The role of electrolytes on protein adsorption at a hydrophilic solid-water interface

被引：24
|
作者：
Wendorf, Janet R. [1 ]
Radke, Clayton J. [1 ]
Blanch, Harvey W. [1 ]
机构：
[1] Univ Calif Berkeley, Dept Chem Engn, Berkeley, CA 94720 USA
来源：
COLLOIDS AND SURFACES B-BIOINTERFACES | 2010年 / 75卷 / 01期
基金：
美国国家科学基金会;
关键词：
Protein adsorption; Solid-liquid interfaces; Salt excipients; Electrolytes; HYDROPHOBIC-INTERACTION CHROMATOGRAPHY; BOVINE SERUM-ALBUMIN; ISOELECTRIC POINT; IONIC-STRENGTH; NEUTRAL SALTS; ZERO CHARGE; STABILITY; SURFACES; TEMPERATURE; LYSOZYME;
D O I：
10.1016/j.colsurfb.2009.08.015
中图分类号：
Q6 [生物物理学];
学科分类号：
071011 ;
摘要：
The adsorption of four proteins, RNase A. HEWL, BSA. and beta-Lac, was examined on the surface of a negatively charged SiO2/TiO2 optical waveguide. The amount of adsorbed protein followed the salt series Mg2+ > Li+ > Na+ > K+ and for anions Cl- > Br- > I- This ordering was attributed to protein adsorption being primarily influenced by changes in hydrophobic interactions between the surface and the protein resulting from differences in water structure arising from the presence of electrolytes (C) 2009 Elsevier B V All rights reserved
引用
收藏
页码：100 / 106
页数：7
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