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Volumn 20, Issue 23-24, 1999, Pages 2265-2279

Cellular recognition of synthetic peptide amphiphiles in self-assembled monolayer films

Author keywords

Biomimetic materials; Cell adhesion; Cell spreading; Langmuir Blodgett films; Peptide amphiphiles; RGD

Indexed keywords

AMPHOPHILE; ARGINYLGLYCYLASPARTIC ACID; BIOMATERIAL; COPOLYMER; INTEGRIN RECEPTOR; MEMBRANE RECEPTOR; POLYETHYLENE TEREPHTHALATE; POLYMACON; POLYURETHAN; POLYVINYL ALCOHOL; SCLEROPROTEIN; SYNTHETIC PEPTIDE;

EID: 0032700806     PISSN: 01429612     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0142-9612(99)00157-X     Document Type: Article
Times cited : (117)

References (49)
  • 1
    • 0006416224 scopus 로고
    • Peptide sequences in matrix proteins recognized by adhesion receptors
    • D.H. Rohrbach, & R. Timpl. San Diego: Academic Press
    • Humphries M.J. Peptide sequences in matrix proteins recognized by adhesion receptors. Rohrbach D.H., Timpl R. Molecular and cellular aspects of basement membranes. 1993;289-308 Academic Press, San Diego.
    • (1993) Molecular and Cellular Aspects of Basement Membranes , pp. 289-308
    • Humphries, M.J.1
  • 2
    • 0029775681 scopus 로고    scopus 로고
    • RGD and other recognition sequences for integrins
    • Ruoslahti E. RGD and other recognition sequences for integrins. Ann Rev Cell Dev Biol. 12:1996;697-715.
    • (1996) Ann Rev Cell Dev Biol , vol.12 , pp. 697-715
    • Ruoslahti, E.1
  • 3
    • 0024477452 scopus 로고
    • n-albumin conjugates as a model substratum for integrin-mediated cell adhesion
    • n-albumin conjugates as a model substratum for integrin-mediated cell adhesion. Exp Cell Res. 182:1989;186-196.
    • (1989) Exp Cell Res , vol.182 , pp. 186-196
    • Danilov, Y.N.1    Juliano, R.L.2
  • 4
    • 0029298915 scopus 로고
    • Synthesis and use of a new bromoacetyl-derivatized heterotrifunctional amino acid for conjugation of cyclic RGD-containing peptides derived from human bone sialoprotein
    • Ivanov B., Grzesik W., Robey F.A. Synthesis and use of a new bromoacetyl-derivatized heterotrifunctional amino acid for conjugation of cyclic RGD-containing peptides derived from human bone sialoprotein. Bioconjugate Chem. 6:1995;269-277.
    • (1995) Bioconjugate Chem , vol.6 , pp. 269-277
    • Ivanov, B.1    Grzesik, W.2    Robey, F.A.3
  • 5
    • 0028686661 scopus 로고
    • Cell attachment and motility on materials modified by surface-active RGD-containing peptides
    • Glass J., Blevitt J., Dickerson K., Pierschbacher M., Craig W.S. Cell attachment and motility on materials modified by surface-active RGD-containing peptides. Ann NY Acad Sci. 745:1994;177-186.
    • (1994) Ann NY Acad Sci , vol.745 , pp. 177-186
    • Glass, J.1    Blevitt, J.2    Dickerson, K.3    Pierschbacher, M.4    Craig, W.S.5
  • 7
    • 0025300277 scopus 로고
    • Covalent surface immobilization of Arg-Gly-Asp- And Tyr-Ile-Gly-Ser-Arg-containing peptides to obtain well-defined cell-adhesive substrates
    • Massia S.P., Hubbell J.A. Covalent surface immobilization of Arg-Gly-Asp- and Tyr-Ile-Gly-Ser-Arg-containing peptides to obtain well-defined cell-adhesive substrates. Anal Biochem. 187:1990;292-301.
