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Plasma protein adsorption to surfaces grafted with dense homopolymer and copolymer brushes containing poly(N-isopropylacrylamide)

TitlePlasma protein adsorption to surfaces grafted with dense homopolymer and copolymer brushes containing poly(N-isopropylacrylamide)
Publication TypeJournal Article
Year of Publication2004
AuthorsJanzen, J, Le, Y, Kizhakkedathu, JN, Brooks, DE
JournalJournal of Biomaterials Science-Polymer Edition
Volume15
Pagination1121-1135
Type of ArticleProceedings Paper
ISBN Number0920-5063
KeywordsADSORPTION, BIOMATERIALS, block copolymer, CHROMATOGRAPHY, FIBRINOGEN ADSORPTION, grafted latex, I-125 radiolabel, MODEL, OXIDE), plasma protein, POLY(ETHYLENE GLYCOL), POLY(N-ISOPROPYLACRYLAMIDE), polymer brush, POLYMER BRUSHES, PREVENTION, SDS-PAGE, SELF-ASSEMBLED MONOLAYERS, SERUM-ALBUMIN ADSORPTION
Abstract

Growing polymer chains from surface initiators in principle allows much more dense polymer surface layers to be created than can be produced by grafting of whole (self-excluding) chains. We have utilized aqueous atom transfer radical polymerization to graft a series of cleavable hydrophilic poly (N-isopropylacrylamide) (PNIPAM) homopolymers and block copolymers of substituted acry-lamides from polystyrene latex to give brushes of controlled MW and surface density. Average chain separations much less than their free solution radii of gyration have been achieved. Exposure to radiolabeled single proteins or to whole plasma and subsequent analysis by SDS-PAGE shows that PNIPAM brushes decrease protein adsorption relative to the latex surface or other substituted polyacrylamides. The PNIPAM brushes exhibit a second-order phase transition around 30degreesC as reflected by a decrease in the hydrodynamic thickness of the brush at higher temperatures. Total plasma protein adsorption is increased at 40degreesC compared to 20degreesC but there is significant differential adsorption behavior among the proteins detected by gel-electrophoresis analysis.

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