- 229960004405 aprotinin Drugs 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- PXXJHWLDUBFPOL-UHFFFAOYSA-N benzamidine Chemical compound NC(=N)C1=CC=CC=C1 PXXJHWLDUBFPOL-UHFFFAOYSA-N 0.000 description 1
- 229920000249 biocompatible polymer Polymers 0.000 description 1
- 229920002988 biodegradable polymer Polymers 0.000 description 1
- 239000004621 biodegradable polymer Substances 0.000 description 1
- 239000003114 blood coagulation factor Substances 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 230000008094 contradictory effect Effects 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 229940042399 direct acting antivirals protease inhibitors Drugs 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 239000004744 fabric Substances 0.000 description 1
- 239000000535 fibrinogen concentrate Substances 0.000 description 1
- 210000005161 hepatic lobe Anatomy 0.000 description 1
- 230000001771 impaired effect Effects 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 238000011065 in-situ storage Methods 0.000 description 1
- 230000000415 inactivating effect Effects 0.000 description 1
- ZPNFWUPYTFPOJU-LPYSRVMUSA-N iniprol Chemical compound C([C@H]1C(=O)NCC(=O)NCC(=O)N[C@H]2CSSC[C@H]3C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@H](C(N[C@H](C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC=4C=CC=CC=4)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC=4C=CC=CC=4)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCCN)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(N)=N)NC2=O)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC=2C=CC=CC=2)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H]2N(CCC2)C(=O)[C@@H](N)CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N2[C@@H](CCC2)C(=O)N2[C@@H](CCC2)C(=O)N[C@@H](CC=2C=CC(O)=CC=2)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(=O)N2[C@@H](CCC2)C(=O)N3)C(=O)NCC(=O)NCC(=O)N[C@@H](C)C(O)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@H](C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@H](C(=O)N1)C(C)C)[C@@H](C)O)[C@@H](C)CC)=O)[C@@H](C)CC)C1=CC=C(O)C=C1 ZPNFWUPYTFPOJU-LPYSRVMUSA-N 0.000 description 1
- 239000000594 mannitol Substances 0.000 description 1
- 235000010355 mannitol Nutrition 0.000 description 1
- 239000000137 peptide hydrolase inhibitor Substances 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 229940039716 prothrombin Drugs 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 238000007789 sealing Methods 0.000 description 1
- 238000011477 surgical intervention Methods 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 210000004291 uterus Anatomy 0.000 description 1
Classifications
-
- 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
- A61L31/04—Macromolecular materials
- A61L31/043—Proteins; Polypeptides; Degradation products thereof
- A61L31/046—Fibrin; Fibrinogen
-
- 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
- A61L24/00—Surgical adhesives or cements; Adhesives for colostomy devices
- A61L24/04—Surgical adhesives or cements; Adhesives for colostomy devices containing macromolecular materials
- A61L24/10—Polypeptides; Proteins
- A61L24/106—Fibrin; Fibrinogen
Landscapes
- Health & Medical Sciences (AREA)
- Veterinary Medicine (AREA)
- Surgery (AREA)
- Epidemiology (AREA)
- Life Sciences & Earth Sciences (AREA)
- Animal Behavior & Ethology (AREA)
- General Health & Medical Sciences (AREA)
- Public Health (AREA)
- Vascular Medicine (AREA)
- Heart & Thoracic Surgery (AREA)
- Materials For Medical Uses (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Medicinal Preparation (AREA)
Priority Applications (11)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| DE10025001A DE10025001A1 (de) | 2000-05-22 | 2000-05-22 | Gewebekleber mit verbesserten anti-adhäsiven Eigenschaften |
