Influence of endogenous albumin binding on blood-material interactions

R. C. Eberhart, M. S. Munro, J. R. Frautschi, M. Lubin, F. J. Clubb, C. W. Miller, V. I. Sevastianov

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A method has been developed to enhance the albumin affinity of a number of medical polymers, based on alkylation of the surface with straight-chain 16- or 18-carbon alkyl groups. This method has been demonstrated to induce the rapid binding of albumin from single and binary protein solutions, from plasma, and apparently, from whole blood. The bound albumin resists fluid shear or chemically induced desorption. Fibrinogen adsorption is inhibited in vitro and in vivo. Complement protein C3 activation from plasma is inhibited. Fibrin formation and platelet aggregation is inhibited in short-term in vivo experiments. Long-term catheter implant studies suggest that the C18 alkylation is more effective than most, if not all, currently available treatments for the retention of a clean, biocompatible, blood-contacting surface. No data have been obtained to date that conflict with the hypothesis that a renewable albumin layer, so formed, blocks the adsorption or conformational alteration of plasma proteins that otherwise might initiate or participate in various host defenses.

Original languageEnglish (US)
Pages (from-to)78-95
Number of pages18
JournalAnnals of the New York Academy of Sciences
Publication statusPublished - 1987


ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Eberhart, R. C., Munro, M. S., Frautschi, J. R., Lubin, M., Clubb, F. J., Miller, C. W., & Sevastianov, V. I. (1987). Influence of endogenous albumin binding on blood-material interactions. Annals of the New York Academy of Sciences, 516, 78-95.