Fluorometric investigation on the interaction of oleanolic acid with bovine serum albumin
Fluorometric investigation on the interaction of oleanolic acid with bovine serum albumin
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DOI：
10.1016/j.molstruc.2007.08.020
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发表时间：
2008-05-15
影响因子：
3.8
通讯作者：
Zhang, Yuntao
中科院分区：
文献类型：
--
作者：
Cheng, Zhengjun;Zhang, Yuntao
采用荧光光谱、圆二色谱、紫外-可见吸收光谱和傅里叶变换红外光谱研究了生理条件下油酸与牛血清白蛋白（BSA）的相互作用。通过对不同温度下发射猝灭的光谱分析，揭示了油酸对牛血清白蛋白的猝灭机理为静态猝灭机理。得到了不同温度下的结合位点数n和结合常数K。根据Forster能量转移理论计算了油酸和蛋白质之间的距离r。红外光谱、圆二色光谱和紫外-可见吸收光谱实验结果表明，油酸对蛋白质的二级结构产生了干扰。根据van 't霍夫方程计算了热力学参数Δ H-0、Δ G（0）和Δ S-0，表明氢键和货车德瓦耳力是稳定配合物的分子间力.分子模拟研究了BSA与油酸的相互作用。(C)2007 Elsevier B. V.保留所有权利。
The interactions between oleanolic acid and bovine serum albumin (BSA) have been studied by fluorescence, circular dichroism (CD), UV-vis absorption and Fourier transform infrared spectroscopy (FTIR) under physiological conditions. Spectroscopic analysis of the emission quenching at different temperatures has revealed that the quenching mechanism of bovine serum albumin by oleanolic acid is static quenching mechanism. The binding sites number n and binding constants K are obtained at various temperatures. The distance r between oleanolic acid and the protein is evaluated according to the theory of Forster energy transfer. The results by FTIR, CD and UV-vis absorption spectra experiment indicate that the secondary structures of protein have been perturbed in the presence of oleanolic acid. The thermodynamic parameters Delta H-0, Delta G(0), and Delta S-0 are calculated according to van't Hoff equation, which indicates that the hydrogen bonds and van der-waals are the intermolecular forces stabilizing the complex. Molecular modeling studies the interaction BSA with oleanolic acid. (C) 2007 Elsevier B.V. All rights reserved.