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Immobilization of Proteins via PEG Chains

  • Krister Holmberg
  • Karin Bergström
  • Maj-Britt Stark
Part of the Topics in Applied Chemistry book series (TAPP)

Abstract

Grafting of poly(ethylene glycol) (or PEG) to solid surfaces has been recognized as a technique for obtaining low protein adsorption and low cell adhesion characteristics.1,2 For instance, PEG coating is reported to give a marked suppression of plasma protein adsorption and platelet adhesion leading to reduced risk of thrombus formation, as demonstrated both in vitro and in vivo.3–5

Keywords

Cloud Point Protein Adsorption Aqueous Buffer Free Lipase Plasma Protein Adsorption 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. 1.
    E. W. Merrill and E. W. Salzman, ASAIO J. 6, 60 (1983).Google Scholar
  2. 2.
    J. H. Lee and J. D. Andrade, in: Polymer Surface Dynamics (J. D. Andrade, ed.), p. 119, Plenum Press, New York (1988).CrossRefGoogle Scholar
  3. 3.
    S. Nagaoka, Y. Mori, H. Takiuchi, K. Yokota, H. Tanzawa, and S. Nishiumi, Polym. Prepr. 24, 67 (1983).Google Scholar
  4. 4.
    S. Nagaoka, Trans. Am. Soc. Internal Organs 10, 76 (1988).Google Scholar
  5. 5.
    S. Nagaoka and A. Nakao, Biomaterials 11, 119 (1990).PubMedCrossRefGoogle Scholar
  6. 6.
    F. E. Bailey, Jr. and J. V. Koleske, Poly(ethyleneoxide), Academic Press, New York (1976).Google Scholar
  7. 7.
    D. W. J. Osmond. B. Vincent, and F. A. Waite, Colloid Polym. Sci. 253, 676 (1975).CrossRefGoogle Scholar
  8. 8.
    T. F. Tadros, in: The Effect of Polymers on Dispersion Properties (T. F. Tadros, ed.), p. 1, Academic Press, New York (1982).Google Scholar
  9. 9.
    D. Knoll and J. Hermans, J. Biol. Chem. 258, 5710 (1983).PubMedGoogle Scholar
  10. 10.
    P A. Srere and K. Uyeda, in: Methods in Enzymology, Vol. 44: Immobilized Enzymes (K. Mosbach, ed.), p. 11, Academic Press, New York (1976).CrossRefGoogle Scholar
  11. 11.
    G. A. Quash, V. Thomas, G. Ogier, S. E. Alaoui, J.-G. Delcros, H. Ripoll, A.-M. Roch, S. Legastelois, R. Gibert, and J.-P Ripoll, in: Covalently Modified Antigens and Antibodies in Diagnosis and Therapy (G. A. Quash and J. D. Rodwell, eds.), p. 155, Marcel Dekker, New York (1989).Google Scholar
  12. 12.
    J. Turková, in: Methods in Enzymology, Vol. 44: Immobilized Enzymes (K. Mosbach, ed.), p. 66, Academic Press, New York (1976).CrossRefGoogle Scholar
  13. 13.
    G. Karlström, A. Carlsson, and B. Lindman, J. Phys. Chem. 94, 5005 (1990).CrossRefGoogle Scholar
  14. 14.
    T. Nakagawa, in: Nonionic Surfactants (M. J. Schick, ed.), Chapter 17, Marcel Dekker, New York (1967).Google Scholar
  15. 15.
    R. Kjellander and E. Florin, J. Chem. Soc, Earaday Trans. 177, 2053 (1981).CrossRefGoogle Scholar
  16. 16.
    G. Karlström, J. Phys. Chem. 89, 4962 (1985).CrossRefGoogle Scholar
  17. 17.
    E. Florin, R. Kjellander, and J. C. Eriksson, J. Chem. Soc, Earaday Trans. 180, 2889 (1984).CrossRefGoogle Scholar
  18. 18.
    P. M. Claesson, R. Kjellander, P Stenius, and H. K. Christenson, J. Chem. Soc, Earaday Trans. 182, 2735 (1986).CrossRefGoogle Scholar
  19. 19.
    M. Malmsten, P. M. Claesson, E. Pezron, and I. Pezron, Langmuir 6, 1572 (1990).CrossRefGoogle Scholar
  20. 20.
    F. Tiberg, C. Brink, M. Hellsten, and K. Holmberg, Colloid Polym. Sci., in press.Google Scholar
  21. 21.
    C. Andrén, K. Holmberg, B. Lindman, and M. Malmsten, Swedish patent application 8904397-0 (1989).Google Scholar
  22. 22.
    W. R. Gombotz and A. S. Hoffman, J. Appl. Polym. Sci. 42, 285 (1988).Google Scholar
  23. 23.
    D. H. Napper, J. Colloid Interface Sci. 58, 390 (1977).CrossRefGoogle Scholar
  24. 24.
    I. Danielsson and B. Lindman, Colloid Surf. 3, 391 (1981).CrossRefGoogle Scholar
  25. 25.
