메뉴 건너뛰기




Volumn 85, Issue 1, 2013, Pages 69-77

Tuning peptide affinity for biofunctionalized surfaces

Author keywords

Bioinert; Biomaterial; Biomimetic; GEPI; Immobilization; Mussel; Peptide; Phage display; Surface coating

Indexed keywords

BONE MORPHOGENETIC PROTEIN 2; DOPA; FIBROBLAST GROWTH FACTOR 2; INTEGRIN; PEPTIDE; STROMAL CELL DERIVED FACTOR 1ALPHA; TRANSFORMING GROWTH FACTOR BETA; VASCULOTROPIN;

EID: 84882943538     PISSN: 09396411     EISSN: 18733441     Source Type: Journal    
DOI: 10.1016/j.ejpb.2013.02.006     Document Type: Article
Times cited : (13)

References (119)
  • 1
    • 0018346438 scopus 로고
    • Magnetite in freshwater magnetotactic bacteria
    • R.B. Frankel, R.P. Blakemore, and R.S. Wolfe Magnetite in freshwater magnetotactic bacteria Science 203 1979 1355 1356
    • (1979) Science , vol.203 , pp. 1355-1356
    • Frankel, R.B.1    Blakemore, R.P.2    Wolfe, R.S.3
  • 4
    • 77950789209 scopus 로고    scopus 로고
    • Holding on by a hard-shell thread
    • P.B. Messersmith Holding on by a hard-shell thread Science 328 2010 180 181
    • (2010) Science , vol.328 , pp. 180-181
    • Messersmith, P.B.1
  • 6
    • 0023438761 scopus 로고
    • Tissue-biomaterial interactions
    • D.F. Williams Tissue-biomaterial interactions J. Mater. Sci. 22 1987 3421 3445
    • (1987) J. Mater. Sci. , vol.22 , pp. 3421-3445
    • Williams, D.F.1
  • 7
    • 0035797979 scopus 로고    scopus 로고
    • Self-assembled monolayers that resist the adsorption of proteins and the adhesion of bacterial and mammalian cells
    • E. Ostuni, R.G. Chapman, M.N. Liang, G. Meluleni, G. Pier, D.E. Ingber, and G.M. Whitesides Self-assembled monolayers that resist the adsorption of proteins and the adhesion of bacterial and mammalian cells Langmuir 17 2001 6336 6343
    • (2001) Langmuir , vol.17 , pp. 6336-6343
    • Ostuni, E.1    Chapman, R.G.2    Liang, M.N.3    Meluleni, G.4    Pier, G.5    Ingber, D.E.6    Whitesides, G.M.7
  • 9
    • 0029556388 scopus 로고
    • Stability and self-exchange in alkanethiol monolayers
    • J.B. Schlenoff, M. Li, and H. Ly Stability and self-exchange in alkanethiol monolayers J. Am. Chem. Soc. 117 1995 12528 12536
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 12528-12536
    • Schlenoff, J.B.1    Li, M.2    Ly, H.3
  • 10
    • 35348945857 scopus 로고    scopus 로고
    • Mussel-inspired surface chemistry for multifunctional coatings
    • H. Lee, S.M. Dellatore, W.M. Miller, and P.B. Messersmith Mussel-inspired surface chemistry for multifunctional coatings Science 318 2007 426 430
    • (2007) Science , vol.318 , pp. 426-430
    • Lee, H.1    Dellatore, S.M.2    Miller, W.M.3    Messersmith, P.B.4
  • 11
    • 84858394503 scopus 로고    scopus 로고
    • Biocompatible and bioactive surface modifications for prolonged in vivo efficacy
    • S.R. Meyers, and M.W. Grinstaff Biocompatible and bioactive surface modifications for prolonged in vivo efficacy Chem. Rev. 112 2012 1615 1632
    • (2012) Chem. Rev. , vol.112 , pp. 1615-1632
    • Meyers, S.R.1    Grinstaff, M.W.2
  • 12
    • 0021818675 scopus 로고
    • Filamentous fusion phage - Novel expression vectors that display cloned antigens on the virion surface
    • G.P. Smith Filamentous fusion phage - novel expression vectors that display cloned antigens on the virion surface Science 228 1985 1315 1317
    • (1985) Science , vol.228 , pp. 1315-1317
    • Smith, G.P.1
  • 13
    • 0028926048 scopus 로고
    • Protein-protein interactions - Methods for detection and analysis
    • E.M. Phizicky, and S. Fields Protein-protein interactions - methods for detection and analysis Microbiol. Rev. 59 1995 94 123
    • (1995) Microbiol. Rev. , vol.59 , pp. 94-123
    • Phizicky, E.M.1    Fields, S.2
  • 15
    • 0026669435 scopus 로고
    • Engineered iron oxide-adhesion mutants of the Escherichia coli phage lambda receptor
    • S. Brown Engineered iron oxide-adhesion mutants of the Escherichia coli phage lambda receptor Proc. Natl. Acad. Sci. USA 89 1992 8651 8655
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 8651-8655
    • Brown, S.1
  • 16
    • 0030969778 scopus 로고    scopus 로고
    • Metal-recognition by repeating polypeptides
    • S. Brown Metal-recognition by repeating polypeptides Nat. Biotechnol. 15 1997 269 272
    • (1997) Nat. Biotechnol. , vol.15 , pp. 269-272
    • Brown, S.1
  • 17
    • 0034621827 scopus 로고    scopus 로고
    • Selection of peptides with semiconductor binding specificity for directed nanocrystal assembly
    • S.R. Whaley, D.S. English, E.L. Hu, P.F. Barbara, and A.M. Belcher Selection of peptides with semiconductor binding specificity for directed nanocrystal assembly Nature 405 2000 665 668
    • (2000) Nature , vol.405 , pp. 665-668
    • Whaley, S.R.1    English, D.S.2    Hu, E.L.3    Barbara, P.F.4    Belcher, A.M.5
  • 19
    • 0028947997 scopus 로고