    • (1990) Anal Biochem , vol.187 , pp. 292-301
    • Massia, S.P.1    Hubbell, J.A.2
  • 8
    • 0025881229 scopus 로고
    • 3-mediated fibroblast spreading and 140 nm for focal contact and stress fiber formation
    • 3 -mediated fibroblast spreading and 140 nm for focal contact and stress fiber formation J Cell Biol. 114:1991;1089-1100.
    • (1991) J Cell Biol , vol.114 , pp. 1089-1100
    • Massia, S.P.1    Hubbell, J.A.2
  • 9
    • 0026114629 scopus 로고
    • Human endothelial cell interactions with surface-coupled adhesion peptides on a nonadhesive glass substrate and two polymeric biomaterials
    • Massia S.P., Hubbell J.A. Human endothelial cell interactions with surface-coupled adhesion peptides on a nonadhesive glass substrate and two polymeric biomaterials. J Biomed Mater Res. 25:1991;223-242.
    • (1991) J Biomed Mater Res , vol.25 , pp. 223-242
    • Massia, S.P.1    Hubbell, J.A.2
  • 10
    • 0026686460 scopus 로고
    • Surface-grafted cell-binding peptides in tissue engineering of the vascular graft
    • Hubbell J.A., Massia S.P., Drumheller P.D. Surface-grafted cell-binding peptides in tissue engineering of the vascular graft. Ann NY Acad Sci. 665:1992;253-258.
    • (1992) Ann NY Acad Sci , vol.665 , pp. 253-258
    • Hubbell, J.A.1    Massia, S.P.2    Drumheller, P.D.3
  • 11
    • 0029958627 scopus 로고    scopus 로고
    • Effect of receptor-ligand affinity on the strength of endothelial cell adhesion
    • Xiao Y., Truskey G.A. Effect of receptor-ligand affinity on the strength of endothelial cell adhesion. Biophys J. 71:1996;2869-2884.
    • (1996) Biophys J , vol.71 , pp. 2869-2884
    • Xiao, Y.1    Truskey, G.A.2
  • 12
    • 0031259844 scopus 로고    scopus 로고
    • The detachment strength and morphology of bone cells contacting materials modified with a peptide sequence found within bone sialoprotein
    • Rezania A., Thomas C.H., Branger A.B., Waters C.M., Healy K.E. The detachment strength and morphology of bone cells contacting materials modified with a peptide sequence found within bone sialoprotein. J Biomed Mater Res. 37:1997;9-19.
    • (1997) J Biomed Mater Res , vol.37 , pp. 9-19
    • Rezania, A.1    Thomas, C.H.2    Branger, A.B.3    Waters, C.M.4    Healy, K.E.5
  • 13
    • 0023687433 scopus 로고
    • Covalent attachment of an Arg-Gly-Asp sequence peptide to derivatizable polyacrylamide surfaces: Support of fibroblast adhesion and long-term growth
    • Brandley B.K., Schnaar R.L. Covalent attachment of an Arg-Gly-Asp sequence peptide to derivatizable polyacrylamide surfaces. support of fibroblast adhesion and long-term growth Anal Biochem. 172:1988;270-278.
    • (1988) Anal Biochem , vol.172 , pp. 270-278
    • Brandley, B.K.1    Schnaar, R.L.2
  • 14
    • 0009501329 scopus 로고
    • Immobilization of a fibronectin fragment at the surface of a polyetherurethane film
    • Breuers W., Klee D., Höcker H., Mittermayer C. Immobilization of a fibronectin fragment at the surface of a polyetherurethane film. J Mater Sci. 2:1991;106-109.
    • (1991) J Mater Sci , vol.2 , pp. 106-109
    • Breuers, W.1    Klee, D.2    Höcker, H.3    Mittermayer, C.4
  • 16
    • 0028347517 scopus 로고
    • Synthesis of hemocompatible materials. Part 1: Surface modification of polyurethanes based on poly(chloroalkylvinylether)s by RGD fragments
    • Sanchez M., Deffieux A., Bordenave L., Baquey C., Fontanille M. Synthesis of hemocompatible materials. Part 1. surface modification of polyurethanes based on poly(chloroalkylvinylether)s by RGD fragments Clin Mater. 15:1994;253-258.
