Spectroscopic studies on binding of Puerarin to human serum albumin

被引:25
作者
Li, Jinhua [1 ]
Ren, Cuiling [1 ]
Zhang, Yaheng [1 ]
Liu, Xiaoyan [1 ]
Yao, Xiaojun [1 ]
Hu, Zhide [1 ]
机构
[1] Lanzhou Univ, Dept Chem, Lanzhou 730000, Peoples R China
关键词
Puerarin; human serum albumin; fluorescence quenching technique; circular dichroism; FT-IR spectroscopy; molecular modeling;
D O I
10.1016/j.molstruc.2007.10.020
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 interaction between Puerarin with human serum albumin has been studied for the first time by spectroscopic methods including fluorescence quenching technology, circular dichroism (CD) spectroscopy and Fourier transform infrared (FT-IR) spectroscopy under simulative physiological conditions. The results of fluorescence titration revealed that Puerarin can strongly quench the intrinsic fluorescence of HSA by static quenching and there is a single class of binding site on HSA. In addition, the studies of CD spectroscopy and FT-IR spectroscopy showed that the binding of Puerarin to HSA changed slightly molecular conformation of HSA. Furthermore, the thermodynamic functions Delta H degrees and Delta S degrees for the reaction were calculated to be -9.067 U mol(-1) and 54.315 J mol(-1) K-1 according to van't Hoff equation. These data suggested that both hydrogen bond and hydrophobic interaction play a major role in the binding of Puerarin to HSA, which is in good agreement with the result of molecular modeling study. (C) 2008 Published by Elsevier B.V.
引用
收藏
页码:64 / 69
页数:6
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