    • Expression of thioredoxin random peptide libraries on the Escherichia coli cell surface as functional fusions to flagellin: A system designed for exploring protein-protein interactions
    • Z.J. Lu, K.S. Murray, V. Vancleave, E.R. Lavallie, M.L. Stahl, and J.M. McCoy Expression of thioredoxin random peptide libraries on the Escherichia coli cell surface as functional fusions to flagellin: a system designed for exploring protein-protein interactions Bio-Technology 13 1995 366 372
    • (1995) Bio-Technology , vol.13 , pp. 366-372
    • Lu, Z.J.1    Murray, K.S.2    Vancleave, V.3    Lavallie, E.R.4    Stahl, M.L.5    McCoy, J.M.6
  • 21
    • 79952120224 scopus 로고    scopus 로고
    • Material binding peptides for nanotechnology
    • U.O.S. Seker, and H.V. Demir Material binding peptides for nanotechnology Molecules 16 2011 1426 1451
    • (2011) Molecules , vol.16 , pp. 1426-1451
    • Seker, U.O.S.1    Demir, H.V.2
  • 23
    • 34548530712 scopus 로고    scopus 로고
    • Selection and analysis of solid-binding peptides
    • F. Baneyx, and D.T. Schwartz Selection and analysis of solid-binding peptides Curr. Opin. Biotechnol. 18 2007 312 317
    • (2007) Curr. Opin. Biotechnol. , vol.18 , pp. 312-317
    • Baneyx, F.1    Schwartz, D.T.2
  • 24
    • 36249002371 scopus 로고    scopus 로고
    • Conformational control of inorganic adhesion in a designer protein engineered for cuprous oxide binding
    • W.S. Choe, M.S.R. Sastry, C.K. Thai, H. Dai, D.T. Schwartz, and F. Baneyx Conformational control of inorganic adhesion in a designer protein engineered for cuprous oxide binding Langmuir 23 2007 11347 11350
    • (2007) Langmuir , vol.23 , pp. 11347-11350
    • Choe, W.S.1    Sastry, M.S.R.2    Thai, C.K.3    Dai, H.4    Schwartz, D.T.5    Baneyx, F.6
  • 25
    • 0025112794 scopus 로고
    • Searching for peptide ligands with an epitope library
    • J.K. Scott, and G.P. Smith Searching for peptide ligands with an epitope library Science 249 1990 386 390
    • (1990) Science , vol.249 , pp. 386-390
    • Scott, J.K.1    Smith, G.P.2
  • 26
    • 0027946232 scopus 로고
    • Isolation of a peptide antagonist to the thrombin receptor using phage display
    • J. Doorbar, and G. Winter Isolation of a peptide antagonist to the thrombin receptor using phage display J. Mol. Biol. 244 1994 361 369
    • (1994) J. Mol. Biol. , vol.244 , pp. 361-369
    • Doorbar, J.1    Winter, G.2
  • 27
    • 34547583175 scopus 로고    scopus 로고
    • Peptide tags for enhanced cellular and protein adhesion to single-crystal line sapphire
    • E.M. Krauland, B.R. Peelle, K.D. Wittrup, and A.M. Belcher Peptide tags for enhanced cellular and protein adhesion to single-crystal line sapphire Biotechnol. Bioeng. 97 2007 1009 1020
    • (2007) Biotechnol. Bioeng. , vol.97 , pp. 1009-1020
    • Krauland, E.M.1    Peelle, B.R.2    Wittrup, K.D.3    Belcher, A.M.4
  • 28
    • 32244448431 scopus 로고    scopus 로고
    • Endowing a ferritin-like cage protein with high affinity and selectivity for certain inorganic materials
    • K. Sano, K. Ajima, K. Iwahori, M. Yudasaka, S. Iijima, I. Yamashita, and K. Shiba Endowing a ferritin-like cage protein with high affinity and selectivity for certain inorganic materials Small 1 2005 826 832
    • (2005) Small , vol.1 , pp. 826-832
    • Sano, K.1    Ajima, K.2    Iwahori, K.3    Yudasaka, M.4    Iijima, S.5    Yamashita, I.6    Shiba, K.7
  • 29
    • 64149118082 scopus 로고    scopus 로고
    • Quantitative affinity of genetically engineered repeating polypeptides to inorganic surfaces
    • U.O.S. Seker, B. Wilson, D. Sahin, C. Tamerler, and M. Sarikaya Quantitative affinity of genetically engineered repeating polypeptides to inorganic surfaces Biomacromolecules 10 2009 250 257
    • (2009) Biomacromolecules , vol.10 , pp. 250-257
    • Seker, U.O.S.1    Wilson, B.2    Sahin, D.3    Tamerler, C.4    Sarikaya, M.5
  • 30
    • 61549090001 scopus 로고    scopus 로고
    • Context-dependent adsorption behavior of cyclic and linear peptides on metal oxide surfaces
    • H. Chen, X. Su, K.-G. Neoh, and W.-S. Choe Context-dependent adsorption behavior of cyclic and linear peptides on metal oxide surfaces Langmuir 25 2008 1588 1593
    • (2008) Langmuir , vol.25 , pp. 1588-1593
    • Chen, H.1    Su, X.2    Neoh, K.-G.3    Choe, W.-S.4
  • 32
    • 9744243512 scopus 로고    scopus 로고
    • Binding specificity of a peptide on semiconductor surfaces
    • K. Goede, P. Busch, and M. Grundmann Binding specificity of a peptide on semiconductor surfaces Nano Lett. 4 2004 2115 2120
    • (2004) Nano Lett. , vol.4 , pp. 2115-2120
    • Goede, K.1    Busch, P.2    Grundmann, M.3
  • 33
    • 84861667865 scopus 로고    scopus 로고
    • Screening for silver nanoparticle-binding peptides by using a peptide array
    • M. Kuboyama, R. Kato, M. Okochi, and H. Honda Screening for silver nanoparticle-binding peptides by using a peptide array Biochem. Eng. J. 66 2012 73 77
