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Volumn 28, Issue 32, 2007, Pages 4739-4747

Protein repellent properties of covalently attached PEG coatings on nanostructured SiO2-based interfaces

Author keywords

Biofunctionalization; Cell adhesion; Nanostructures; Poly(ethylene glycol) (PEG); Protein adsorption; Quartz crystal microbalance (QCM)

Indexed keywords

ADSORPTION; CELL ADHESION; COVALENT BONDS; GLASS; NANOSTRUCTURES; PROTEINS; QUARTZ CRYSTAL MICROBALANCES; SELF ASSEMBLY; SILICA;

EID: 34548023629     PISSN: 01429612     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biomaterials.2007.07.038     Document Type: Article
Times cited : (188)

References (36)
  • 1
    • 0036629182 scopus 로고    scopus 로고
    • Towards quantitative assays with peptide chips: a surface engineering approach
    • Houseman B.T., and Mrksich M. Towards quantitative assays with peptide chips: a surface engineering approach. Trend Biotechnol 20 (2002) 279-281
    • (2002) Trend Biotechnol , vol.20 , pp. 279-281
    • Houseman, B.T.1    Mrksich, M.2
  • 2
    • 4644271368 scopus 로고    scopus 로고
    • Peptide arrays: towards routine implementation
    • Min D.H., and Mrksich M. Peptide arrays: towards routine implementation. Curr Opin Chem Biol 8 (2004) 554-558
    • (2004) Curr Opin Chem Biol , vol.8 , pp. 554-558
    • Min, D.H.1    Mrksich, M.2
  • 3
    • 2542458247 scopus 로고    scopus 로고
    • Swelling behavior of self-assembled monolayers of alkanethiol-terminated poly(ethylene glycol): a neutron reflectometry study
    • Fick J., Steitz R., Leiner V., Tokumitsu S., Himmelhaus M., and Grunze M. Swelling behavior of self-assembled monolayers of alkanethiol-terminated poly(ethylene glycol): a neutron reflectometry study. Langmuir 20 (2004) 3848-3853
    • (2004) Langmuir , vol.20 , pp. 3848-3853
    • Fick, J.1    Steitz, R.2    Leiner, V.3    Tokumitsu, S.4    Himmelhaus, M.5    Grunze, M.6
  • 5
    • 2542453791 scopus 로고    scopus 로고
    • Construction of cell-resistant surfaces by immobilization of poly(ethylene glycol) on gold
    • Mougin K., Lawrence M.B., Fernandez E.J., and Hillier A.C. Construction of cell-resistant surfaces by immobilization of poly(ethylene glycol) on gold. Langmuir 20 (2004) 4302-4305
    • (2004) Langmuir , vol.20 , pp. 4302-4305
    • Mougin, K.1    Lawrence, M.B.2    Fernandez, E.J.3    Hillier, A.C.4
  • 6
    • 0034324760 scopus 로고    scopus 로고
    • A high-density poly(ethylene glycol) polymer brush for immobilization on glass-type surfaces
    • Piehler J., Brecht A., Valiokas R., Liedberg B., and Gauglitz G. A high-density poly(ethylene glycol) polymer brush for immobilization on glass-type surfaces. Biosens Bioelectron 15 (2000) 473-481
    • (2000) Biosens Bioelectron , vol.15 , pp. 473-481
    • Piehler, J.1    Brecht, A.2    Valiokas, R.3    Liedberg, B.4    Gauglitz, G.5
  • 7
    • 0035846777 scopus 로고    scopus 로고
    • Grafting of high-density poly(ethylene glycol) monolayers on Si(1 1 1)
    • Zhu X.Y., Jun Y., Staarup D.R., Major R.C., Danielson S., Boiadjiev V., et al. Grafting of high-density poly(ethylene glycol) monolayers on Si(1 1 1). Langmuir 17 (2001) 7798-7803
    • (2001) Langmuir , vol.17 , pp. 7798-7803
    • Zhu, X.Y.1    Jun, Y.2    Staarup, D.R.3    Major, R.C.4    Danielson, S.5    Boiadjiev, V.6
  • 8
    • 0036201921 scopus 로고    scopus 로고
    • Effects of cloud-point grafting, chain length, and density of PEG layers on competitive adsorption of ocular proteins
