JP2012140408A - 合成で、規定されたフィブロネクチン模倣ペプチドおよびそれで修飾された表面 - Google Patents
合成で、規定されたフィブロネクチン模倣ペプチドおよびそれで修飾された表面 Download PDFInfo
- Publication number
- JP2012140408A JP2012140408A JP2011269062A JP2011269062A JP2012140408A JP 2012140408 A JP2012140408 A JP 2012140408A JP 2011269062 A JP2011269062 A JP 2011269062A JP 2011269062 A JP2011269062 A JP 2011269062A JP 2012140408 A JP2012140408 A JP 2012140408A
- Authority
- JP
- Japan
- Prior art keywords
- seq
- fibronectin
- absent
- exist
- cell
- 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.)
- Granted
Links
- 108010067306 Fibronectins Proteins 0.000 title claims abstract description 70
- 102000016359 Fibronectins Human genes 0.000 title claims abstract description 70
- 108090000765 processed proteins & peptides Proteins 0.000 title description 9
- 150000001875 compounds Chemical class 0.000 claims abstract description 63
- 238000000576 coating method Methods 0.000 claims description 20
- NTEDOEBWPRVVSG-FQUUOJAGSA-N (2s)-1-[(2r)-2-[[(2s)-2-[[2-[[(2s)-2-[(2-aminoacetyl)amino]-5-(diaminomethylideneamino)pentanoyl]amino]acetyl]amino]-3-carboxypropanoyl]amino]-3-hydroxypropanoyl]pyrrolidine-2-carboxylic acid Chemical compound NC(N)=NCCC[C@H](NC(=O)CN)C(=O)NCC(=O)N[C@@H](CC(O)=O)C(=O)N[C@H](CO)C(=O)N1CCC[C@H]1C(O)=O NTEDOEBWPRVVSG-FQUUOJAGSA-N 0.000 claims description 18
- 108010053299 glycyl-arginyl-glycyl-aspartyl-seryl-proline Proteins 0.000 claims description 18
- 239000011248 coating agent Substances 0.000 claims description 16
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 claims description 5
- 229910052757 nitrogen Inorganic materials 0.000 claims description 5
- 229910052698 phosphorus Inorganic materials 0.000 claims description 4
- 125000003275 alpha amino acid group Chemical group 0.000 claims 3
- 230000003278 mimic effect Effects 0.000 abstract description 9
- 101001027128 Homo sapiens Fibronectin Proteins 0.000 abstract description 4
- 210000004027 cell Anatomy 0.000 description 53
- 150000001413 amino acids Chemical group 0.000 description 25
- 238000004113 cell culture Methods 0.000 description 15
- 235000001014 amino acid Nutrition 0.000 description 13
- 229940024606 amino acid Drugs 0.000 description 13
- 102000010834 Extracellular Matrix Proteins Human genes 0.000 description 12
- 108010037362 Extracellular Matrix Proteins Proteins 0.000 description 12
- 230000021164 cell adhesion Effects 0.000 description 12
- 241001465754 Metazoa Species 0.000 description 7
- 210000001519 tissue Anatomy 0.000 description 7
- 239000002609 medium Substances 0.000 description 5
- 210000002744 extracellular matrix Anatomy 0.000 description 4
- 238000011002 quantification Methods 0.000 description 4
- 238000006467 substitution reaction Methods 0.000 description 4
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 3
- 239000006144 Dulbecco’s modified Eagle's medium Substances 0.000 description 3
- 206010060862 Prostate cancer Diseases 0.000 description 3
- 208000000236 Prostatic Neoplasms Diseases 0.000 description 3
- 230000024245 cell differentiation Effects 0.000 description 3
- 230000010261 cell growth Effects 0.000 description 3
- 230000012292 cell migration Effects 0.000 description 3
- 208000005017 glioblastoma Diseases 0.000 description 3
- 102000006495 integrins Human genes 0.000 description 3
- 108010044426 integrins Proteins 0.000 description 3