    • (2012) Biochem. Eng. J. , vol.66 , pp. 73-77
    • Kuboyama, M.1    Kato, R.2    Okochi, M.3    Honda, H.4
  • 34
    • 84867529434 scopus 로고    scopus 로고
    • Biocompatible silicon surfaces through orthogonal click chemistries and a high affinity silicon oxide binding peptide
    • R. Hassert, M. Pagel, Z. Ming, T. Häupl, B. Abel, K. Braun, M. Wiessler, and A.G. Beck-Sickinger Biocompatible silicon surfaces through orthogonal click chemistries and a high affinity silicon oxide binding peptide Bioconjugate Chem. 23 2012 2129 2137
    • (2012) Bioconjugate Chem. , vol.23 , pp. 2129-2137
    • Hassert, R.1    Pagel, M.2    Ming, Z.3    Häupl, T.4    Abel, B.5    Braun, K.6    Wiessler, M.7    Beck-Sickinger, A.G.8
  • 37
    • 0344012217 scopus 로고    scopus 로고
    • A hexapeptide motif that electrostatically binds to the surface of titanium
    • K.I. Sano, and K. Shiba A hexapeptide motif that electrostatically binds to the surface of titanium J. Am. Chem. Soc. 125 2003 14234 14235
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 14234-14235
    • Sano, K.I.1    Shiba, K.2
  • 38
    • 16244366831 scopus 로고    scopus 로고
    • Specificity and biomineralization activities of Ti-binding peptide-1 (tbp-1)
    • K.I. Sano, H. Sasaki, and K. Shiba Specificity and biomineralization activities of Ti-binding peptide-1 (tbp-1) Langmuir 21 2005 3090 3095
    • (2005) Langmuir , vol.21 , pp. 3090-3095
    • Sano, K.I.1    Sasaki, H.2    Shiba, K.3
  • 40
    • 21044458558 scopus 로고    scopus 로고
    • Peptide aptamers: Recent developments for cancer therapy
    • C. Borghouts, C. Kunz, and B. Groner Peptide aptamers: recent developments for cancer therapy Expert Opin. Biol. Ther. 5 2005 783 797
    • (2005) Expert Opin. Biol. Ther. , vol.5 , pp. 783-797
    • Borghouts, C.1    Kunz, C.2    Groner, B.3
  • 44
    • 78649852683 scopus 로고    scopus 로고
    • Chemical modifications designed to improve peptide stability: Incorporation of non-natural amino acids, pseudo-peptide bonds, and cyclization
    • L. Gentilucci, R. De Marco, and L. Cerisoli Chemical modifications designed to improve peptide stability: incorporation of non-natural amino acids, pseudo-peptide bonds, and cyclization Curr. Pharm. Des. 16 2010 3185 3203
    • (2010) Curr. Pharm. Des. , vol.16 , pp. 3185-3203
    • Gentilucci, L.1    De Marco, R.2    Cerisoli, L.3
  • 45
    • 77957943568 scopus 로고    scopus 로고
    • Staphylococcus aureus resistance on titanium coated with multivalent pegylated-peptides
    • X. Khoo, G.A. O'Toole, S.A. Nair, B.D. Snyder, D.J. Kenan, and M.W. Grinstaff Staphylococcus aureus resistance on titanium coated with multivalent pegylated-peptides Biomaterials 31 2010 9285 9292
    • (2010) Biomaterials , vol.31 , pp. 9285-9292
    • Khoo, X.1    O'Toole, G.A.2    Nair, S.A.3    Snyder, B.D.4    Kenan, D.J.5    Grinstaff, M.W.6
  • 48
    • 0019499337 scopus 로고
    • Polyphenolic substance of Mytilus edulis: Novel adhesive containing L-DOPA and hydroxyproline
    • J.H. Waite, and M.L. Tanzer Polyphenolic substance of Mytilus edulis: novel adhesive containing L-DOPA and hydroxyproline Science 212 1981 1038 1040
    • (1981) Science , vol.212 , pp. 1038-1040
    • Waite, J.H.1    Tanzer, M.L.2
  • 49
    • 0021099316 scopus 로고
    • Evidence for a repeating 3,4-dihydroxyphenylalanine- and hydroxyproline-containing decapeptide in the adhesive protein of the mussel, Mytilus edulis L
    • J.H. Waite Evidence for a repeating 3,4-dihydroxyphenylalanine- and hydroxyproline-containing decapeptide in the adhesive protein of the mussel, Mytilus edulis L J. Biol. Chem. 258 1983 2911 2915
    • (1983) J. Biol. Chem. , vol.258 , pp. 2911-2915
    • Waite, J.H.1
  • 50
    • 0019336856 scopus 로고
    • The bioadhesive of Mytilus byssus - A protein containing L-DOPA
    • J.H. Waite, and M.L. Tanzer The bioadhesive of Mytilus byssus - a protein containing L-DOPA Biochem. Biophys. Res. Commun. 96 1980 1554 1561
    • (1980) Biochem. Biophys. Res. Commun. , vol.96 , pp. 1554-1561
    • Waite, J.H.1    Tanzer, M.L.2
  • 51
    • 0000769202 scopus 로고
    • Natures underwater adhesive specialist
    • J.H. Waite Natures underwater adhesive specialist Chemtech 17 1987 692 697
    • (1987) Chemtech , vol.17 , pp. 692-697
    • Waite, J.H.1
  • 54
    • 74449090189 scopus 로고    scopus 로고
    • General functionalization route for cell adhesion on non-wetting surfaces
    • S.H. Ku, J. Ryu, S.K. Hong, H. Lee, and C.B. Park General functionalization route for cell adhesion on non-wetting surfaces Biomaterials 31 2010 2535 2541
    • (2010) Biomaterials , vol.31 , pp. 2535-2541
    • Ku, S.H.1    Ryu, J.2    Hong, S.K.3    Lee, H.4    Park, C.B.5
  • 55
    • 79953857478 scopus 로고    scopus 로고
    • 2 nanotubes with bone morphogenetic protein 2 and its synergistic effect on the differentiation of mesenchymal stem cells
