荧光光谱法结合分子对接研究邻苯二甲酸单环己酯与牛血清白蛋白的相互作用  

Intermolecular interactions between monocyclohexyl phthalate and bovine serum albumin

作　　者：杨雯雁 马秀兰 张宇 YANG Wenyan;MA Xiulan;ZHANG Yu(Yunnan Electric Power Test and Research Institute(Group)Co.Ltd.,Kunming 650217,China;School of Pharmacy,Nanchang University,Nanchang 330000,China)

机构地区：[1]云南电力试验研究院(集团)有限公司,昆明650217 [2]南昌大学药学院,南昌330000

出　　处：《分析试验室》2023年第9期1236-1241,共6页Chinese Journal of Analysis Laboratory

摘　　要：通过荧光光谱、圆二色谱及计算机模拟技术研究了邻苯二甲酸单环己酯(MCHP)与牛血清白蛋白(BSA)的相互作用机制。结果表明:MCHP能够自发进入BSA的结合位点I,并引起BSA的内源荧光猝灭;BSA-MCHP复合物的稳定性随着温度上升而下降;除了氢键和范德华力,MCHP与BSA之间的Pi-Sigma、Pi-Alkyl以及Alkyl作用力在结合过程中也发挥了重要作用;MCHP诱导BSA的二级结构发生改变,其中α-螺旋的含量从游离态的66.5%下降至复合态的59.0%;计算机模拟结果表明,BSA的Trp213和Arg198残基与MCHP的2个羰基上的氧原子形成2个氢键,并且Trp213与MCHP之间的相互作用是导致BSA荧光猝灭的重要因素。The interaction mechanism between monocyclohexyl phthalate(MCHP)and bovine serum albumin(BSA)was studied by fluorescence spectroscopy,circular dichroism and computer simulation techniques.The results showed that MCHP can spontaneously enter the binding site I of BSA and cause the endogenous fluorescence quenching of BSA.The stability of BSA-MCHP complex decreased with the increase of temperature.In addition to hydrogen bond and van der Waals force,the Pi-Sigma,Pi-Alkyl and Alkyl forces also played an important role in the binding process.The secondary structure of BSA was changed by MCHP and the content of α-helix decreased from 66.5% in free state to 59.0% in complex state.Computer simulation results indicated that Trp213 and Arg198 residues of BSA formed two hydrogen bonds with the oxygen atoms on the two carbonyl groups of MCHP and the interaction between Trp213 and MCHP was an important factor causing the quenching of BSA fluorescence.

关 键 词：邻苯二甲酸单环己酯 牛血清白蛋白 多光谱实验 分子对接 相互作用 

分 类 号：TQ414[化学工程]