A molecular-thermodynamic model for the interactions between globular proteins in aqueous solutions:: Applications to bovine serum albumin (BSA), lysozyme, α-chymotrypsin, and immuno-gamma-globulins (IgG) solutions

被引:35
|
作者
Jin, Lin [1 ]
Yu, Yang-Xin [1 ]
Gao, Guang-Hua [1 ]
机构
[1] Tsinghua Univ, Dept Chem Engn, Beijing 100084, Peoples R China
基金
中国国家自然科学基金;
关键词
osmotic pressure; globular proteins; Yukawa potential; bovine serum albumin; lysozyme; alpha-chymotrypsin; IgG; equation of state;
D O I
10.1016/j.jcis.2006.08.046
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
To investigate globular protein-protein and protein-salt interactions in electrolyte solutions, a potential of mean force including hard-core repulsion, van der Waals attraction and electric double layer repulsion is proposed in this work. Both van der Waals attraction and double-layer repulsion are represented using hard spheres with two-Yukawa tails. The explicit analytical solution of osmotic pressure is derived from the first-order mean spherical approximation. From the comparison between the calculated and experimental values of osmotic pressures for aqueous bovine serum albumin (BSA), lysozyme, alpha-chymotrypsin, and immuno-gamma-globulins (IgG) solutions, we found that the proposed model is adequate for the description of the interactions between proteins at low ionic strength and small self-association of protein molecules. At high ionic strength, the charge inversions of protein molecules should be taken into account. (c) 2006 Elsevier Inc. All rights reserved.
引用
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页码:77 / 83
页数:7
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