    • 2 nanotubes with bone morphogenetic protein 2 and its synergistic effect on the differentiation of mesenchymal stem cells Biomacromolecules 12 2011 1097 1105
    • (2011) Biomacromolecules , vol.12 , pp. 1097-1105
    • Lai, M.1    Cai, K.Y.2    Zhao, L.3    Chen, X.Y.4    Hou, Y.H.5    Yang, Z.X.6
  • 56
    • 69049107589 scopus 로고    scopus 로고
    • Methicillin-resistant Staphylococcus aureus strain USA300: Origin and epidemiology
    • F.C. Tenover, and R.V. Goering Methicillin-resistant Staphylococcus aureus strain USA300: origin and epidemiology J. Antimicrob. Chemother. 64 2009 441 446
    • (2009) J. Antimicrob. Chemother. , vol.64 , pp. 441-446
    • Tenover, F.C.1    Goering, R.V.2
  • 57
    • 79551539487 scopus 로고    scopus 로고
    • Antifouling coatings: Recent developments in the design of surfaces that prevent fouling by proteins, bacteria, and marine organisms
    • I. Banerjee, R.C. Pangule, and R.S. Kane Antifouling coatings: recent developments in the design of surfaces that prevent fouling by proteins, bacteria, and marine organisms Adv. Mater. 23 2011 690 718
    • (2011) Adv. Mater. , vol.23 , pp. 690-718
    • Banerjee, I.1    Pangule, R.C.2    Kane, R.S.3
  • 60
    • 68849111119 scopus 로고    scopus 로고
    • Polymerizable vancomycin derivatives for bactericidal biomaterial surface modification: Structure-function evaluation
    • M.C. Lawson, R. Shoemaker, K.B. Hoth, C.N. Bowman, and K.S. Anseth Polymerizable vancomycin derivatives for bactericidal biomaterial surface modification: structure-function evaluation Biomacromolecules 10 2009 2221 2234
    • (2009) Biomacromolecules , vol.10 , pp. 2221-2234
    • Lawson, M.C.1    Shoemaker, R.2    Hoth, K.B.3    Bowman, C.N.4    Anseth, K.S.5
  • 61
    • 33645688585 scopus 로고    scopus 로고
    • Rapid, room-temperature synthesis of antibacterial bionanocomposites of lysozyme with amorphous silica or titania
    • H.R. Luckarift, M.B. Dickerson, K.H. Sandhage, and J.C. Spain Rapid, room-temperature synthesis of antibacterial bionanocomposites of lysozyme with amorphous silica or titania Small 2 2006 640 643
    • (2006) Small , vol.2 , pp. 640-643
    • Luckarift, H.R.1    Dickerson, M.B.2    Sandhage, K.H.3    Spain, J.C.4
  • 64
    • 41149164295 scopus 로고    scopus 로고
    • Incorporation of a hydrophobic antibacterial peptide into amphiphilic polyelectrolyte multilayers: A bioinspired approach to prepare biocidal thin coatings
    • A. Guyomard, E. De, T. Jouenne, J.J. Malandain, G. Muller, and K. Glinel Incorporation of a hydrophobic antibacterial peptide into amphiphilic polyelectrolyte multilayers: a bioinspired approach to prepare biocidal thin coatings Adv. Funct. Mater. 18 2008 758 765
    • (2008) Adv. Funct. Mater. , vol.18 , pp. 758-765
    • Guyomard, A.1    De, E.2    Jouenne, T.3    Malandain, J.J.4    Muller, G.5    Glinel, K.6
  • 65
    • 77951014179 scopus 로고    scopus 로고
    • Prevention of biofilm formation on titanium surfaces modified with conjugated molecules comprised of antimicrobial and titanium-binding peptides
    • M. Yoshinari, T. Kato, K. Matsuzaka, T. Hayakawa, and K. Shiba Prevention of biofilm formation on titanium surfaces modified with conjugated molecules comprised of antimicrobial and titanium-binding peptides Biofouling 26 2009 103 110
    • (2009) Biofouling , vol.26 , pp. 103-110
    • Yoshinari, M.1    Kato, T.2    Matsuzaka, K.3    Hayakawa, T.4    Shiba, K.5
  • 66
    • 84862794152 scopus 로고    scopus 로고
    • Gentamicin and bone morphogenic protein-2 (bmp-2)-delivering heparinized-titanium implant with enhanced antibacterial activity and osteointegration
    • D.-W. Lee, Y.-P. Yun, K. Park, and S.E. Kim Gentamicin and bone morphogenic protein-2 (bmp-2)-delivering heparinized-titanium implant with enhanced antibacterial activity and osteointegration Bone 50 2012 974 982
    • (2012) Bone , vol.50 , pp. 974-982
    • Lee, D.-W.1    Yun, Y.-P.2    Park, K.3    Kim, S.E.4
  • 67
    • 0040292131 scopus 로고    scopus 로고
    • Probing resistance to protein adsorption of oligo(ethylene glycol)-terminated self-assembled monolayers by scanning force microscopy
    • K. Feldman, G. Hahner, N.D. Spencer, P. Harder, and M. Grunze Probing resistance to protein adsorption of oligo(ethylene glycol)-terminated self-assembled monolayers by scanning force microscopy J. Am. Chem. Soc. 121 1999 10134 10141
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 10134-10141
    • Feldman, K.1    Hahner, G.2    Spencer, N.D.3    Harder, P.4    Grunze, M.5
  • 68
    • 18044399825 scopus 로고    scopus 로고
    • Poly(l-lysine)-g-poly(ethylene glycol) layers on metal oxide surfaces: Attachment mechanism and effects of polymer architecture on resistance to protein adsorption
