Interaction of bovine serum albumin and human blood plasma with PEO-tethered surfaces : influence of PEO chain length, grafting density, and temperature

Solid surfaces are modified by grafting poly(ethylene oxide), PEO, to influence their interaction with indwelling particles, in particular molecules of bovine serum albumin and human plasma proteins. As a rule, the grafted PEO layers suppress protein adsorption. The suppression is most effective whe...

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Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1992. - 20(2004), 10 vom: 11. Mai, Seite 4162-7
1. Verfasser: Norde, Willem (VerfasserIn)
Weitere Verfasser: Gage, Dick
Format: Aufsatz
Sprache:English
Veröffentlicht: 2004
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Biocompatible Materials Blood Proteins Serum Albumin, Bovine 27432CM55Q Polyethylene Glycols 3WJQ0SDW1A
Beschreibung
Zusammenfassung:Solid surfaces are modified by grafting poly(ethylene oxide), PEO, to influence their interaction with indwelling particles, in particular molecules of bovine serum albumin and human plasma proteins. As a rule, the grafted PEO layers suppress protein adsorption. The suppression is most effective when the PEO layer is in a molecular brush conformation having a reciprocal grafting density (area per grafted PEO chain) less than the dimensions of the protein molecules. Nevertheless, the protein molecules may penetrate the PEO brush to some extent. For a given grafting density, the penetration is facilitated by increasing thickness of the brush. Tenuous brushes of reciprocal grafting densities exceeding the protein molecular dimensions enhance protein adsorption. The results point to a weak attractive interaction between PEO and protein. The protein repellency of a densely PEO-brushed surface is ascribed to a high activation energy for the protein molecules to enter the brush. Varying the temperature between 22 and 38 degrees C does not significantly affect the range of grafting density over which the brush changes from protein-attractive to protein-repellent
Beschreibung:Date Completed 31.01.2006
Date Revised 26.10.2019
published: Print
Citation Status MEDLINE
ISSN:1520-5827