高等学校化学学报 ›› 2015, Vol. 36 ›› Issue (3): 516-522.doi: 10.7503/cjcu20141007

• 物理化学 • 上一篇    下一篇

2'-羟基-2,4-二溴二苯醚与人血清白蛋白作用机制的光谱研究与计算模拟

董露1, 易忠胜1(), 伍智蔚1, 王海洋1, 张爱茜2   

  1. 1. 桂林理工大学化学与生物工程学院, 桂林 541004
    2. 环境化学与生态毒理学国家重点实验室, 中国科学院生态环境研究中心, 北京 100085
  • 收稿日期:2014-11-17 出版日期:2015-03-10 发布日期:2015-01-30
  • 作者简介:联系人简介: 易忠胜, 男, 博士, 教授, 主要从事化学计量学和环境毒理学研究. E-mail: yzs@glut.edu.cn
  • 基金资助:
    国家自然科学基金(批准号: 21267008, 21167006)和广西自然科学基金(批准号2013GXNSFAA 019034)资助

Mechanism Study on the Interaction Between 2'-Hydroxy-2,4-dibromo Diphenyl Ethers and Human Serum Albumin Based on Spectroscopic Methods and Computional Simulations

DONG Lu1, YI Zhongsheng1,*(), WU Zhiwei1, WANG Haiyang1, ZHANG Aiqian2   

  1. 1. College of Chemistry and Bioengineering, Guilin University of Technology, Guilin 541004, China
    2. State Key Laboratory of Environmental Chemistry and Ecotoxicology, Research Center for Eco-environmental Sciences,Chinese Academy of Sciences, Beijing 100085, China
  • Received:2014-11-17 Online:2015-03-10 Published:2015-01-30
  • Contact: YI Zhongsheng E-mail:yzs@glut.edu.cn
  • Supported by:
    † Supported by the National Natural Science Foundation of China(Nos.21267008, 21167006) and the Guangxi Natural Science Foundation of China(No.2013GXNSFAA019034)

摘要:

采用分子对接、 分子动力学模拟和光谱法研究了2'-羟基-2,4-二溴二苯醚(2'-OH-BDE-7)与人血清白蛋白(HSA)的相互作用. 同步荧光光谱研究表明, 2'-OH-BDE-7诱导HSA的构象产生变化, 并与分子动力学模拟的结果相吻合. 荧光光谱表明, 2'-OH-BDE-7能引起HSA荧光猝灭, 且其作用机制为静态猝灭和非辐射能量转移. 热力学分析得出ΔG<0, ΔH<0和ΔS<0, 表明氢键和范德华力在HSA-2'-OH-BDE-7的体系中起着重要作用. 竞争实验和分子对接结果表明2'-OH-BDE-7主要结合在HSA的位点Ⅰ. 将计算模拟和光谱实验研究相结合, 为研究小分子和蛋白质相互作用机制提供更多的信息.

关键词: 人血清白蛋白, 2'-羟基-2,4-二溴二苯醚, 荧光光谱法, 分子对接, 分子动力学模拟

Abstract:

The interaction between 2'-hydroxy-2,4-dibromo diphenyl ethers(2'-OH-BDE-7) and human serum albumin(HSA) was investigated with molecular docking, molecular dynamics simulation and spectroscopy techniques. The results of synchronous fluorescence spectroscopy indicated that the conformation of HSA was changed when 2'-OH-BDE-7 binding to HSA, which consistent with the results of molecular dynamics simulations. In addition, the results of fluorescence spectroscopy experiment showed that the intrinsic fluorescence quenching of HSA was reduced by 2'-OH-BDE-7. Static quenching and non-radiation energy transfer are the two main reasons leading to the fluorescence quenching of HSA by 2'-OH-BDE-7. In the process of binding, the entropy, the enthalpy and the Gibbs free energy were negative, which suggested that the interaction between 2'-OH-BDE-7 and HSA was driven mainly by hydrophobic forces and van de Waals forces. Finally, a similar conclusion was obtained from the competitive experiment and molecular docking, which shown 2'-OH-BDE-7 binded human serum albumin at site Ⅰ. Excellent agreement was founded between computer simulations results and spectral experiments to provide more information for the mechanism study on the interaction between 2'-OH-BDE-7 and HSA.

Key words: Human serum albumin, 2'-Hydroxy-2,4-dibromo diphenyl ether(2'-OH-BDE-7), Fluorescence spectrum, Molecular docking, Molecular dynamics simulation

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