    • G.L. Kenausis, J. Voros, D.L. Elbert, N.P. Huang, R. Hofer, L. Ruiz-Taylor, M. Textor, J.A. Hubbell, and N.D. Spencer Poly(l-lysine)-g- poly(ethylene glycol) layers on metal oxide surfaces: attachment mechanism and effects of polymer architecture on resistance to protein adsorption J. Phys. Chem. B 104 2000 3298 3309
    • (2000) J. Phys. Chem. B , vol.104 , pp. 3298-3309
    • Kenausis, G.L.1    Voros, J.2    Elbert, D.L.3    Huang, N.P.4    Hofer, R.5    Ruiz-Taylor, L.6    Textor, M.7    Hubbell, J.A.8    Spencer, N.D.9
  • 69
    • 0037427331 scopus 로고    scopus 로고
    • Mussel adhesive protein mimetic polymers for the preparation of nonfouling surfaces
    • J.L. Dalsin, B.H. Hu, B.P. Lee, and P.B. Messersmith Mussel adhesive protein mimetic polymers for the preparation of nonfouling surfaces J. Am. Chem. Soc. 125 2003 4253 4258
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 4253-4258
    • Dalsin, J.L.1    Hu, B.H.2    Lee, B.P.3    Messersmith, P.B.4
  • 71
    • 12844278724 scopus 로고    scopus 로고
    • Protein resistance of titanium oxide surfaces modified by biologically inspired mPEG-DOPA
    • J.L. Dalsin, L.J. Lin, S. Tosatti, J. Voros, M. Textor, and P.B. Messersmith Protein resistance of titanium oxide surfaces modified by biologically inspired mPEG-DOPA Langmuir 21 2005 640 646
    • (2005) Langmuir , vol.21 , pp. 640-646
    • Dalsin, J.L.1    Lin, L.J.2    Tosatti, S.3    Voros, J.4    Textor, M.5    Messersmith, P.B.6
  • 72
    • 0034700098 scopus 로고    scopus 로고
    • Measuring the forces involved in polyvalent adhesion of uropathogenic Escherichia coli to mannose-presenting surfaces
    • M.N. Liang, S.P. Smith, S.J. Metallo, I.S. Choi, M. Prentiss, and G.M. Whitesides Measuring the forces involved in polyvalent adhesion of uropathogenic Escherichia coli to mannose-presenting surfaces Proc. Natl. Acad. Sci. USA 97 2000 13092 13096
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13092-13096
    • Liang, M.N.1    Smith, S.P.2    Metallo, S.J.3    Choi, I.S.4    Prentiss, M.5    Whitesides, G.M.6
  • 73
    • 0033330657 scopus 로고    scopus 로고
    • Microbial biofilms: Their development and significance for medical device-related infections
    • M. Habash, and G. Reid Microbial biofilms: their development and significance for medical device-related infections J. Clin. Pharmacol. 39 1999 887 898
    • (1999) J. Clin. Pharmacol. , vol.39 , pp. 887-898
    • Habash, M.1    Reid, G.2
  • 74
    • 0021271957 scopus 로고
    • Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule
    • M.D. Pierschbacher, and E. Ruoslahti Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule Nature 309 1984 30 33
    • (1984) Nature , vol.309 , pp. 30-33
    • Pierschbacher, M.D.1    Ruoslahti, E.2
  • 75
    • 17344362877 scopus 로고    scopus 로고
    • Signaling by integrin receptors
    • C.C. Kumar Signaling by integrin receptors Oncogene 17 1998 1365 1373
    • (1998) Oncogene , vol.17 , pp. 1365-1373
    • Kumar, C.C.1
  • 76
    • 0023463846 scopus 로고
    • Cell-surface receptors for extracellular-matrix molecules
    • C.A. Buck, and A.F. Horwitz Cell-surface receptors for extracellular-matrix molecules Annu. Rev. Cell Biol. 3 1987 179 205
    • (1987) Annu. Rev. Cell Biol. , vol.3 , pp. 179-205
    • Buck, C.A.1    Horwitz, A.F.2
  • 78
    • 0041559949 scopus 로고    scopus 로고
    • RGD modified polymers: Biomaterials for stimulated cell adhesion and beyond
    • U. Hersel, C. Dahmen, and H. Kessler RGD modified polymers: biomaterials for stimulated cell adhesion and beyond Biomaterials 24 2003 4385 4415
    • (2003) Biomaterials , vol.24 , pp. 4385-4415
    • Hersel, U.1    Dahmen, C.2    Kessler, H.3
  • 79
    • 20144363075 scopus 로고    scopus 로고
    • Biomaterials functionalization using a novel peptide that selectively binds to a conducting polymer
    • A.B. Sanghvi, K.P.H. Miller, A.M. Belcher, and C.E. Schmidt Biomaterials functionalization using a novel peptide that selectively binds to a conducting polymer Nat. Mater. 4 2005 496 502
    • (2005) Nat. Mater. , vol.4 , pp. 496-502
    • Sanghvi, A.B.1    Miller, K.P.H.2    Belcher, A.M.3    Schmidt, C.E.4
  • 81
    • 26844571289 scopus 로고    scopus 로고
    • In vivo effects of RGD-coated titanium implants inserted in two bone-gap models
    • B. Elmengaard, J.E. Bechtold, and K. Søballe In vivo effects of RGD-coated titanium implants inserted in two bone-gap models J. Biomed. Mater. Res. Part A 75A 2005 249 255
    • (2005) J. Biomed. Mater. Res. Part A , vol.75 A , pp. 249-255
    • Elmengaard, B.1    Bechtold, J.E.2    Søballe, K.3
  • 82
    • 33646501397 scopus 로고    scopus 로고
    • Enhanced bone apposition around biofunctionalized sandblasted and acid-etched titanium implant surfaces - A histomorphometric study in miniature pigs
    • Y. Germanier, S. Tosatti, N. Broggini, M. Textor, and D. Buser Enhanced bone apposition around biofunctionalized sandblasted and acid-etched titanium implant surfaces - a histomorphometric study in miniature pigs Clin. Oral Implants Res. 17 2006 251 257
