2,3,3'-三氯联苯与人血清白蛋白之间相互作用的计算模拟及光谱研究  

Investigation on Interaction between 2,3,3'-Trichloro Biphenyl and Human Serum Albumin by Computer Simulation and Spectroscopy

作　　者：艾芳婷 易忠胜[1] 蒙延娟 张爱茜[2] 

机构地区：[1]桂林理工大学化学与生物工程学院,广西桂林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

出　　处：《分析测试学报》2014年第2期179-184,共6页Journal of Instrumental Analysis

基　　金：国家自然科学基金(21167006;21267008);广西自然科学基金(2013GXNSFAA019034);环境化学与生态毒理学国家重点实验室开放基金(KF2011-21)

摘　　要：利用分子对接、分子动力学模拟、荧光光谱、紫外光谱及同步荧光光谱法研究了2,3,3'-三氯联苯(PCB-20)与人血清白蛋白(HSA)的相互作用。分子对接结果表明,PCB-20与HSA通过疏水作用力稳定结合于HSA的疏水空腔内。光谱法实验结果表明,PCB-20通过与HSA形成HSA-PCB20复合物从而对HSA具有荧光猝灭作用,猝灭原因是静态猝灭和非辐射能量转移,热力学参数也表明两者结合的主要驱动力为疏水作用力,计算模拟与实验结果吻合度较高。分子动力学模拟结果表明,PCB-20能够与HSA稳定结合,且与同步荧光光谱实验共同证明其对HSA的构象变化产生了一定影响。The interaction between 2,3,3′-trichloro biphenyl（PCB-20） and human serum albumin （HSA） was investigated by molecular docking,molecular dynamics （MD） simulation,fluorescence spectroscopy,ultraviolet spectrum and synchronous fluorescence.The intrinsic fluorescence quenching of HSA by PCB-20 was a result of the formation of PCB20-HSA complex,and the quenching reasons were both static quenching and non-radiation energy transfer,which was consistent with the molecular docking.Molecular docking studies and thermodynamic analysis revealed that the binding behavior was mainly governed by hydrophobic force.MD and synchronous fluorescence revealed that HSA does have a slight conformational change when it binds with PCB-20.MD simulation also provided a support that the stability of HSA-PCB20 complex are better than that of free protein with PCB-20.Excellent agreement was found between the experimental and theoretical results.

关 键 词：2 3 3'-三氯联苯(PCB-20) HSA 分子对接 分子动力学模拟 光谱法 

分 类 号：O657.3[理学—分析化学] O625.13[理学—化学]