- 238000000034 method Methods 0.000 description 3
- 108090000623 proteins and genes Proteins 0.000 description 3
- 230000007480 spreading Effects 0.000 description 3
- 239000000126 substance Substances 0.000 description 3
- 230000001225 therapeutic effect Effects 0.000 description 3
- IYMAXBFPHPZYIK-BQBZGAKWSA-N Arg-Gly-Asp Chemical group NC(N)=NCCC[C@H](N)C(=O)NCC(=O)N[C@@H](CC(O)=O)C(O)=O IYMAXBFPHPZYIK-BQBZGAKWSA-N 0.000 description 2
- 102000008186 Collagen Human genes 0.000 description 2
- 108010035532 Collagen Proteins 0.000 description 2
- 102000009123 Fibrin Human genes 0.000 description 2
- 108010073385 Fibrin Proteins 0.000 description 2
- BWGVNKXGVNDBDI-UHFFFAOYSA-N Fibrin monomer Chemical compound CNC(=O)CNC(=O)CN BWGVNKXGVNDBDI-UHFFFAOYSA-N 0.000 description 2
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 description 2
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 2
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 2
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 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
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 2
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 2
- 238000000719 MTS assay Methods 0.000 description 2
- 231100000070 MTS assay Toxicity 0.000 description 2
- 102000019361 Syndecan Human genes 0.000 description 2
- 108050006774 Syndecan Proteins 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
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 2
- 238000002835 absorbance Methods 0.000 description 2
- 238000004458 analytical method Methods 0.000 description 2
- 230000015572 biosynthetic process Effects 0.000 description 2
- 229920001436 collagen Polymers 0.000 description 2
- 230000001419 dependent effect Effects 0.000 description 2
- 239000003814 drug Substances 0.000 description 2
- 230000000694 effects Effects 0.000 description 2
- 239000012894 fetal calf serum Substances 0.000 description 2
- 229950003499 fibrin Drugs 0.000 description 2
- 230000006870 function 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
- 238000011534 incubation Methods 0.000 description 2
- 230000002401 inhibitory effect Effects 0.000 description 2
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 2
- 229960000310 isoleucine Drugs 0.000 description 2
- 239000000178 monomer Substances 0.000 description 2
- 238000010899 nucleation Methods 0.000 description 2
- 239000000816 peptidomimetic Substances 0.000 description 2
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 2
- 239000013641 positive control Substances 0.000 description 2
- 235000018102 proteins Nutrition 0.000 description 2
- 102000004169 proteins and genes Human genes 0.000 description 2
- 230000011664 signaling Effects 0.000 description 2
- 238000010532 solid phase synthesis reaction Methods 0.000 description 2
- 238000003786 synthesis reaction Methods 0.000 description 2
- 229940124597 therapeutic agent Drugs 0.000 description 2
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 2
- 239000004474 valine Substances 0.000 description 2
- 230000029663 wound healing Effects 0.000 description 2
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 1
- 208000005623 Carcinogenesis Diseases 0.000 description 1
- 206010009944 Colon cancer Diseases 0.000 description 1
- 239000006145 Eagle's minimal essential medium Substances 0.000 description 1