    • Kingshott P., Thissen H., and Griesser H. Effects of cloud-point grafting, chain length, and density of PEG layers on competitive adsorption of ocular proteins. Biomaterials 23 (2002) 2043-2056
    • (2002) Biomaterials , vol.23 , pp. 2043-2056
    • Kingshott, P.1    Thissen, H.2    Griesser, H.3
  • 9
    • 0035135778 scopus 로고    scopus 로고
    • Poly(l-lysine)-g-poly(ethylene glycol) layers on metal oxide surfaces: surface-analytical characterization and resistance to serum and fibrinogen adsorption
    • Huang N.P., Michel R., Vörös J., Textor M., Hofer R., Rossi A., et al. Poly(l-lysine)-g-poly(ethylene glycol) layers on metal oxide surfaces: surface-analytical characterization and resistance to serum and fibrinogen adsorption. Langmuir 17 (2001) 489-498
    • (2001) Langmuir , vol.17 , pp. 489-498
    • Huang, N.P.1    Michel, R.2    Vörös, J.3    Textor, M.4    Hofer, R.5    Rossi, A.6
  • 10
    • 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
    • Kenausis G.L., Vörös J., Elbert D.L., Huang N.P., Hofer R., Ruiz-Taylor L., et al. 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    Vörös, J.2    Elbert, D.L.3    Huang, N.P.4    Hofer, R.5    Ruiz-Taylor, L.6
  • 11
    • 0035970110 scopus 로고    scopus 로고
    • Ruiz-Taylor LA, Martin TL, Zaugg FG, Witte K, Indermuhle P, Nock S, et al. In: Proceedings of the National Academy of Sciences of the United States of America 2001;98:852-7.
  • 12
    • 0024304793 scopus 로고
    • Enhancement of serum fibronectin adsorption and the clonal plating efficiencies of Swiss mouse 3T3 fibroblast and MM14 mouse myoblast cells on polymer substrates modified by radiofrequency plasma deposition
    • Chinn J.A., Horbett T.A., Ratner B.D., Schway M.B., Haque Y., and Hauschka S.D. Enhancement of serum fibronectin adsorption and the clonal plating efficiencies of Swiss mouse 3T3 fibroblast and MM14 mouse myoblast cells on polymer substrates modified by radiofrequency plasma deposition. J Colloid Interface Sci 127 (1989) 67-87
    • (1989) J Colloid Interface Sci , vol.127 , pp. 67-87
    • Chinn, J.A.1    Horbett, T.A.2    Ratner, B.D.3    Schway, M.B.4    Haque, Y.5    Hauschka, S.D.6
  • 13
    • 16344387672 scopus 로고    scopus 로고
    • Comparison of coatings from reactive star shaped PEG-stat-PPG prepolymers and grafted linear PEG for biological and medical applications
    • Groll J., Ademovic Z., Ameringer T., Klee D., and Möller M. Comparison of coatings from reactive star shaped PEG-stat-PPG prepolymers and grafted linear PEG for biological and medical applications. Biomacromolecules 6 (2005) 956-962
    • (2005) Biomacromolecules , vol.6 , pp. 956-962
    • Groll, J.1    Ademovic, Z.2    Ameringer, T.3    Klee, D.4    Möller, M.5
  • 14
    • 2442442861 scopus 로고    scopus 로고
    • Biofunctionalized polymer surfaces exhibiting minimal interaction towards immobilized proteins
    • Amergoulova E.V., Groll J., Heyes C.D., Ameringer T., Röcker C., Möller M., et al. Biofunctionalized polymer surfaces exhibiting minimal interaction towards immobilized proteins. Chem Phys Chem 5 (2004) 552-555
    • (2004) Chem Phys Chem , vol.5 , pp. 552-555
    • Amergoulova, E.V.1    Groll, J.2    Heyes, C.D.3    Ameringer, T.4    Röcker, C.5    Möller, M.6
  • 15
    • 0037418502 scopus 로고    scopus 로고
    • Covalent coupling of antibodies to self-assembled monolayers of carboxy-functionalized poly(ethylene glycol): protein resistance and specific binding of biomolecules