    • (2006) Clin. Oral Implants Res. , vol.17 , pp. 251-257
    • Germanier, Y.1    Tosatti, S.2    Broggini, N.3    Textor, M.4    Buser, D.5
  • 84
    • 42249087139 scopus 로고    scopus 로고
    • The effect of integrin-specific bioactive coatings on tissue healing and implant osseointegration
    • T.A. Petrie, J.E. Raynor, C.D. Reyes, K.L. Burns, D.M. Collard, and A.J. Garcia The effect of integrin-specific bioactive coatings on tissue healing and implant osseointegration Biomaterials 29 2008 2849 2857
    • (2008) Biomaterials , vol.29 , pp. 2849-2857
    • Petrie, T.A.1    Raynor, J.E.2    Reyes, C.D.3    Burns, K.L.4    Collard, D.M.5    Garcia, A.J.6
  • 85
    • 33846267301 scopus 로고    scopus 로고
    • Peri-implant bone formation and implant integration strength of peptide-modified p(AAM-co-EG/AAC) interpenetrating polymer network-coated titanium implants
    • T.A. Barber, J.E. Ho, A. De Ranieri, A.S. Virdi, D.R. Sumner, and K.E. Healy Peri-implant bone formation and implant integration strength of peptide-modified p(AAM-co-EG/AAC) interpenetrating polymer network-coated titanium implants J. Biomed. Mater. Res., Part A 80A 2007 306 320
    • (2007) J. Biomed. Mater. Res., Part A , vol.80 A , pp. 306-320
    • Barber, T.A.1    Ho, J.E.2    De Ranieri, A.3    Virdi, A.S.4    Sumner, D.R.5    Healy, K.E.6
  • 86
    • 0029778085 scopus 로고    scopus 로고
    • Structural and functional aspects of RGD-containing cyclic pentapeptides as highly potent and selective integrin αvβ3 antagonists
    • R. Haubner, R. Gratias, B. Diefenbach, S.L. Goodman, A. Jonczyk, and H. Kessler Structural and functional aspects of RGD-containing cyclic pentapeptides as highly potent and selective integrin αvβ3 antagonists J. Am. Chem. Soc. 118 1996 7461 7472
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 7461-7472
    • Haubner, R.1    Gratias, R.2    Diefenbach, B.3    Goodman, S.L.4    Jonczyk, A.5    Kessler, H.6
  • 88
    • 0037023363 scopus 로고    scopus 로고
    • Crystal structure of the extracellular segment of integrin alphavbeta3 in complex with an Arg-Gly-Asp ligand
    • J.P. Xiong, T. Stehle, R. Zhang, A. Joachimiak, M. Frech, S.L. Goodman, and M.A. Arnaout Crystal structure of the extracellular segment of integrin alphavbeta3 in complex with an Arg-Gly-Asp ligand Science 296 2002 151 155
    • (2002) Science , vol.296 , pp. 151-155
    • Xiong, J.P.1    Stehle, T.2    Zhang, R.3    Joachimiak, A.4    Frech, M.5    Goodman, S.L.6    Arnaout, M.A.7
  • 89
    • 11144280456 scopus 로고    scopus 로고
    • In vivo study of the effect of RGD treatment on bone ongrowth on press-fit titanium alloy implants
    • B. Elmengaard, J.E. Bechtold, and K. Soballe In vivo study of the effect of RGD treatment on bone ongrowth on press-fit titanium alloy implants Biomaterials 26 2005 3521 3526
    • (2005) Biomaterials , vol.26 , pp. 3521-3526
    • Elmengaard, B.1    Bechtold, J.E.2    Soballe, K.3
  • 90
    • 0037170020 scopus 로고    scopus 로고
    • Solid-phase synthesis of c(RGDfK) derivatives: On-resin cyclisation and lysine functionalisation
    • C.F. McCusker, P.J. Kocienski, F.T. Boyle, and A.G. Schatzlein Solid-phase synthesis of c(RGDfK) derivatives: on-resin cyclisation and lysine functionalisation Bioorg. Med. Chem. Lett. 12 2002 547 549
    • (2002) Bioorg. Med. Chem. Lett. , vol.12 , pp. 547-549
    • McCusker, C.F.1    Kocienski, P.J.2    Boyle, F.T.3    Schatzlein, A.G.4
  • 91
    • 84869791587 scopus 로고    scopus 로고
    • On-resin-synthesis of an acylated and fluorescence-labeled cyclic integrin ligand for modification of poly(lactic-co-glycolic acid)
    • R. Hassert, P.G. Hoffmeister, M. Pagel, M. Hacker, M. Schulz-Siegmund, and A.G. Beck-Sickinger On-resin-synthesis of an acylated and fluorescence-labeled cyclic integrin ligand for modification of poly(lactic-co-glycolic acid) Chem. Biodivers. 9 2012 2648 2658
    • (2012) Chem. Biodivers. , vol.9 , pp. 2648-2658
    • Hassert, R.1    Hoffmeister, P.G.2    Pagel, M.3    Hacker, M.4    Schulz-Siegmund, M.5    Beck-Sickinger, A.G.6
  • 92
    • 80053521886 scopus 로고    scopus 로고
    • 2 substrate via tyrosinase-catalyzed oxidative reaction
    • 2 substrate via tyrosinase-catalyzed oxidative reaction J. Mater. Chem. 21 2011 15906 15908
    • (2011) J. Mater. Chem. , vol.21 , pp. 15906-15908
    • Park, K.M.1    Park, K.D.2
  • 93
    • 34447279470 scopus 로고    scopus 로고
    • Cell adhesion biomaterial based on mussel adhesive protein fused with RGD peptide
    • D.S. Hwang, S.B. Sim, and H.J. Cha Cell adhesion biomaterial based on mussel adhesive protein fused with RGD peptide Biomaterials 28 2007 4039 4046
    • (2007) Biomaterials , vol.28 , pp. 4039-4046
    • Hwang, D.S.1    Sim, S.B.2    Cha, H.J.3
  • 94
    • 77957311585 scopus 로고    scopus 로고
    • Cell behavior on extracellular matrix mimic materials based on mussel adhesive protein fused with functional peptides