- 102100031812 Fibulin-1 Human genes 0.000 description 1
- 101710170731 Fibulin-1 Proteins 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
- 239000004471 Glycine Substances 0.000 description 1
- 102000003886 Glycoproteins Human genes 0.000 description 1
- 108090000288 Glycoproteins Proteins 0.000 description 1
- 102000008055 Heparan Sulfate Proteoglycans Human genes 0.000 description 1
- 229920002971 Heparan sulfate Polymers 0.000 description 1
- 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 description 1
- 241000282412 Homo Species 0.000 description 1
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 1
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 1
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 1
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 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
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 1
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 1
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 1
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 1
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 description 1
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 1
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 1
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 1
- 239000004472 Lysine Substances 0.000 description 1
- 206010028980 Neoplasm Diseases 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- 239000012980 RPMI-1640 medium Substances 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- 108090000054 Syndecan-2 Proteins 0.000 description 1
- 102000004142 Trypsin Human genes 0.000 description 1
- 108090000631 Trypsin Proteins 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 230000002776 aggregation Effects 0.000 description 1
- 238000004220 aggregation Methods 0.000 description 1
- 235000004279 alanine Nutrition 0.000 description 1
- 230000004075 alteration Effects 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 108010072041 arginyl-glycyl-aspartic acid Proteins 0.000 description 1
- 125000003118 aryl group Chemical group 0.000 description 1
- 235000009582 asparagine Nutrition 0.000 description 1
- 229960001230 asparagine Drugs 0.000 description 1
- 235000003704 aspartic acid Nutrition 0.000 description 1
- 230000008901 benefit Effects 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
- 230000004071 biological effect Effects 0.000 description 1
- 229920001222 biopolymer Polymers 0.000 description 1
- 210000004899 c-terminal region Anatomy 0.000 description 1
- 201000011510 cancer Diseases 0.000 description 1
- 230000004712 cancer cell adhesion Effects 0.000 description 1
- 230000036952 cancer formation Effects 0.000 description 1
- 231100000504 carcinogenesis Toxicity 0.000 description 1
- 230000004663 cell proliferation Effects 0.000 description 1
- 230000005754 cellular signaling Effects 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 208000029742 colonic neoplasm Diseases 0.000 description 1
- 239000000356 contaminant Substances 0.000 description 1
- 238000007796 conventional method Methods 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
- 230000008021 deposition Effects 0.000 description 1
- 239000000539 dimer Substances 0.000 description 1
- 230000013020 embryo development Effects 0.000 description 1
- 210000000981 epithelium Anatomy 0.000 description 1
