Study on the interaction of 6-thioguanine with bovine serum albumin by spectroscopic techniques
Study on the interaction of 6-thioguanine with bovine serum albumin by spectroscopic techniques
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光谱技术研究6-硫鸟嘌呤与牛血清白蛋白的相互作用
DOI：
10.1016/j.molstruc.2008.10.041
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发表时间：
2009-02-28
影响因子：
3.8
通讯作者：
Lu, Zuhong
中科院分区：
文献类型：
--
作者：
Qu, Peng;Lu, Hua;Lu, Zuhong
用紫外-可见吸收光谱、圆二色谱和荧光光谱研究了6-硫代鸟嘌呤(6-TG)与牛血清白蛋白(BSA)的相互作用。实验结果表明，6-TG对BSA的猝灭机理为静态猝灭。评估了各种结合参数。Delta H-0、Delta G(0)和Delta S-0表明，6-TG与牛血清白蛋白相互作用时，疏水作用力起主要作用。根据Forster的非辐射能量转移理论，计算了供体(BSA)和受体(6-Tg)之间的结合距离r。圆二色谱结果表明，6-TG与BSA的结合引起了BSA的构象变化。(C)2008爱思唯尔B.V.保留所有权利。
The interaction of 6-thioguanine (6-TG) and bovine serum albumin (BSA) was investigated by UV-Vis absorption, circular dichroism (CD) spectra and florescence spectroscopy. The experimental results indicated that the quenching mechanism of BSA by 6-TG was a static quenching procedure. Various binding parameters have been evaluated. Delta H-0, Delta G(0) and Delta S-0, indicated that hydrophobic forces played a major role when 6-TG interacted with BSA. Based on the Forster's theory of non-radiation energy transfer, the binding distance, r between the donor (BSA) and acceptor (6-TG) was evaluated. CD spectral results showed that the binding of 6-TG to BSA induced conformational changes in BSA. (C) 2008 Elsevier B.V. All rights reserved.