计算模拟与光谱法研究4-羟基-2,2’,3,4’-四溴二苯醚与人血清白蛋白的相互作用

发布时间：2018-05-18 14:13

本文选题：羟基化多溴联苯醚 + 人血清白蛋白　；参考：《化学通报》2017年02期

【摘要】：利用分子模拟、荧光光谱、紫外吸收光谱等方法,研究了4-羟基-2,2’,3,4’-四溴二苯醚(4-OHBDE-42)与人血清白蛋白(HSA)的相互作用。三维荧光分析表明,4-OH-BDE-42的存在降低了HSA的荧光强度,且使HSA的微环境和构象发生变化。荧光光谱和紫外吸收光谱显示,4-OH-BDE-42与HSA结合后显著猝灭了HSA的内源性荧光,猝灭机制为静态猝灭与非辐射能量转移。结合常数Ka106L·mol-1,表明两者的结合作用较强,结合距离r为3.66nm。根据热力学参数分析,ΔH0,ΔS0,即4-OH-BDE-42与HSA之间结合的主要作用力为疏水作用,这与分子对接、结合自由能分析结论一致。结合自由能贡献分析表明,LYS199、GLU292、ARG257、ARG218、ALA291、HIS242为4-OH-BDE-42与HSA结合的关键氨基酸残基。
[Abstract]:The interaction between 4-OHBDE-42 (4-OHBDE-42) and human serum albumin (HSA) was studied by molecular simulation, fluorescence spectra and UV absorption spectra. Three-dimensional fluorescence analysis showed that the presence of 4-OH-BDE-42 reduced the fluorescence intensity of HSA and changed the microenvironment and conformation of HSA. Fluorescence spectra and UV absorption spectra showed that 4-OH-BDE-42 significantly quenched the endogenous fluorescence of HSA after binding with HSA. The quenching mechanism was static quenching and non-radiative energy transfer. The binding constant Ka106L mol-1 indicates that the binding distance is 3.66 nm. According to thermodynamic parameter analysis, 螖 H _ 0, 螖 S _ 0, that is, the hydrophobic interaction between 4-OH-BDE-42 and HSA is the main force, which is consistent with the conclusion of molecular docking and binding free energy analysis. The combined free energy contribution analysis showed that LYS199GLU292AG257ALA291HIS242 was the key amino acid residue for the binding of 4-OH-BDE-42 and HSA.
【作者单位】：桂林理工大学化学与生物工程学院广西高校食品安全与检测重点实验室岩溶地区水污染控制与用水安全保障协同创新中心;
【基金】：国家自然科学基金项目(21267008) 广西自然科学基金项目(2013GXNSFAA019034) 广西高等学校高水平创新团队及卓越学者计划项目(桂教人[2014]49号)资助
【分类号】：R99;O657.3

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