- 239000012091 fetal bovine serum Substances 0.000 description 1
- 235000013922 glutamic acid Nutrition 0.000 description 1
- 239000004220 glutamic acid Substances 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 230000012010 growth Effects 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 229920000669 heparin Polymers 0.000 description 1
- 229960002897 heparin Drugs 0.000 description 1
- 230000028993 immune response Effects 0.000 description 1
- 230000009851 immunogenic response Effects 0.000 description 1
- 238000012606 in vitro cell culture Methods 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 230000000977 initiatory effect Effects 0.000 description 1
- 230000033001 locomotion Effects 0.000 description 1
- 239000011159 matrix material Substances 0.000 description 1
- 229930182817 methionine Natural products 0.000 description 1
- 230000005012 migration Effects 0.000 description 1
- 238000013508 migration Methods 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- DIOQZVSQGTUSAI-UHFFFAOYSA-N n-butylhexane Natural products CCCCCCCCCC DIOQZVSQGTUSAI-UHFFFAOYSA-N 0.000 description 1
- 239000013642 negative control Substances 0.000 description 1
- 239000008188 pellet Substances 0.000 description 1
- 238000010647 peptide synthesis reaction Methods 0.000 description 1
- 229920001184 polypeptide Polymers 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 102000004196 processed proteins & peptides Human genes 0.000 description 1
- 239000000047 product Substances 0.000 description 1
- 238000004445 quantitative analysis Methods 0.000 description 1
- 238000012207 quantitative assay Methods 0.000 description 1
- 230000001105 regulatory effect Effects 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 102000027257 transmembrane receptors Human genes 0.000 description 1
- 108091008578 transmembrane receptors Proteins 0.000 description 1
- 239000012588 trypsin Substances 0.000 description 1
- 230000000007 visual effect Effects 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
- C07K14/435—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
- 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
- A61L27/00—Materials for grafts or prostheses or for coating grafts or prostheses
- A61L27/36—Materials for grafts or prostheses or for coating grafts or prostheses containing ingredients of undetermined constitution or reaction products thereof, e.g. transplant tissue, natural bone, extracellular matrix
- A61L27/38—Materials for grafts or prostheses or for coating grafts or prostheses containing ingredients of undetermined constitution or reaction products thereof, e.g. transplant tissue, natural bone, extracellular matrix containing added animal cells
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12M—APPARATUS FOR ENZYMOLOGY OR MICROBIOLOGY; APPARATUS FOR CULTURING MICROORGANISMS FOR PRODUCING BIOMASS, FOR GROWING CELLS OR FOR OBTAINING FERMENTATION OR METABOLIC PRODUCTS, i.e. BIOREACTORS OR FERMENTERS
- C12M3/00—Tissue, human, animal or plant cell, or virus culture apparatus
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N5/00—Undifferentiated human, animal or plant cells, e.g. cell lines; Tissues; Cultivation or maintenance thereof; Culture media therefor
- C12N5/0068—General culture methods using substrates
