光谱法及分子对接研究邻苯二甲酸单乙基己基酯与人血清白蛋白的相互作用  

Study on the interaction between mono( 2-ethylhexyl ) phthalate and HAS by spectrometry and molecular docking

作　　者：庹浔 饶博文 徐霖霖 刘昭清 吕小兰 TUO Xun;RAO Bo-wen;XU Lin-lin;LIU Zhao-qing;Lv Xiao-lan(College of Chemistry,Nanchang University,Nanchang 330000;School of Pharmacy,Nanchang University,Nanchang 330000)

机构地区：[1]南昌大学化学学院,南昌330000 [2]南昌大学药学院,南昌330000

出　　处：《分析试验室》2019年第12期1381-1386,共6页Chinese Journal of Analysis Laboratory

基　　金：国家自然科学基金(31860153);江西省自然科学基金面上项目(20181BAB204003)资助

摘　　要：通过荧光光谱法、紫外分光光度法以及分子对接技术探究邻苯二甲酸单乙基己基酯(MEHP)与人血清白蛋白(HSA)之间的相互作用及其作用机制。光谱学数据显示,MEHP诱导HSA内源荧光猝灭是因为两者间发生非辐射能量转移并形成稳定的复合物;不同温度下的热力学常数表明范德华力或氢键为MEHP与HSA结合的主要驱动力;三维荧光光谱结果证实MEHP改变了HSA的构象;同步荧光光谱和位点实验表明,MEHP在位点Ⅰ与HSA结合。根据光谱学的研究结果,采用分子对接技术模拟MEHP与HSA在分子水平上的相互作用机制,结果与光谱学研究结果一致。In this study,the interaction mechanisms between Mono(2-ethylhexyl)phthalate(MEHP)and human serum albumin(HSA)were investigated by fluorescence spectroscopy,ultraviolet spectrophotometry and molecular docking method.Data from spectroscopy studies revealed that MEHP induced endogenous fluorescence quenching of HSA due to non-radiative energy transfer and formation of stable complexes.The thermodynamic constants indicated that Van der Waals forces or hydrogen bonds were the main driving force for the combination of MEHP and HSA.The results of three-dimensional fluorescence spectroscopy confirmed that the conformation of HSA was changed by MEHP.Based on the results of simultaneous fluorescence spectroscopy and site experiments,it indicated that the bind site of MEHP-HSA complex located on the site I of HSA.Finnally,the molecular docking technique was used to simulate the interaction mechanism between MEHP and HSA at the molecular level,and the results were consistent with the results of spectroscopy studies.

关 键 词：塑化剂 邻苯二甲酸单乙基己基酯 HSA 光谱法 分子对接 

分 类 号：TQ937[化学工程]