Influence of substrate hydrophobicity on the adsorption of collagen in the presence of pluronic F68, albumin, or calf serum

被引：79

作者：

Dewez, JL

Berger, V

Schneider, YJ

Rouxhet, PG

机构：

[1] UNIV CATHOLIQUE LOUVAIN,UNITE CHIM INTERFACES,B-1348 LOUVAIN,BELGIUM

[2] UNIV CATHOLIQUE LOUVAIN,ADV MAT RES CTR,B-1348 LOUVAIN,BELGIUM

[3] UNIV CATHOLIQUE LOUVAIN,BIOCHIM CELLULAIRE LAB,B-1348 LOUVAIN,BELGIUM

来源：

JOURNAL OF COLLOID AND INTERFACE SCIENCE | 1997年 / 191卷 / 01期

关键词：

adsorption; adsorption competition; protein; collagen; Pluronic; human serum albumin; fetal calf serum; polystyrene surface; cell adhesion;

D O I：

10.1006/jcis.1997.4908

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

The influence of Pluronic F68 [a poly(ethylene oxide)-poly(propylene oxide)-poly(ethylene oxide) copolymer surfactant], serum albumin (HSA), and fetal calf serum (FCS) on the adsorption of type I collagen by polymer substrates was investigated using radiolabeling and XPS analysis. Three different kinds of polystyrene substrates with increasing level of hydrophobicity were used. Change in the state of hydration of the sorbent and protein surfaces appears to be the main driving force for collagen adsorption. Pluronic F68 strongly reduces collagen adsorption, the reduction being more pronounced with higher substrate hydrophobicity. This explains why epithelial cell adhesion on substrates preconditioned with a solution of Pluronic F68 and collagen is strongly influenced by substrate hydrophobicity. Collagen adsorption is also reduced in the presence of HSA and FCS, but the reduction and its sensitivity to substrate hydrophobicity are lower than with Pluronic F68. (C) 1997 Academic Press.

引用

页码：1 / 10

页数：10

共 68 条

[1] PROTEIN ADSORPTION TO POLYMER PARTICLES - ROLE OF SURFACE-PROPERTIES [J].