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N2533/00—Supports or coatings for cell culture, characterised by material
- C12N2533/50—Proteins
- C12N2533/52—Fibronectin; Laminin
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Zoology (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Biomedical Technology (AREA)
- Medicinal Chemistry (AREA)
- Biochemistry (AREA)
- Wood Science & Technology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Biotechnology (AREA)
- Cell Biology (AREA)
- Molecular Biology (AREA)
- Biophysics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Epidemiology (AREA)
- Dermatology (AREA)
- Public Health (AREA)
- Transplantation (AREA)
- Microbiology (AREA)
- Gastroenterology & Hepatology (AREA)
- Toxicology (AREA)
- Veterinary Medicine (AREA)
- Oral & Maxillofacial Surgery (AREA)
- Animal Behavior & Ethology (AREA)
- General Engineering & Computer Science (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Botany (AREA)
- Virology (AREA)
- Sustainable Development (AREA)
- Peptides Or Proteins (AREA)
- Materials For Medical Uses (AREA)
- Polymers & Plastics (AREA)
Abstract
【解決手段】柔軟なリンカーで接ぎ合わされたフィブロネクチン細胞結合性ドメインの少なくとも2つの領域を含む化合物。領域は、フィブロネクチンの1または複数の機能的特徴を模倣する様式で互いに相互作用し、このような化合物で被覆された表面は、フィブロネクチンで被覆された表面の細胞接着を模倣する。
【選択図】図1
Description
本出願は、その内容が参照により本明細書に組み込まれている、2010年12月8日に出願した米国仮出願第61/420,818号の利益を主張するものである。
Claims (18)
- 柔軟なリンカーで接ぎ合わされたフィブロネクチン細胞結合性ドメインの少なくとも2つの領域を含む化合物であって、
少なくとも1つの領域は、アミノ酸配列GRGDSP(配列番号1)を含み、
別の領域は、X1X2X3X4X5X6X7X8X9X10X11X12X13RX15PX17SRNX21X22TLTX26(配列番号2)を含み、式中、
X1はKを表すかまたは存在せず、
X2はKを表すかまたは存在せず、
X3はKを表すかまたは存在せず、
X4はKを表すかまたは存在せず、
X5はKを表すかまたは存在せず、
X6はKを表すかまたは存在せず、
X7はS、V、A、Gを表すかまたは存在せず、
X8はG、Aを表すかまたは存在せず、
X9はRまたはGを表し、
X10はP、A、QまたはGを表し、
X11はRまたはKを表し、
X12はE、Q、W、AまたはGを表し、
X13はDまたはEを表し、
X15はV、LまたはIを表し、
X17はHまたはPを表し、
X21はS、TまたはGを表し、
X22はIまたはLを表し、
X26はNまたはHを表す
ことを特徴とする化合物。 - X7は、Sを表すことを特徴とする請求項1に記載の化合物。
- X8は、Gを表すことを特徴とする請求項2に記載の化合物。
- X9は、Rを表すことを特徴とする請求項3に記載の化合物。
- X10は、GまたはAを表すことを特徴とする請求項4に記載の化合物。
- X11は、Rを表すことを特徴とする請求項5に記載の化合物。
- X12は、E、AまたはGを表すことを特徴とする請求項6に記載の化合物。
- X13は、Dを表すことを特徴とする請求項7に記載の化合物。
- X15は、Vを表すことを特徴とする請求項8に記載の化合物。
- X17は、Hを表すことを特徴とする請求項9に記載の化合物。
- X22は、Iを表すことを特徴とする請求項10に記載の化合物。
- X26は、Nを表すことを特徴とする請求項11に記載の化合物。
- 前記柔軟なリンカーは、アミノ酸配列SGSGSGSGS(配列番号3)、GGSGGSGGS(配列番号4)、SGTGSGTGS(配列番号5)またはGGGSGGGSGG(配列番号6)を含むことを特徴とする請求項1に記載の化合物。
- 前記柔軟なリンカーは、アミノ酸配列SGSGSGSGS(配列番号3)、GGSGGSGGS(配列番号4)、SGTGSGTGS(配列番号5)またはGGGSGGGSGG(配列番号6)を含むことを特徴とする請求項12に記載の化合物。
- 少なくとも一部分は、請求項1に記載の被覆を表面上に含むことを特徴とする表面。
- 少なくとも一部分は、請求項14に記載の被覆を表面上に含むことを特徴とする表面。
- フィブロネクチンで被覆された表面の1または複数の機能的特徴を模倣することを特徴とする請求項15に記載の表面。
- その上に請求項17に記載の表面を含むことを特徴とする組成物。
Applications Claiming Priority (4)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
US42081810P | 2010-12-08 | 2010-12-08 | |
US61/420,818 | 2010-12-08 | ||
US13/309,756 | 2011-12-02 | ||
US13/309,756 US8921516B2 (en) | 2010-12-08 | 2011-12-02 | Synthetic, defined fibronectin mimetic peptides and surfaces modified with the same |
Publications (2)
Publication Number | Publication Date |
---|---|
JP2012140408A true JP2012140408A (ja) | 2012-07-26 |
JP5996865B2 JP5996865B2 (ja) | 2016-09-21 |
Family
ID=45093544
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP2011269062A Expired - Fee Related JP5996865B2 (ja) | 2010-12-08 | 2011-12-08 | 合成で、規定されたフィブロネクチン模倣ペプチドおよびそれで修飾された表面 |
Country Status (7)
Country | Link |
---|---|
US (1) | US8921516B2 (ja) |
EP (1) | EP2463301B1 (ja) |
JP (1) | JP5996865B2 (ja) |