    • B.H. Choi, Y.S. Choi, D.G. Kane, B.J. Kim, Y.H. Song, and H.J. Cha Cell behavior on extracellular matrix mimic materials based on mussel adhesive protein fused with functional peptides Biomaterials 31 2010 8980 8988
    • (2010) Biomaterials , vol.31 , pp. 8980-8988
    • Choi, B.H.1    Choi, Y.S.2    Kane, D.G.3    Kim, B.J.4    Song, Y.H.5    Cha, H.J.6
  • 95
    • 72149121291 scopus 로고    scopus 로고
    • Promotion of osteoblast proliferation on complex coacervation-based hyaluronic acid - Recombinant mussel adhesive protein coatings on titanium
    • D.S. Hwang, J.H. Waite, and M. Tirrell Promotion of osteoblast proliferation on complex coacervation-based hyaluronic acid - recombinant mussel adhesive protein coatings on titanium Biomaterials 31 2010 1080 1084
    • (2010) Biomaterials , vol.31 , pp. 1080-1084
    • Hwang, D.S.1    Waite, J.H.2    Tirrell, M.3
  • 96
    • 34347346201 scopus 로고    scopus 로고
    • Protein immobilization strategies for protein biochips
    • F. Rusmini, Z.Y. Zhong, and J. Feijen Protein immobilization strategies for protein biochips Biomacromolecules 8 2007 1775 1789
    • (2007) Biomacromolecules , vol.8 , pp. 1775-1789
    • Rusmini, F.1    Zhong, Z.Y.2    Feijen, J.3
  • 97
    • 70350257632 scopus 로고    scopus 로고
    • Advances in enzyme immobilisation
    • D. Brady, and J. Jordaan Advances in enzyme immobilisation Biotechnol. Lett. 31 2009 1639 1650
    • (2009) Biotechnol. Lett. , vol.31 , pp. 1639-1650
    • Brady, D.1    Jordaan, J.2
  • 98
    • 13844306318 scopus 로고    scopus 로고
    • Enzymatic activity on a chip: The critical role of protein orientation
    • T. Cha, A. Guo, and X.Y. Zhu Enzymatic activity on a chip: the critical role of protein orientation Proteomics 5 2005 416 419
    • (2005) Proteomics , vol.5 , pp. 416-419
    • Cha, T.1    Guo, A.2    Zhu, X.Y.3
  • 99
    • 84857438845 scopus 로고    scopus 로고
    • Simultaneous "one pot" expressed protein ligation and Cu-I-catalyzed azide/alkyne cycloaddition for protein immobilization
    • M. Steinhagen, K. Holland-Nell, M. Meldal, and A.G. Beck-Sickinger Simultaneous "one pot" expressed protein ligation and Cu-I-catalyzed azide/alkyne cycloaddition for protein immobilization ChemBioChem 12 2011 2426 2430
    • (2011) ChemBioChem , vol.12 , pp. 2426-2430
    • Steinhagen, M.1    Holland-Nell, K.2    Meldal, M.3    Beck-Sickinger, A.G.4
  • 100
    • 10344265554 scopus 로고    scopus 로고
    • Oriented attachment and membrane reconstitution of his-tagged cytochrome c oxidase to a gold electrode: In situ monitoring by surface-enhanced infrared absorption spectroscopy
    • K. Ataka, F. Giess, W. Knoll, R. Naumann, S. Haber-Pohlmeier, B. Richter, and J. Heberle Oriented attachment and membrane reconstitution of his-tagged cytochrome c oxidase to a gold electrode: in situ monitoring by surface-enhanced infrared absorption spectroscopy J. Am. Chem. Soc. 126 2004 16199 16206
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 16199-16206
    • Ataka, K.1    Giess, F.2    Knoll, W.3    Naumann, R.4    Haber-Pohlmeier, S.5    Richter, B.6    Heberle, J.7
  • 101
    • 34250766201 scopus 로고    scopus 로고
    • The strep-tag system for one-step purification and high-affinity detection or capturing of proteins
    • T.G.M. Schmidt, and A. Skerra The strep-tag system for one-step purification and high-affinity detection or capturing of proteins Nat. Protoc. 2 2007 1528 1535
    • (2007) Nat. Protoc. , vol.2 , pp. 1528-1535
    • Schmidt, T.G.M.1    Skerra, A.2
  • 103
    • 34250019537 scopus 로고
    • Bone - Formation by autoinduction
    • M.R. Urist Bone - formation by autoinduction Science 150 1965 893 899
    • (1965) Science , vol.150 , pp. 893-899
    • Urist, M.R.1
  • 104
    • 2442638878 scopus 로고    scopus 로고
    • The use of recombinant human bone morphometric protein-2 (rhBMP-2) in orthopaedic applications
    • S.N. Khan, and J.M. Lane The use of recombinant human bone morphometric protein-2 (rhBMP-2) in orthopaedic applications Expert Opin. Biol. Ther. 4 2004 741 748
    • (2004) Expert Opin. Biol. Ther. , vol.4 , pp. 741-748
    • Khan, S.N.1    Lane, J.M.2
  • 105
    • 18244366347 scopus 로고    scopus 로고
    • BMP-2 liberated from biomimetic implant coatings induces and sustains direct ossification in an ectopic rat model
    • Y. Liu, K. de Groot, and E.B. Hunziker BMP-2 liberated from biomimetic implant coatings induces and sustains direct ossification in an ectopic rat model Bone 36 2005 745 757
    • (2005) Bone , vol.36 , pp. 745-757
    • Liu, Y.1    De Groot, K.2    Hunziker, E.B.3
  • 106
    • 0025857671 scopus 로고
    • Recombinant human bone morphogenetic protein-2 stimulates osteoblastic maturation and inhibits myogenic differentiation in vitro