    • (1994) Clin Mater , vol.15 , pp. 253-258
    • Sanchez, M.1    Deffieux, A.2    Bordenave, L.3    Baquey, C.4    Fontanille, M.5
  • 17
    • 0024704946 scopus 로고
    • Development of a novel artificial matrix with cell adhesion peptides for cell culture and artificial and hybrid organs
    • Matsuda T., Kondo A., Makino K., Akutsu T. Development of a novel artificial matrix with cell adhesion peptides for cell culture and artificial and hybrid organs. Trans Am Soc Artif Intern Organs. 35:1989;677-679.
    • (1989) Trans Am Soc Artif Intern Organs , vol.35 , pp. 677-679
    • Matsuda, T.1    Kondo, A.2    Makino, K.3    Akutsu, T.4
  • 18
    • 0026206729 scopus 로고
    • Synthesis and evaluation of oligopeptide RGDS exhibiting cell-attachment activity
    • Hirano Y., Hayashi T., Goto K., Nakajima A. Synthesis and evaluation of oligopeptide RGDS exhibiting cell-attachment activity. Polymer Bulletin. 26:1991;363-370.
    • (1991) Polymer Bulletin , vol.26 , pp. 363-370
    • Hirano, Y.1    Hayashi, T.2    Goto, K.3    Nakajima, A.4
  • 19
    • 0027558326 scopus 로고
    • Two-dimensional artificial extracellular matrix: Bioadhesive peptide-immobilized surface design
    • Kondoh A., Makino K., Matsuda T. Two-dimensional artificial extracellular matrix. bioadhesive peptide-immobilized surface design J Appl Polymer Sci. 47:1993;1983-1988.
    • (1993) J Appl Polymer Sci , vol.47 , pp. 1983-1988
    • Kondoh, A.1    Makino, K.2    Matsuda, T.3
  • 20
    • 0029361095 scopus 로고
    • Photochemical surface derivatization of a peptide containing Arg-Gly-Asp (RGD)
    • Sugawara T., Matsuda T. Photochemical surface derivatization of a peptide containing Arg-Gly-Asp (RGD). J Biomed Mater Res. 29:1995;1047-1052.
    • (1995) J Biomed Mater Res , vol.29 , pp. 1047-1052
    • Sugawara, T.1    Matsuda, T.2
  • 21
    • 0025087925 scopus 로고
    • Covalently attached GRGD on polymer surfaces promotes biospecific adhesion of mammalian cells
    • Massia S.P., Hubbell J.A. Covalently attached GRGD on polymer surfaces promotes biospecific adhesion of mammalian cells. Ann NY Acad Sci. 589:1990;261-270.
    • (1990) Ann NY Acad Sci , vol.589 , pp. 261-270
    • Massia, S.P.1    Hubbell, J.A.2
  • 22
    • 0029862210 scopus 로고    scopus 로고
    • Improved endothelial cell attachment on ePTFE vascular grafts pretreated with synthetic RGD-containing peptides
    • Walluscheck K.P., Steinhoff G., Kelm S., Haverich A. Improved endothelial cell attachment on ePTFE vascular grafts pretreated with synthetic RGD-containing peptides. Eur J Vasc Endovasc Surg. 12:1996;321-330.
    • (1996) Eur J Vasc Endovasc Surg , vol.12 , pp. 321-330
    • Walluscheck, K.P.1    Steinhoff, G.2    Kelm, S.3    Haverich, A.4
  • 23
    • 0026261770 scopus 로고
    • Materials for enhancing cell adhesion by immobilization of cell-adhesive peptide
    • Ito Y., Kajihara M., Imanishi Y. Materials for enhancing cell adhesion by immobilization of cell-adhesive peptide. J Biomed Mater Res. 25:1991;1325-1337.