KR (1) | KR101976207B1 (ja) |
CN (1) | CN102585014A (ja) |
CA (1) | CA2760924C (ja) |
PT (1) | PT2463301E (ja) |
Families Citing this family (19)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
ES2513866T3 (es) | 2009-05-13 | 2014-10-27 | Sio2 Medical Products, Inc. | Revestimiento e inspección de recipientes |
WO2013170052A1 (en) | 2012-05-09 | 2013-11-14 | Sio2 Medical Products, Inc. | Saccharide protective coating for pharmaceutical package |
US9458536B2 (en) | 2009-07-02 | 2016-10-04 | Sio2 Medical Products, Inc. | PECVD coating methods for capped syringes, cartridges and other articles |
US11624115B2 (en) | 2010-05-12 | 2023-04-11 | Sio2 Medical Products, Inc. | Syringe with PECVD lubrication |
US9878101B2 (en) | 2010-11-12 | 2018-01-30 | Sio2 Medical Products, Inc. | Cyclic olefin polymer vessels and vessel coating methods |
US9272095B2 (en) | 2011-04-01 | 2016-03-01 | Sio2 Medical Products, Inc. | Vessels, contact surfaces, and coating and inspection apparatus and methods |
CN102351946A (zh) * | 2011-10-12 | 2012-02-15 | 中国药科大学 | 一组多聚促愈合肽 |
US11116695B2 (en) | 2011-11-11 | 2021-09-14 | Sio2 Medical Products, Inc. | Blood sample collection tube |
CN103930595A (zh) | 2011-11-11 | 2014-07-16 | Sio2医药产品公司 | 用于药物包装的钝化、pH保护性或润滑性涂层、涂布方法以及设备 |
WO2014071061A1 (en) | 2012-11-01 | 2014-05-08 | Sio2 Medical Products, Inc. | Coating inspection method |
US9903782B2 (en) | 2012-11-16 | 2018-02-27 | Sio2 Medical Products, Inc. | Method and apparatus for detecting rapid barrier coating integrity characteristics |
US9764093B2 (en) | 2012-11-30 | 2017-09-19 | Sio2 Medical Products, Inc. | Controlling the uniformity of PECVD deposition |
AU2013352436B2 (en) | 2012-11-30 | 2018-10-25 | Sio2 Medical Products, Inc. | Controlling the uniformity of PECVD deposition on medical syringes, cartridges, and the like |
EP2961858B1 (en) | 2013-03-01 | 2022-09-07 | Si02 Medical Products, Inc. | Coated syringe. |
CN110074968B (zh) | 2013-03-11 | 2021-12-21 | Sio2医药产品公司 | 涂布包装材料 |
US9937099B2 (en) | 2013-03-11 | 2018-04-10 | Sio2 Medical Products, Inc. | Trilayer coated pharmaceutical packaging with low oxygen transmission rate |
WO2014144926A1 (en) | 2013-03-15 | 2014-09-18 | Sio2 Medical Products, Inc. | Coating method |
EP3693493A1 (en) | 2014-03-28 | 2020-08-12 | SiO2 Medical Products, Inc. | Antistatic coatings for plastic vessels |
EP3337915B1 (en) | 2015-08-18 | 2021-11-03 | SiO2 Medical Products, Inc. | Pharmaceutical and other packaging with low oxygen transmission rate |
Citations (8)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JPH0297397A (ja) * | 1988-06-30 | 1990-04-09 | Takara Shuzo Co Ltd | 細胞接着活性ポリペプチド |
JPH02502261A (ja) * | 1987-11-09 | 1990-07-26 | チロン・オフサルミックス・インコーポレイテッド | 人工器官デバイスの移植 |
JPH03127742A (ja) * | 1989-10-13 | 1991-05-30 | Takara Shuzo Co Ltd | 癌転移抑制剤 |
JPH07504812A (ja) * | 1991-12-05 | 1995-06-01 | ザ スクリップス リサーチ インスティテュート | 細胞付着を促進するための新規なポリペプチド |
JP2001503265A (ja) * | 1996-10-25 | 2001-03-13 | ジー.ディー.サール アンド カンパニー | 新規なflt3受容体アゴニスト |
JP2006087396A (ja) * | 2004-09-27 | 2006-04-06 | National Institute For Environmental Studies | 細胞培養基質及びその製造方法 |
JP2010530222A (ja) * | 2007-06-06 | 2010-09-09 | べーリンガー インゲルハイム インターナショナル ゲーエムベーハー | ナトリウム利尿融合タンパク質 |
JP2012120531A (ja) * | 2010-12-08 | 2012-06-28 | Becton Dickinson & Co | 合成で、規定されたコラーゲン模倣表面を用いる細胞培養の方法 |
