Investigation of the interaction between endocrine disruptor bisphenol A and human serum albumin.

Investigation of the interaction between endocrine disruptor bisphenol A and human serum albumin.
复制标题

DOI:
10.1016/j.chemosphere.2010.04.076
复制
发表时间:
2010-08
期刊:
影响因子:
8.8
通讯作者:
Xiao-yun Xie;Xiao-ru Wang;Xiangmei Xu;Huijun Sun;Xingguo Chen
Xiao-yun Xie;Xiao-ru Wang;Xiangmei Xu;Huijun Sun;Xingguo Chen
中科院分区:
环境科学与生态学2区
文献类型:
--
作者:
Xiao-yun Xie;Xiao-ru Wang;Xiangmei Xu;Huijun Sun;Xingguo Chen

文献摘要

被引文献

相似文献

本研究采用分子模拟、荧光光谱、紫外-可见光谱(UV-Vis)、傅里叶变换红外光谱(FT-IR)和圆二色谱(CD)等方法研究了内分泌干扰物双酚A(BPA)与人血清白蛋白(HSA)的相互作用。用Scatchard方程测定了BPA与HSA的缔合常数。测定了结合反应的热力学参数(ΔG0、ΔH0和ΔS0),表明BPA-HSA相互作用中存在疏水作用力,与分子模拟结果吻合较好。用UV-Vis、FT-IR和CD光谱证实了双酚A对蛋白质二级结构的影响。根据Förster的无辐射能量转移理论计算了BPA与HSA的平均结合距离r=1.82 nm。
In this study, the interaction of the endocrine disruptor bisphenol A (BPA) and human serum albumin (HSA) was investigated by molecular modelling, fluorescence, ultraviolet–visible spectroscopy (UV–vis), Fourier transform infrared spectroscopy (FT-IR) and circular dichroism spectroscopy (CD). The association constants between BPA and HSA were determined using the Scatchard equation. The thermodynamic parameters of the binding reaction (ΔG0, ΔH0and ΔS0) were measured, and they indicated the presence of hydrophobic forces in the BPA–HSA interaction, which agreed well with the results from molecular modelling. The alterations of protein secondary structure in the presence of BPA were confirmed by UV–vis, FT-IR and CD spectroscopy. Lastly, the average binding distance, r, between BPA and HSA was evaluated and found to be 1.82nm according to Förster’s theory of non-radiation energy transfer.