    • (1991) J Biomed Mater Res , vol.25 , pp. 1325-1337
    • Ito, Y.1    Kajihara, M.2    Imanishi, Y.3
  • 24
    • 0026342146 scopus 로고
    • Synthesis and cell attachment activity of bioactive oligopeptides: RGD, RGDS, RGDV, and RGDT
    • Hirano Y., Kando Y., Hayashi T., Goto K., Nakajima A. Synthesis and cell attachment activity of bioactive oligopeptides. RGD, RGDS, RGDV, and RGDT J Biomed Mater Res. 25:1991;1523-1534.
    • (1991) J Biomed Mater Res , vol.25 , pp. 1523-1534
    • Hirano, Y.1    Kando, Y.2    Hayashi, T.3    Goto, K.4    Nakajima, A.5
  • 25
    • 0027356124 scopus 로고
    • Cell-attachment activities of surface immobilized oligopeptides RGD, RGDS, RGDV, RGDT, and YIGSR towards five cell lines
    • Hirano Y., Okuno M., Hayashi T., Goto K., Nakajima A. Cell-attachment activities of surface immobilized oligopeptides RGD, RGDS, RGDV, RGDT, and YIGSR towards five cell lines. J Biomater Sci Polymer Edn. 4:1993;235-243.
    • (1993) J Biomater Sci Polymer Edn , vol.4 , pp. 235-243
    • Hirano, Y.1    Okuno, M.2    Hayashi, T.3    Goto, K.4    Nakajima, A.5
  • 26
    • 0028116664 scopus 로고
    • Polymer networks with grafted cell adhesion peptides for highly biospecific cell adhesive substrates
    • Drumheller P.D., Hubbell J.A. Polymer networks with grafted cell adhesion peptides for highly biospecific cell adhesive substrates. Anal Biochem. 222:1994;380-388.
    • (1994) Anal Biochem , vol.222 , pp. 380-388
    • Drumheller, P.D.1    Hubbell, J.A.2
  • 27
    • 0032007690 scopus 로고    scopus 로고
    • Incorporation of adhesion peptides into nonadhesive hydrogels useful for tissue resurfacing
    • Hern D.L., Hubbell J.A. Incorporation of adhesion peptides into nonadhesive hydrogels useful for tissue resurfacing. J Biomed Mater Res. 39:1998;266-276.
    • (1998) J Biomed Mater Res , vol.39 , pp. 266-276
    • Hern, D.L.1    Hubbell, J.A.2
  • 28
    • 0029113344 scopus 로고
    • Synthetic lipidation of peptides and amino acids: Monolayer structure and properties
    • Berndt P., Fields G.B., Tirrell M. Synthetic lipidation of peptides and amino acids. monolayer structure and properties J Am Chem Soc. 117:1995;9515-9522.
    • (1995) J Am Chem Soc , vol.117 , pp. 9515-9522
    • Berndt, P.1    Fields, G.B.2    Tirrell, M.3
  • 29
    • 0030482156 scopus 로고    scopus 로고
    • Self-assembling amphiphiles for construction of protein molecular architecture
    • Yu Y.-C., Berndt P., Tirrell M., Fields G.B. Self-assembling amphiphiles for construction of protein molecular architecture. J Am Chem Soc. 118:1996;12515-12520.
    • (1996) J Am Chem Soc , vol.118 , pp. 12515-12520
    • Yu, Y.-C.1    Berndt, P.2    Tirrell, M.3    Fields, G.B.4
  • 30
    • 0030696098 scopus 로고    scopus 로고
    • Construction of biologically active protein molecular architecture using self-assembling peptide-amphiphiles
    • Yu Y.-C., Pakalns T., Dori Y., McCarthy J.B., Tirrell M., Fields G.B. Construction of biologically active protein molecular architecture using self-assembling peptide-amphiphiles. Methods Enzymol. 289:1997;571-587.
