Spectroscopic studies on the interaction between an anticancer drug ampelopsin and bovine serum albumin
Spectroscopic studies on the interaction between an anticancer drug ampelopsin and bovine serum albumin
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DOI：
10.1016/j.saa.2011.11.048
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发表时间：
2012-02-15
影响因子：
4.4
通讯作者：
Zeng, Zhengzhi
中科院分区：
文献类型：
--
作者：
Shi, Yanjun;Liu, Hongyan;Zeng, Zhengzhi
在模拟生理条件下，用荧光光谱、圆二色谱和时间分辨光谱研究了抗癌药物蛇葡萄素(AMP)与牛血清白蛋白(BSA)的相互作用。荧光数据表明，AMP对牛血清白蛋白的本征荧光有较强的猝灭作用。计算了结合常数和结合位点数。热力学参数表明，氢键和弱范德华力在相互作用中起主要作用。位点标记竞争实验表明，AMP与BSA的结合可能位于第III位。根据Forster理论，得到AMP与BSA的平均结合距离(r=5.47 nm)。根据同步荧光光谱、CD数据和平均荧光寿命值，AMP与BSA的结合导致了BSA的构象变化。(C)2011爱思唯尔B.V.保留所有权利。
The interaction between bovine serum albumin (BSA) and the anticancer drug molecule ampelopsin (AMP) was investigated using fluorescence spectroscopy, circular dichroism (CD) spectra, and time-resolved spectra under simulated physiological conditions. Fluorescence data showed that the intrinsic fluorescence of BSA was strongly quenched by AMP in terms of a dynamic quenching process. Binding constants and binding sites were calculated. The thermodynamic parameters indicated that the hydrogen bonding and weak van der Waals force played a major role in the interaction. The site marker competitive experiments suggested that the binding site of AMP and BSA was probably located on site III. Based on the Forster's theory, the average binding distance between AMP and BSA was obtained (r=5.47 nm). The binding of AMP and BSA leaded to conformational changes of BSA according to synchronous fluorescence spectra, CD data and mean fluorescence lifetime values. (C) 2011 Elsevier B.V. All rights reserved.