Alkylated cellulosic membranes with enhanced albumin affinity: influence of competing proteins.

J. R. Frautschi, R. C. Eberhart, J. A. Hubbell

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

4-Vinyl pyridine was grafted to the surface of the cellulosic membrane Cuprophan, and subsequently alkylated with both non-fatty acid-like C10 (GVP-C10) and fatty acid-like C16 (GVP-C16) aliphatic chains. In vitro albumin adsorption studies from single and binary protein solutions, as well as from dilute plasma demonstrated a significant enhancement (1.4-3.89 times) of albumin binding to both the GVP-C10 and GVP-C16 surfaces, relative to unmodified Cuprophan. It is speculated that enhanced albumin adsorption to a surface may improve surface thromboresistance. Further, these results suggest that there is no difference between the enhanced albumin adsorption of the fatty acid and nonfatty like alkyl chains, C10 and C16.

Original languageEnglish
Pages (from-to)563-575
Number of pages13
JournalJournal of biomaterials science. Polymer edition
Volume7
Issue number7
StatePublished - Dec 1 1995
Externally publishedYes

Fingerprint

Albumins
Adsorption
Proteins
Membranes
Fatty acids
Fatty Acids
Pyridine
Plasmas
Acids
cuprammonium cellulose

ASJC Scopus subject areas

  • Biophysics
  • Biomaterials

Cite this

Alkylated cellulosic membranes with enhanced albumin affinity : influence of competing proteins. / Frautschi, J. R.; Eberhart, R. C.; Hubbell, J. A.

In: Journal of biomaterials science. Polymer edition, Vol. 7, No. 7, 01.12.1995, p. 563-575.

Research output: Contribution to journalArticle

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