    • (1997) Methods Enzymol , vol.289 , pp. 571-587
    • Yu, Y.-C.1    Pakalns, T.2    Dori, Y.3    McCarthy, J.B.4    Tirrell, M.5    Fields, G.B.6
  • 31
    • 0031603860 scopus 로고    scopus 로고
    • Protein-like molecular architecture: Biomaterial applications for inducing cellular receptor binding and signal transduction
    • Fields G.B., Lauer J.L., Dori Y., Forns P., Yu Y.-C., Tirrell M. Protein-like molecular architecture. biomaterial applications for inducing cellular receptor binding and signal transduction Biopolymers. 47:1998;143-151.
    • (1998) Biopolymers , vol.47 , pp. 143-151
    • Fields, G.B.1    Lauer, J.L.2    Dori, Y.3    Forns, P.4    Yu, Y.-C.5    Tirrell, M.6
  • 32
    • 0032494447 scopus 로고    scopus 로고
    • Minimal lipidation stabilizes protein-like molecular architecture
    • Yu Y.-C., Tirrell M., Fields G.B. Minimal lipidation stabilizes protein-like molecular architecture. J Am Chem Soc. 120:1998;9979-9987.
    • (1998) J Am Chem Soc , vol.120 , pp. 9979-9987
    • Yu, Y.-C.1    Tirrell, M.2    Fields, G.B.3
  • 33
    • 0033514426 scopus 로고    scopus 로고
    • Structure and dynamics of peptide-amphiphiles incorporating triple-helical proteinlike molecular architecture
    • Yu Y.-C., Roontga V., Daragan V.A., Mayo K.H., Tirrell M., Fields G.B. Structure and dynamics of peptide-amphiphiles incorporating triple-helical proteinlike molecular architecture. Biochemistry. 38:1999;1659-1668.
    • (1999) Biochemistry , vol.38 , pp. 1659-1668
    • Yu, Y.-C.1    Roontga, V.2    Daragan, V.A.3    Mayo, K.H.4    Tirrell, M.5    Fields, G.B.6
  • 34
    • 0038132116 scopus 로고    scopus 로고
    • Behavior of lipid-modified peptides in membrane-mimetic monolayers at the air/water interface
    • Winger T.M., Chaikof E.L. Behavior of lipid-modified peptides in membrane-mimetic monolayers at the air/water interface. Langmuir. 13:1997;3256-3259.
    • (1997) Langmuir , vol.13 , pp. 3256-3259
    • Winger, T.M.1    Chaikof, E.L.2
  • 35
    • 0030087825 scopus 로고    scopus 로고
    • Lipopeptide conjugates: Biomolecular building blocks for receptor activating membrane-mimetic structures
    • Winger T.M., Ludovice P.J., Chaikof E.L. Lipopeptide conjugates. biomolecular building blocks for receptor activating membrane-mimetic structures Biomaterials. 17:1996;437-441.
    • (1996) Biomaterials , vol.17 , pp. 437-441
    • Winger, T.M.1    Ludovice, P.J.2    Chaikof, E.L.3
  • 36
    • 0026496886 scopus 로고
    • The three-dimensional structure of the tenth type III module of fibronectin: An insight into RGD-mediated interactions
    • Main A.L., Harvey T.S., Baron M., Boyd J., Campbell I.D. The three-dimensional structure of the tenth type III module of fibronectin. an insight into RGD-mediated interactions Cell. 71:1992;671-678.
    • (1992) Cell , vol.71 , pp. 671-678
    • Main, A.L.1    Harvey, T.S.2    Baron, M.3    Boyd, J.4    Campbell, I.D.5
  • 37
    • 0028276559 scopus 로고
    • Crystals of the cell-binding module of fibronectin obtained from a series of recombinant fragments differing in length
    • Dickinson C.D., Gay D.A., Parello J., Ruoslahti E., Ely K.R. Crystals of the cell-binding module of fibronectin obtained from a series of recombinant fragments differing in length. J Mol Biol. 237:1994;123-127.