| EP01111013A EP1157706A3 (de) | 2000-05-22 | 2001-05-08 | Verwendung von fibrinogenhaltigem Gewebekleber zur Verhinderung von Gewebsadhäsionen |
| DK07011684.3T DK1837039T3 (en) | 2000-05-22 | 2001-05-08 | Tissue adhesives, containing fibrinogen, to prevent tissue adhesion. |
| ES07011684.3T ES2602452T3 (es) | 2000-05-22 | 2001-05-08 | Utilización de un pegamento tisular que contiene fibrinógeno para la evitación de adherencias de tejidos |
| EP07011684.3A EP1837039B1 (de) | 2000-05-22 | 2001-05-08 | Verwendung von fibrinogenhaltigem Gewebekleber zur Verhinderung von Gewebsadhäsionen |
| CA2348119A CA2348119C (en) | 2000-05-22 | 2001-05-17 | Tissue glue with improved antiadhesive properties |
| JP2001150784A JP2001327592A (ja) | 2000-05-22 | 2001-05-21 | 抗癒着特性が改善された組織接着剤 |
| AU46166/01A AU784520B2 (en) | 2000-05-22 | 2001-05-21 | Tissues glue with improved antiadhesive properties |
| KR1020010027633A KR100858226B1 (ko) | 2000-05-22 | 2001-05-21 | 유착방지성이 개선된 조직 아교 |
| US09/861,657 US20020001584A1 (en) | 2000-05-22 | 2001-05-22 | Tissue glue with improved antiadhesive properties |
| US10/199,018 US7276235B2 (en) | 1998-11-18 | 2002-07-22 | Tissue glue with improved antiadhesive properties |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| DE10025001A DE10025001A1 (de) | 2000-05-22 | 2000-05-22 | Gewebekleber mit verbesserten anti-adhäsiven Eigenschaften |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| DE10025001A1 true DE10025001A1 (de) | 2001-11-29 |
Family
ID=7642919
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| DE10025001A Ceased DE10025001A1 (de) | 1998-11-18 | 2000-05-22 | Gewebekleber mit verbesserten anti-adhäsiven Eigenschaften |
Country Status (9)
| Country | Link |
|---|---|
| US (1) | US20020001584A1 (https=) |
| EP (2) | EP1837039B1 (https=) |
| JP (1) | JP2001327592A (https=) |
| KR (1) | KR100858226B1 (https=) |
| AU (1) | AU784520B2 (https=) |
| CA (1) | CA2348119C (https=) |
| DE (1) | DE10025001A1 (https=) |
| DK (1) | DK1837039T3 (https=) |
| ES (1) | ES2602452T3 (https=) |
Families Citing this family (16)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE10025001A1 (de) | 2000-05-22 | 2001-11-29 | Aventis Behring Gmbh | Gewebekleber mit verbesserten anti-adhäsiven Eigenschaften |
| AU2002213195A1 (en) * | 2000-10-13 | 2002-04-22 | Baxter Healthcare S.A. | Reduction or prevention of post-surgical adhesion formation with fibrinogen |
| US9119901B2 (en) | 2005-04-28 | 2015-09-01 | Warsaw Orthopedic, Inc. | Surface treatments for promoting selective tissue attachment to medical impants |
| US8414907B2 (en) | 2005-04-28 | 2013-04-09 | Warsaw Orthopedic, Inc. | Coatings on medical implants to guide soft tissue healing |
| KR100785378B1 (ko) * | 2005-09-05 | 2007-12-14 | 주식회사 바이오레인 | 다층구조의 유착방지제 |
| GB0909136D0 (en) * | 2009-05-28 | 2009-07-01 | Profibrix Bv | Dry powder composition |
| PL2435028T3 (pl) * | 2009-05-28 | 2017-09-29 | Profibrix Bv | Uszczelniacz fibrynowy w postaci suchego proszku |
| JP5808898B2 (ja) * | 2009-09-29 | 2015-11-10 | 一般財団法人化学及血清療法研究所 | 組織癒着防止剤 |
| US9504736B2 (en) | 2010-09-23 | 2016-11-29 | The Regents Of The University Of California | Administration of serine protease inhibitors to the stomach |
| CN112807325A (zh) | 2014-03-25 | 2021-05-18 | 恒翼生物医药科技(上海)有限公司 | 用于治疗自身消化的组合物 |
| BR112017018772B1 (pt) | 2015-03-12 | 2021-09-21 | Km Biologics Co., Ltd. | Material antiadesão, método para a preparação e kit do referido material e biomembrana substituta, método para a preparação e kit da referida membrana |
| CA3010986A1 (en) | 2016-01-11 | 2017-07-20 | Leading BioSciences, Inc. | Compositions and methods for treating and preventing adhesions and ileus |
| WO2020121290A1 (en) | 2018-12-12 | 2020-06-18 | Omrix Biopharmaceuticals Ltd. | High concentrated protein compositions for preventing tissue adhesion |
