Fluorescence spectroscopy study on the interaction between Gossypol and bovine serum albumin
Fluorescence spectroscopy study on the interaction between Gossypol and bovine serum albumin
复制标题
棉酚与牛血清白蛋白相互作用的荧光光谱研究
DOI：
10.1016/j.molstruc.2008.10.053
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发表时间：
2009-02-28
影响因子：
3.8
通讯作者：
Guo, Peng
中科院分区：
文献类型：
--
作者：
Yang, Jian;Jing, Zheng Hua;Guo, Peng
用荧光光谱法研究了棉酚与牛血清白蛋白（BSA）结合反应的特征。结果表明，棉酚对牛血清白蛋白的荧光猝灭是一个静态猝灭过程。在293和303 K下，棉酚与BSA的结合常数K-A分别为1.51 × 10 ~（6）和1.15 × 10 ~（6）L·mol ~（-1）。棉酚与BSA之间只有一个结合位点。根据热力学参数。更可能的是疏水和静电相互作用参与结合过程。根据Forster非辐射能量转移理论，求得了供体（BSA）与受体（棉酚）之间的平均结合距离（r = 2.18nm）。用同步荧光光谱法研究了棉酚对牛血清白蛋白构象的影响。(C)2008 Elsevier B. V.保留所有权利。
The characteristics of the binding reaction of Gossypol with bovine serum albumin (BSA) were studied by fluorescence spectroscopy. The experimental results showed that Gossypol caused the fluorescence quenching of BSA through a static quenching procedure. The binding constant K-A of Gossypol with BSA at 293 and 303 K were obtained as 1.51 X 10(6) and 1.15 x 10(6) L mol(-1), respectively. There is one binding site between Gossypol and BSA. According to the thermodynamic parameters. it is more likely that hydrophobic and electrostatic interactions are involved in the binding process. Based on the Forster non-radiation energy transfer theory, the average binding distance between the donor (BSA) and the acceptor (Gossypol) was obtained (r = 2.18 nm). The effect of Gossypol on the conformation of BSA was analyzed using synchronous fluorescence spectroscopy. (C) 2008 Elsevier B.V. All rights reserved.