    • (1994) J Mol Biol , vol.237 , pp. 123-127
    • Dickinson, C.D.1    Gay, D.A.2    Parello, J.3    Ruoslahti, E.4    Ely, K.R.5
  • 38
    • 0001511468 scopus 로고
    • Variants of the cell recognition site of fibronectin that retain attachment-promoting activity
    • Pierschbacher M.D., Ruoslahti E. Variants of the cell recognition site of fibronectin that retain attachment-promoting activity. Proc Natl Acad Sci USA. 81:1984;5985-5988.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 5985-5988
    • Pierschbacher, M.D.1    Ruoslahti, E.2
  • 39
    • 0001400994 scopus 로고
    • Template synthesis of two-dimensional network of cross-linked acrylate polymer in a cast multibilayer film
    • Asakuma S., Okada H., Kunitake T. Template synthesis of two-dimensional network of cross-linked acrylate polymer in a cast multibilayer film. J Am Chem Soc. 113:1991;1749-1755.
    • (1991) J Am Chem Soc , vol.113 , pp. 1749-1755
    • Asakuma, S.1    Okada, H.2    Kunitake, T.3
  • 43
    • 5244297041 scopus 로고
    • C-H stretching modes and the structure of n-alkyl chains. 1. Long, disordered chains
    • Snyder R.G., Strauss H.L., Elliger C.A. C-H stretching modes and the structure of. n -alkyl chains. 1. Long, disordered chains J Phys Chem. 86:1982;5145-5150.
    • (1982) J Phys Chem , vol.86 , pp. 5145-5150
    • Snyder, R.G.1    Strauss, H.L.2    Elliger, C.A.3
  • 45
    • 0026020583 scopus 로고
    • Receptor functions for the integrin VLA-3: Fibronectin, collagen, and laminin binding are differentially influenced by Arg-Gly-Asp peptide and by divalent cations
    • Elices M.J., Urry L.A., Hemler M.E. Receptor functions for the integrin VLA-3. fibronectin, collagen, and laminin binding are differentially influenced by Arg-Gly-Asp peptide and by divalent cations J Cell Biol. 112:1991;169-181.
    • (1991) J Cell Biol , vol.112 , pp. 169-181
    • Elices, M.J.1    Urry, L.A.2    Hemler, M.E.3
  • 47
    • 0032515913 scopus 로고    scopus 로고
    • 1 integrin-mediated signal transduction events: Implications for a collagen structural modulation mechanism of tumor cell invasion
    • 1 integrin-mediated signal transduction events implications for a collagen structural modulation mechanism of tumor cell invasion Biochemistry. 37:1998;5279-5287.
    • (1998) Biochemistry , vol.37 , pp. 5279-5287
    • Lauer, J.L.1    Gendron, C.M.2    Fields, G.B.3
  • 48
    • 0030833050 scopus 로고    scopus 로고
    • Interrelation of motility, cytoskeletal organization and gap junctional communication with invasiveness of melanocytic cells in vitro
    • Helige C., Zellnig G., Hofmann-Wellenhof R., Fink-Puches R., Smolle J., Tritthart H.A. Interrelation of motility, cytoskeletal organization and gap junctional communication with invasiveness of melanocytic cells in vitro. Invasion Metastasis. 17:1997;26-41.
    • (1997) Invasion Metastasis , vol.17 , pp. 26-41
    • Helige, C.1    Zellnig, G.2    Hofmann-Wellenhof, R.3    Fink-Puches, R.4    Smolle, J.5    Tritthart, H.A.6
  • 49
    • 0029026634 scopus 로고
    • Endothelial cell interactions with synthetic peptides from the carboxyl-terminal heparin-binding domains of fibronectin
    • Huebsch J.C., McCarthy J.B., Diglio C.A., Mooradian D.L. Endothelial cell interactions with synthetic peptides from the carboxyl-terminal heparin-binding domains of fibronectin. Circulation Res. 77:1995;43-53.
    • (1995) Circulation Res , vol.77 , pp. 43-53
    • Huebsch, J.C.1    McCarthy, J.B.2    Diglio, C.A.3    Mooradian, D.L.4


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