Influence of macromolecular crowding upon the stability and state of association of proteins: Predictions and observations

被引:220
作者
Minton, AP [1 ]
机构
[1] NIDDKD, Lab Biochem & Genet, NIH, US PHS, Bethesda, MD 20892 USA
关键词
protein denaturation; protein aggregation; macromolecular excipients;
D O I
10.1002/jps.20417
中图分类号
R914 [药物化学];
学科分类号
100701 ;
摘要
The concept of excluded volume and possible effects of excluded volume on the reactivity of macromolecules in highly volume-occupied or 'crowded' media are introduced and briefly summarized. Theoretical and experimental studies of the effect of crowding on protein folding and unfolding, and on the effect of crowding on protein association and aggregation, are reviewed. Possible effects of the effect of crowding on an initially native protein that can undergo unfolding, self-association of native protein, and/or aggregation of non-native protein are considered. (c) 2005 Wiley-Liss, Inc.
引用
收藏
页码:1668 / 1675
页数:8
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