Family Cites Families (6)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US5019646A (en) | 1987-08-25 | 1991-05-28 | Regents Of The University Of Minnesota | Polypeptides with fibronectin activity |
US5171318A (en) | 1987-11-09 | 1992-12-15 | Chiron Ophthalmics, Inc. | Treated corneal prosthetic device |
US5773574A (en) | 1990-12-03 | 1998-06-30 | The Scripps Research Institute | Polypeptides for promoting cell attachment |
US6331409B1 (en) * | 1996-11-21 | 2001-12-18 | The Regents Of The University Of Michigan | Methods and compositions for wound healing |
US20040062882A1 (en) * | 2002-09-30 | 2004-04-01 | Andrea Liebmann-Vinson | Cell adhesion resisting surfaces |
WO2008008523A1 (en) * | 2006-07-14 | 2008-01-17 | Regents Of The University Of Minnesota | COMPOUNDS THAT BIND α5β1 INTEGRIN AND METHODS OF USE |
-
2011
- 2011-12-02 US US13/309,756 patent/US8921516B2/en active Active
- 2011-12-05 EP EP11191960.1A patent/EP2463301B1/en active Active
- 2011-12-05 PT PT111919601T patent/PT2463301E/pt unknown
- 2011-12-06 CA CA2760924A patent/CA2760924C/en active Active
- 2011-12-08 JP JP2011269062A patent/JP5996865B2/ja not_active Expired - Fee Related
- 2011-12-08 KR KR1020110130808A patent/KR101976207B1/ko active IP Right Grant
- 2011-12-08 CN CN2011104625501A patent/CN102585014A/zh active Pending
Patent Citations (8)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JPH02502261A (ja) * | 1987-11-09 | 1990-07-26 | チロン・オフサルミックス・インコーポレイテッド | 人工器官デバイスの移植 |
JPH0297397A (ja) * | 1988-06-30 | 1990-04-09 | Takara Shuzo Co Ltd | 細胞接着活性ポリペプチド |
JPH03127742A (ja) * | 1989-10-13 | 1991-05-30 | Takara Shuzo Co Ltd | 癌転移抑制剤 |
JPH07504812A (ja) * | 1991-12-05 | 1995-06-01 | ザ スクリップス リサーチ インスティテュート | 細胞付着を促進するための新規なポリペプチド |
JP2001503265A (ja) * | 1996-10-25 | 2001-03-13 | ジー.ディー.サール アンド カンパニー | 新規なflt3受容体アゴニスト |
JP2006087396A (ja) * | 2004-09-27 | 2006-04-06 | National Institute For Environmental Studies | 細胞培養基質及びその製造方法 |
JP2010530222A (ja) * | 2007-06-06 | 2010-09-09 | べーリンガー インゲルハイム インターナショナル ゲーエムベーハー | ナトリウム利尿融合タンパク質 |
JP2012120531A (ja) * | 2010-12-08 | 2012-06-28 | Becton Dickinson & Co | 合成で、規定されたコラーゲン模倣表面を用いる細胞培養の方法 |
Also Published As
Publication number | Publication date |
---|---|
US8921516B2 (en) | 2014-12-30 |
JP5996865B2 (ja) | 2016-09-21 |
CA2760924A1 (en) | 2012-06-08 |
US20120149871A1 (en) | 2012-06-14 |
CA2760924C (en) | 2019-11-26 |
KR20120064050A (ko) | 2012-06-18 |
EP2463301B1 (en) | 2015-02-18 |
KR101976207B1 (ko) | 2019-05-07 |
CN102585014A (zh) | 2012-07-18 |
EP2463301A1 (en) | 2012-06-13 |
PT2463301E (pt) | 2015-05-18 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
JP5996865B2 (ja) | 合成で、規定されたフィブロネクチン模倣ペプチドおよびそれで修飾された表面 | |
Mas-Moruno et al. | Novel peptide-based platform for the dual presentation of biologically active peptide motifs on biomaterials | |
Ravi et al. | Maleimide–thiol coupling of a bioactive peptide to an elastin-like protein polymer | |
Cutler et al. | Engineering cell adhesive surfaces that direct integrin α5β1 binding using a recombinant fragment of fibronectin | |
Nishiyama et al. | Type XII and XIV collagens mediate interactions between banded collagen fibers in vitro and may modulate extracellular matrix deformability. | |
Andrade et al. | Improving the affinity of fibroblasts for bacterial cellulose using carbohydrate‐binding modules fused to RGD | |
JP5858411B2 (ja) | コラーゲン結合性分子を付加した改変ラミニンおよびその利用 | |