| IL263679A (en) | 2018-12-12 | 2019-03-31 | Omrix Biopharmaceuticals Ltd | Kits, methods, and compositions for preventing tissue adhesion |
| JP7472142B2 (ja) | 2019-08-01 | 2024-04-22 | Ｋｍバイオロジクス株式会社 | 生体適合性高分子を用いた組織の線維化抑制剤 |
| KR20250127571A (ko) * | 2024-02-19 | 2025-08-26 | 서울대학교산학협력단 | 치료용 인자 전달을 위한 페인팅 가능한 하이드로겔 시스템 개발 |
Family Cites Families (17)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5318524A (en) * | 1990-01-03 | 1994-06-07 | Cryolife, Inc. | Fibrin sealant delivery kit |
| SE9101853D0 (sv) * | 1991-06-17 | 1991-06-17 | Jonas Wadstroem | Improved tissue ashesive |
| ATE180492T1 (de) * | 1991-09-05 | 1999-06-15 | Baxter Int | Topischer fibrinogenkomplex |
| CN1091315A (zh) * | 1992-10-08 | 1994-08-31 | E·R·斯奎布父子公司 | 血纤维蛋白封闭剂组合物及其使用方法 |
| US5290918A (en) * | 1993-02-23 | 1994-03-01 | Haemacure Biotech Inc. | Process for the obtention of a biological adhesive made of concentrated coagulation factors by acidic precipitation |
| US5330974A (en) * | 1993-03-01 | 1994-07-19 | Fibratek, Inc. | Therapeutic fibrinogen compositions |
| JPH0733799A (ja) * | 1993-07-20 | 1995-02-03 | Green Cross Corp:The | 高比活性トロンビンおよびその製造方法 |
| JP3867931B2 (ja) * | 1993-11-08 | 2007-01-17 | 財団法人化学及血清療法研究所 | 液状フィブリノゲン製剤 |
| ATE244584T1 (de) * | 1995-01-16 | 2003-07-15 | Baxter Int | Selbsttragende flächengebilde aus vernetztem fibrin zur hemmung von postoperativen adhäsionen |
| JPH08333277A (ja) * | 1995-06-05 | 1996-12-17 | Hoechst Japan Ltd | ヒト血液凝固第ｘｉｉｉ因子の安定化された水性液製剤 |
| RU2193897C2 (ru) * | 1996-04-04 | 2002-12-10 | Бакстер Акциенгезельшафт | Гемостатическая губка, основанная на коллагене, способ ее получения, повязка для ран, включающая такую губку, и набор для приготовления повязки для ран |
| US6121232A (en) * | 1997-01-31 | 2000-09-19 | Omrix Biopharmaceuticals Sa | Stabilized mixture comprising fibrinogen |
| AT406120B (de) * | 1997-08-28 | 2000-02-25 | Immuno Ag | Gewebekleber |
| JPH11130682A (ja) * | 1997-10-28 | 1999-05-18 | Nihon Pharmaceutical Co Ltd | 血液凝固第ｘｉｉｉ因子の熱安定化法 |
| AU1808999A (en) * | 1997-12-09 | 1999-06-28 | Bristol-Myers Squibb Company | Fibrinolytic inhibitor for sealant |
| DE19853033A1 (de) * | 1998-11-18 | 2000-05-25 | Centeon Pharma Gmbh | Stabilisierte Proteinzubereitung für einen Gewebekleber |
| DE10025001A1 (de) * | 2000-05-22 | 2001-11-29 | Aventis Behring Gmbh | Gewebekleber mit verbesserten anti-adhäsiven Eigenschaften |
-
2000
- 2000-05-22 DE DE10025001A patent/DE10025001A1/de not_active Ceased
-
2001
- 2001-05-08 DK DK07011684.3T patent/DK1837039T3/en active
- 2001-05-08 EP EP07011684.3A patent/EP1837039B1/de not_active Expired - Lifetime
- 2001-05-08 ES ES07011684.3T patent/ES2602452T3/es not_active Expired - Lifetime
- 2001-05-08 EP EP01111013A patent/EP1157706A3/de not_active Ceased
- 2001-05-17 CA CA2348119A patent/CA2348119C/en not_active Expired - Fee Related
- 2001-05-21 AU AU46166/01A patent/AU784520B2/en not_active Ceased
- 2001-05-21 JP JP2001150784A patent/JP2001327592A/ja active Pending
- 2001-05-21 KR KR1020010027633A patent/KR100858226B1/ko not_active Expired - Fee Related
- 2001-05-22 US US09/861,657 patent/US20020001584A1/en not_active Abandoned
Also Published As
| Publication number | Publication date |
|---|---|
| CA2348119C (en) | 2012-01-03 |
| AU4616601A (en) | 2001-11-29 |
| DK1837039T3 (en) | 2016-12-05 |
| CA2348119A1 (en) | 2001-11-22 |
| US20020001584A1 (en) | 2002-01-03 |
| EP1837039A3 (de) | 2011-07-20 |
| AU784520B2 (en) | 2006-04-27 |
| KR20010107601A (ko) | 2001-12-07 |
| ES2602452T3 (es) | 2017-02-21 |
| EP1157706A3 (de) | 2002-03-06 |
| KR100858226B1 (ko) | 2008-09-12 |
| EP1837039B1 (de) | 2016-08-17 |
| JP2001327592A (ja) | 2001-11-27 |
| EP1837039A2 (de) | 2007-09-26 |
| EP1157706A2 (de) | 2001-11-28 |
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