    M. Kahlweit et al. (17 coauthors), J. Colloid Interface Sci. 118, 436 (1987).CrossRefGoogle Scholar
  26. 26.
    B. Gestblom and J. Sjöblom, Langmuir 4, 360 (1988).CrossRefGoogle Scholar
  27. 27.
    K. Holmberg, J. Surface Sci. Teehnol. 5, 209 (1989).Google Scholar
  28. 28.
    K. M. Larsson, P. Adlercreutz, B. Mattiasson, and U. Olsson, Biotech. Bioeng. 36, 135 (1990).CrossRefGoogle Scholar
  29. 29.
    P. D. I. Fletcher, B. H. Robinson, R. B. Freedman, and C. Oldfield, J. Chem. Soc, Faraday Trans. 181, 2667 (1985).Google Scholar
  30. 30.
    K. Bergström and K. Holmberg, Swedish patent application 8904396-2 (1989).Google Scholar
  31. 31.
    S. Lapanje, Physicochemical Aspects of Protein Denaturation, Wiley, New York (1978).Google Scholar
  32. 32.
    E. Österberg, C. Ristoff, and K. Holmberg, Tenside 25, 293 (1988).Google Scholar
  33. 33.
    W. H. Scouten, in: Methods in Enzymology, Vol. 135: Immobilized Enzymes and Cells, Part B (K. Mosbach, ed.), p. 30, Academic Press, New York (1987).CrossRefGoogle Scholar
  34. 34.
    C. Tanford, J. Am. Chem. Soc. 84, 4240 (1962).CrossRefGoogle Scholar
  35. 35.
    J. March, Advanced Organic Chemistry, 3rd ed., p. 316, Wiley, New York (1985).Google Scholar
  36. 36.
    K. Holmberg and M.-B. Stark, Colloids Surfaces 47, 211 (1990).CrossRefGoogle Scholar
  37. 37.
    E. Engvall and P Perlmann, Immunochemistry 8, 871 (1971).PubMedCrossRefGoogle Scholar
  38. 38.
    A. Voller and D. E. Bidwell, in: Alternative Immunoassays (W. P Collins, ed.), Chapter 6, Wiley, New York (1985).Google Scholar
  39. 39.
    A. Gardas and A. Lewartowska, J. Immunol. Methods 106, 251 (1988).PubMedCrossRefGoogle Scholar
  40. 40.
    G. E. Kenny and C. L. Dunsmoor, Isr. J. Med. Sci. 23, 732 (1987).PubMedGoogle Scholar
  41. 41.
    K. Bergström and K. Holmberg, Colloids Surfaces, in press.Google Scholar
  42. 42.
    R. K. Oldham, J. R. Maleckar, J. R. Yannelli, and W. H. West, Cancer Treat. Rev. 16, 5 (1989).PubMedCrossRefGoogle Scholar
  43. 43.
    S. A. Rosenberg, M. T. Lotse, and J. J. Mulé, Ann. Intern. Med. 108, 853 (1988).PubMedCrossRefGoogle Scholar
  44. 44.
    K. A. Smith, Annu. Rev. Cell Biol. 5, 397 (1989).PubMedCrossRefGoogle Scholar
  45. 45.
    S. C. Saris, S. A. Rosenberg, R. B. Friedman, J. T. Rubin, D. Barba, and E. H. Oldfield, J. Neurosurg, 69, 29 (1988).PubMedCrossRefGoogle Scholar
  46. 46.
    T. Maack, V Johnson, S. T. Kau, J. Figueiredo, and D. Sigulem, Kidney International 16, 251 (1979).PubMedCrossRefGoogle Scholar
  47. 47.
    N. V. Katre, M. J. Knauf, and W J. Laird, Proc. Natl. Acad. Sci. U.S.A. 84, 1487 (1987).PubMedCrossRefGoogle Scholar
  48. 48.
    H. Hydén and K. Holmberg, Arzneim.-Forsch./ Drug Res. 36, 120 (1986).Google Scholar
  49. 49.
    K. Bergström, K. Holmberg, H. Hydén, A. Hyltander, and K. Lundholm, unpublished work.Google Scholar
  50. 50.
    S. Srivastava, S. D. Gorham, and J. M. Courtney, Biomaterials 11, 162 (1990).PubMedCrossRefGoogle Scholar
  51. 51.
    F. Grinell, Int. Rev. Cytol. 53, 65 (1978).CrossRefGoogle Scholar
  52. 52.
    K. Hirai, Y. Shimizu, and T. Hino, J. Exp. Pathol. 71, 51 (1990).Google Scholar
  53. 53.
    S. Srivastava, S. D. Gorham, D. A. French, A. A. Shivas, and J. M. Courtney, Biomaterials 11, 155 (1990).PubMedCrossRefGoogle Scholar
  54. 54.
    K. Bergström and K. Holmberg, to appear.Google Scholar
  55. 55.
    M.-B. Stark and K. Holmberg, Biotech. Bioeng. 34, 942 (1989).CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1992

Authors and Affiliations

  • Krister Holmberg
    • 1
  • Karin Bergström
    • 1
  • Maj-Britt Stark
    • 2
  1. 1.Berol NobelStenungsundSweden
  2. 2.Department of HistologyUniversity of GöteborgGöteborgSweden

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