Krishna et al. | Integrin-mediated adhesion and proliferation of human MSCs elicited by a hydroxyproline-lacking, collagen-like peptide | |
Fischer et al. | Concerted action of tenascin-C domains in cell adhesion, anti-adhesion and promotion of neurite outgrowth | |
Roy et al. | Recombinant fibronectin matrix mimetics specify integrin adhesion and extracellular matrix assembly | |
Roy et al. | Chimeric fibronectin matrix mimetic as a functional growth-and migration-promoting adhesive substrate | |
Jeon et al. | Functional enhancement of neuronal cell behaviors and differentiation by elastin-mimetic recombinant protein presenting Arg-Gly-Asp peptides | |
Hozumi et al. | Cell adhesive peptide screening of the mouse laminin α1 chain G domain | |
Sato-Nishiuchi et al. | Recombinant laminin fragments endowed with collagen-binding activity: A tool for conferring laminin-like cell-adhesive activity to collagen matrices | |
Elefteriou et al. | Cell adhesion to tenascin‐X: Mapping of cell adhesion sites and identification of integrin receptors | |
Mochizuki et al. | Integrin‐dependent cell behavior on ECM peptide‐conjugated chitosan membranes | |
Rapuano et al. | Osteoblast‐like cell adhesion to bone sialoprotein peptides | |
CN106715675B (zh) | 包被固体支持物的方法 | |
Peterson et al. | Covalent capture of a collagen mimetic peptide with an integrin-binding motif | |
WO2017034211A1 (ko) | 무기물 표면 접착 또는 코팅용 단백질 접착제 | |
Marko et al. | A novel synthetic peptide polymer with cyclic RGD motifs supports serum-free attachment of anchorage-dependent cells | |
Hozumi et al. | Mixed fibronectin-derived peptides conjugated to a chitosan matrix effectively promotes biological activities through integrins, α4β1, α5β1, αvβ3, and syndecan | |
Park et al. | Bio-functionalization and in-vitro evaluation of titanium surface with recombinant fibronectin and elastin fragment in human mesenchymal stem cell | |
JP2012120531A (ja) | 合成で、規定されたコラーゲン模倣表面を用いる細胞培養の方法 | |
US9193779B2 (en) | Recombinant human fibronectin fragment for cell culture |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A821 Effective date: 20131022 |
|
A711 | Notification of change in applicant |
Free format text: JAPANESE INTERMEDIATE CODE: A711 Effective date: 20131022 |
|
RD02 | Notification of acceptance of power of attorney |
Free format text: JAPANESE INTERMEDIATE CODE: A7422 Effective date: 20131022 |
|
A621 | Written request for application examination |
Free format text: JAPANESE INTERMEDIATE CODE: A621 Effective date: 20141208 |
|
A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20151124 |
|
A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20160224 |
|
A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20160324 |
|
TRDD | Decision of grant or rejection written | ||
A01 | Written decision to grant a patent or to grant a registration (utility model) |
Free format text: JAPANESE INTERMEDIATE CODE: A01 Effective date: 20160726 |
|
A61 | First payment of annual fees (during grant procedure) |
Free format text: JAPANESE INTERMEDIATE CODE: A61 Effective date: 20160825 |
|
R150 | Certificate of patent or registration of utility model |
Ref document number: 5996865 Country of ref document: JP Free format text: JAPANESE INTERMEDIATE CODE: R150 |
|
R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
LAPS | Cancellation because of no payment of annual fees |