Investigation on the interaction between endocrine disruptor triphenyltin with human serum albumin

文献类型： 外文期刊

第一作者： Geng, Bing

作者： Geng, Bing;Liu, Xue;Tian, Yunlong;Ye, Jing;Li, Hongna;Wu, Jinbao

作者机构：

关键词： Human serum albumin (HSA);Triphenyltin (TPT);Fluorescence spectra;Toxicity

期刊名称：SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY （ 影响因子：4.098； 五年影响因子：3.464 ）

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收录情况： SCI

摘要： The interaction between triphenyltin (TPT) and human serum albumin (HSA) in physiological buffer(pH = 7.4) was investigated by the fluorescence quenching technique. The results of fluorescence titration revealed that TPT could strongly quench the intrinsic fluorescence of HSA through a static quenching procedure. The apparent binding constants K and number of binding sites n of TPT with HSA were 2.51 × 10~3 and 0.96 at 298 K which were obtained by the fluorescence quenching method. The thermodynamic parameters enthalpy change (DH), entropy change (DS) were positive, which indicated that the interaction of TPT with HSA was driven mainly by hydrophobic forces. The process of binding was a spontaneous process in which Gibbs free energy change was negative. The distance r between donor (HSA) and acceptor(TPT) was calculated to be 3.13 nm based on Forster’s non-radiative energy transfer theory. The results of synchronous fluorescence, three-dimensional fluorescence and circular dichroism (CD) spectra showed that the triphenyltin induced conformational changes of HSA.

分类号： O657.3

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