    • Herrwerth S., Rosendahl T., Feng C., Fick J., Eck W., Himmelhaus M., et al. Covalent coupling of antibodies to self-assembled monolayers of carboxy-functionalized poly(ethylene glycol): protein resistance and specific binding of biomolecules. Langmuir 19 (2003) 1880-1887
    • (2003) Langmuir , vol.19 , pp. 1880-1887
    • Herrwerth, S.1    Rosendahl, T.2    Feng, C.3    Fick, J.4    Eck, W.5    Himmelhaus, M.6
  • 16
    • 4344564964 scopus 로고    scopus 로고
    • Formation of focal adhesion-stress fibre complexes coordinated by adhesive and non-adhesive surface domains
    • Zimerman B., Arnold M., Ulmer J., Blümmel J., Besser A., Spatz J.P., et al. Formation of focal adhesion-stress fibre complexes coordinated by adhesive and non-adhesive surface domains. Proceedings: Nanobiotechnology 151 (2004) 62-66
    • (2004) Proceedings: Nanobiotechnology , vol.151 , pp. 62-66
    • Zimerman, B.1    Arnold, M.2    Ulmer, J.3    Blümmel, J.4    Besser, A.5    Spatz, J.P.6
  • 19
    • 0041807736 scopus 로고    scopus 로고
    • Micro-nanostructure interfaces fabricated by the use of inorganic block copolymer micellar monolayers as negative resist for electron-beam lithography
    • Glass R., Arnold M., Blümmel J., Küller A., Möller M., and Spatz J.P. Micro-nanostructure interfaces fabricated by the use of inorganic block copolymer micellar monolayers as negative resist for electron-beam lithography. Adv Funct Mater 13 (2003) 569-575
    • (2003) Adv Funct Mater , vol.13 , pp. 569-575
    • Glass, R.1    Arnold, M.2    Blümmel, J.3    Küller, A.4    Möller, M.5    Spatz, J.P.6
  • 21
    • 3242666071 scopus 로고    scopus 로고
    • Self-assembled monolayers. From "simple" model systems to biofunctionalized interfaces
    • Schreiber F. Self-assembled monolayers. From "simple" model systems to biofunctionalized interfaces. J Phys: Condens Matter 16 (2004) R881-R900
    • (2004) J Phys: Condens Matter , vol.16
    • Schreiber, F.1
  • 22
    • 18044398972 scopus 로고    scopus 로고
    • Self-assembled monolayers of thiolates on metals as a form of nanotechnology
    • Love J.C., Estroff L.A., Kriebel J.K., Nuzzo R.G., and Whitesides G.M. Self-assembled monolayers of thiolates on metals as a form of nanotechnology. Chem Rev 105 (2005) 1103-1169
    • (2005) Chem Rev , vol.105 , pp. 1103-1169
    • Love, J.C.1    Estroff, L.A.2    Kriebel, J.K.3    Nuzzo, R.G.4    Whitesides, G.M.5
  • 23
    • 0345979435 scopus 로고    scopus 로고
    • Formation and structure of self-assembled monolayers
    • Ulman A. Formation and structure of self-assembled monolayers. Chem Rev 96 (1996) 1533-1554
    • (1996) Chem Rev , vol.96 , pp. 1533-1554
    • Ulman, A.1
  • 24
    • 0343510028 scopus 로고
    • Conformations of polymers attached to an interface
    • de Gennes P.D. Conformations of polymers attached to an interface. Macromolecules 13 (1980) 1069-1075
    • (1980) Macromolecules , vol.13 , pp. 1069-1075
    • de Gennes, P.D.1
  • 25
    • 84951279351 scopus 로고
    • Verwendung von Schwingquarzen zur Wägung dünner Schichten und zur Mikrowägung
    • Sauerbrey G. Verwendung von Schwingquarzen zur Wägung dünner Schichten und zur Mikrowägung. Zeitschrift für Physik 155 (1959) 206-222
    • (1959) Zeitschrift für Physik , vol.155 , pp. 206-222
    • Sauerbrey, G.1
  • 26
    • 84886158683 scopus 로고    scopus 로고
    • Mineralization of gold nanoparticles in a block copolymer microemulsion