    • A. Yamaguchi, T. Katagiri, T. Ikeda, J.M. Wozney, V. Rosen, E.A. Wang, A.J. Kahn, T. Suda, and S. Yoshiki Recombinant human bone morphogenetic protein-2 stimulates osteoblastic maturation and inhibits myogenic differentiation in vitro J. Cell Biol. 113 1991 681 687
    • (1991) J. Cell Biol. , vol.113 , pp. 681-687
    • Yamaguchi, A.1    Katagiri, T.2    Ikeda, T.3    Wozney, J.M.4    Rosen, V.5    Wang, E.A.6    Kahn, A.J.7    Suda, T.8    Yoshiki, S.9
  • 107
    • 57749185245 scopus 로고    scopus 로고
    • Directional BMP-2 for functionalization of titanium surfaces
    • K. Kashiwagi, T. Tsuji, and K. Shiba Directional BMP-2 for functionalization of titanium surfaces Biomaterials 30 2009 1166 1175
    • (2009) Biomaterials , vol.30 , pp. 1166-1175
    • Kashiwagi, K.1    Tsuji, T.2    Shiba, K.3
  • 108
    • 84864703375 scopus 로고    scopus 로고
    • A novel, biased-like sdf-1 derivative acts synergistically with starPEG-based heparin hydrogels and improves eEPC migration in vitro
    • L. Baumann, S. Prokoph, C. Gabriel, U. Freudenberg, C. Werner, and A.G. Beck-Sickinger A novel, biased-like sdf-1 derivative acts synergistically with starPEG-based heparin hydrogels and improves eEPC migration in vitro J. Control. Release 162 2012 68 75
    • (2012) J. Control. Release , vol.162 , pp. 68-75
    • Baumann, L.1    Prokoph, S.2    Gabriel, C.3    Freudenberg, U.4    Werner, C.5    Beck-Sickinger, A.G.6
  • 109
    • 0014489983 scopus 로고
    • Identification of rapid changes at plasma-solid interfaces
    • L. Vroman, and A.L. Adams Identification of rapid changes at plasma-solid interfaces J. Biomed. Mater. Res. 3 1969 43 67
    • (1969) J. Biomed. Mater. Res. , vol.3 , pp. 43-67
    • Vroman, L.1    Adams, A.L.2
  • 110
    • 38049169501 scopus 로고    scopus 로고
    • Development of an universal affinity fusion tag (poly-DOPA) for immobilizing recombinant proteins on biomaterials
    • H.P. Jennissen, and M. Laub Development of an universal affinity fusion tag (poly-DOPA) for immobilizing recombinant proteins on biomaterials Materialwiss. Werkstofftech. 38 2007 1035 1039
    • (2007) Materialwiss. Werkstofftech. , vol.38 , pp. 1035-1039
    • Jennissen, H.P.1    Laub, M.2
  • 111
    • 35448979846 scopus 로고    scopus 로고
    • Surface presentation of bioactive ligands in a nonadhesive background using DOPA-tethered biotinylated poly(ethylene glycol)
    • R.C. Gunawan, J.A. King, B.P. Lee, P.B. Messersmith, and W.M. Miller Surface presentation of bioactive ligands in a nonadhesive background using DOPA-tethered biotinylated poly(ethylene glycol) Langmuir 23 2007 10635 10643
    • (2007) Langmuir , vol.23 , pp. 10635-10643
    • Gunawan, R.C.1    King, J.A.2    Lee, B.P.3    Messersmith, P.B.4    Miller, W.M.5
  • 112
    • 20444454314 scopus 로고    scopus 로고
    • Polysaccharide-protein surface modification of titanium via a layer-by-layer technique: Characterization and cell behaviour aspects
    • K.Y. Cai, A. Rechtenbach, J.Y. Hao, J. Bossert, and K.D. Jandt Polysaccharide-protein surface modification of titanium via a layer-by-layer technique: characterization and cell behaviour aspects Biomaterials 26 2005 5960 5971
    • (2005) Biomaterials , vol.26 , pp. 5960-5971
    • Cai, K.Y.1    Rechtenbach, A.2    Hao, J.Y.3    Bossert, J.4    Jandt, K.D.5
  • 115
    • 58149094924 scopus 로고    scopus 로고
    • Signal transduction of hyaluronic acid-peptide conjugate for formyl peptide receptor like 1 receptor
    • E.J. Oh, J.W. Kim, J.H. Kong, S.H. Ryu, and S.K. Hahn Signal transduction of hyaluronic acid-peptide conjugate for formyl peptide receptor like 1 receptor Bioconjugate Chem. 19 2008 2401 2408
    • (2008) Bioconjugate Chem. , vol.19 , pp. 2401-2408
    • Oh, E.J.1    Kim, J.W.2    Kong, J.H.3    Ryu, S.H.4    Hahn, S.K.5
  • 116
    • 82855175136 scopus 로고    scopus 로고
    • Surface modification of pancreatic islets using heparin-DOPA conjugate and anti-CD154 mAB for the prolonged survival of intrahepatic transplanted islets in a xenograft model
    • Y.S. Jung, J.H. Jeong, S. Yook, B.H. Im, J. Seo, S.W. Hong, J.B. Park, V.C. Yan, D.Y. Lee, and Y. Byun Surface modification of pancreatic islets using heparin-DOPA conjugate and anti-CD154 mAB for the prolonged survival of intrahepatic transplanted islets in a xenograft model Biomaterials 33 2012 295 303
    • (2012) Biomaterials , vol.33 , pp. 295-303
    • Jung, Y.S.1    Jeong, J.H.2    Yook, S.3    Im, B.H.4    Seo, J.5    Hong, S.W.6    Park, J.B.7    Yan, V.C.8    Lee, D.Y.9    Byun, Y.10
  • 117
    • 70349917806 scopus 로고    scopus 로고
    • Bioorthogonal chemistry: Fishing for selectivity in a sea of functionality
    • E.M. Sletten, and C.R. Bertozzi Bioorthogonal chemistry: fishing for selectivity in a sea of functionality Angew. Chem., Int. Ed. Engl. 48 2009 6974 6998
    • (2009) Angew. Chem., Int. Ed. Engl. , vol.48 , pp. 6974-6998
    • Sletten, E.M.1    Bertozzi, C.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.