Binding affinities of gallotannin analogs with bovine serum albumin: ramifications for polyphenol-protein molecular recognition

被引:45
作者
Feldman, KS [1 ]
Sambandam, A [1 ]
Lemon, ST [1 ]
Nicewonger, RB [1 ]
Long, GS [1 ]
Battaglia, DF [1 ]
Ensel, SM [1 ]
Laci, MA [1 ]
机构
[1] Penn State Univ, Dept Chem, University Pk, PA 16802 USA
关键词
gallotannin; equilibrium dialysis; protein binding;
D O I
10.1016/S0031-9422(99)00144-2
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
A series of gallotannin analogs were prepared by chemical synthesis, and their affinity for the test-case protein bovine serum albumin was measured by equilibrium dialysis. The structure/activity data obtained suggest that the naturally occurring gallotannins, in fact, do not represent the optimal protein recognition agents amongst polyphenolated templates. (C) 1999 Elsevier Science Ltd. All rights reserved.
引用
收藏
页码:867 / 872
页数:6
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