    • Spatz J.P., Mößmer S., and Möller. Mineralization of gold nanoparticles in a block copolymer microemulsion. Chem: Eur J 2 (1996) 1552-1555
    • (1996) Chem: Eur J , vol.2 , pp. 1552-1555
    • Spatz, J.P.1    Mößmer, S.2    Möller3
  • 27
    • 0033639785 scopus 로고    scopus 로고
    • Ordered deposition of inorganic clusters from micellar block copolymer films
    • Spatz J.P., Mößmer S., Hartmann C., Möller M., Herzog T., Krieger M., et al. Ordered deposition of inorganic clusters from micellar block copolymer films. Langmuir 16 (2000) 407-415
    • (2000) Langmuir , vol.16 , pp. 407-415
    • Spatz, J.P.1    Mößmer, S.2    Hartmann, C.3    Möller, M.4    Herzog, T.5    Krieger, M.6
  • 28
    • 0142217347 scopus 로고    scopus 로고
    • Block copolymer micelle nanolithography
    • Glass R., Möller M., and Spatz J.P. Block copolymer micelle nanolithography. Nanotechnology 14 (2003) 1153-1160
    • (2003) Nanotechnology , vol.14 , pp. 1153-1160
    • Glass, R.1    Möller, M.2    Spatz, J.P.3
  • 29
    • 0345393105 scopus 로고    scopus 로고
    • Purification of brain tubulin through two cycles of polymerization-depolymerization in a high-molarity buffer
    • Castoldi M., and Popov A.V. Purification of brain tubulin through two cycles of polymerization-depolymerization in a high-molarity buffer. Protein Expr Purif 32 (2003) 83-88
    • (2003) Protein Expr Purif , vol.32 , pp. 83-88
    • Castoldi, M.1    Popov, A.V.2
  • 30
    • 0035904233 scopus 로고    scopus 로고
    • Eg5 is static in bipolar spindles relative to tubulin: evidence for a static spindle matrix
    • Kapoor T.M., and Mitchison T.J. Eg5 is static in bipolar spindles relative to tubulin: evidence for a static spindle matrix. J Cell Biol 154 (2001) 1125-1133
    • (2001) J Cell Biol , vol.154 , pp. 1125-1133
    • Kapoor, T.M.1    Mitchison, T.J.2
  • 31
    • 33744538097 scopus 로고    scopus 로고
    • Shirley DA. Phys Rev B 1972;5:4709.
  • 32
    • 0000992383 scopus 로고
    • Attenuation of photoelectrons in monolayers of n-alkanethiols adsorbed on copper, silver, and gold
    • Laibinis P.E., Bain C.D., and Whitesides G.M. Attenuation of photoelectrons in monolayers of n-alkanethiols adsorbed on copper, silver, and gold. J Phys Chem 95 (1991) 7017-7021
    • (1991) J Phys Chem , vol.95 , pp. 7017-7021
    • Laibinis, P.E.1    Bain, C.D.2    Whitesides, G.M.3
  • 33
    • 3242741763 scopus 로고
    • Atomic subshell photoionization cross sections and asymmetry parameters: 1
    • Yeh J.J., and Lindau I. Atomic subshell photoionization cross sections and asymmetry parameters: 1
    • (1985) Atom Data Nucl Data Table , vol.32 , pp. 1
    • Yeh, J.J.1    Lindau, I.2
  • 35
    • 85159139860 scopus 로고    scopus 로고
    • Site-specific presentation of single recombinant proteins in defined nanoarrays
    • Wolfram T., Belz F., Schoen T., and Spatz J.P. Site-specific presentation of single recombinant proteins in defined nanoarrays. Biointerphases 2 (2007) 44-48
    • (2007) Biointerphases , vol.2 , pp. 44-48
    • Wolfram, T.1    Belz, F.2    Schoen, T.3    Spatz, J.P.4
  • 36
    • 0030044339 scopus 로고    scopus 로고
    • Kinetics and motility of the Eg5 microtubule motor
    • Lockhart A., and Cross R.A. Kinetics and motility of the Eg5 microtubule motor. Biochemistry 35 (1996) 2365-2373
    • (1996) Biochemistry , vol.35 , pp. 2365-2373
    • Lockhart, A.1    Cross, R.A.2


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