Alkylated cellulosic membranes with enhanced albumin affinity: Influence of competing proteins

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

doi:10.1163/156856295X00481

Alkylated cellulosic membranes with enhanced albumin affinity: Influence of competing proteins

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

Surgery

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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-C 16 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 language	English (US)
Pages (from-to)	563-575
Number of pages	13
Journal	Journal of Biomaterials Science, Polymer Edition
Volume	7
Issue number	7
DOIs	https://doi.org/10.1163/156856295X00481
State	Published - Jan 1 1995

Keywords

Hemodialysis membrane
Polymer
Protein adsorption
Surface modification

ASJC Scopus subject areas

Biophysics
Bioengineering
Biomaterials
Biomedical Engineering

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10.1163/156856295X00481

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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-C 16 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.",

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T1 - Alkylated cellulosic membranes with enhanced albumin affinity

T2 - Influence of competing proteins

AU - Frautschi, J. R.

AU - Eberhart, R. C.

AU - Hubbell, J. A.

PY - 1995/1/1

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N2 - 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-C 16 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.

AB - 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-C 16 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.

KW - Hemodialysis membrane

KW - Polymer

KW - Protein adsorption

KW - Surface modification

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Alkylated cellulosic membranes with enhanced albumin affinity: Influence of competing proteins

Abstract

Keywords

ASJC Scopus subject areas

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