食品科学2017，Vol.38Issue(5)：86-91,6.DOI:10.7506/spkx1002-6630-201705014
黄曲霉毒素G1与人血清白蛋白的结合机理及分子对接
Binding Mechanism and Molecular Docking between Aflatoxin G1 and Human Serum Albumin
摘要
Abstract
The interaction between the mycotoxin aflatoxin G1 (AFG1) and human serum albumin (HSA) was investigated by molecular docking,fluorescence spectroscopy,3D fluorescence spectrum,and circular dichroism (CD) under simulated physiological conditions (pH 7.4).According to the double logarithmic equation,the major binding mechanism between AFG1 and HSA was a static quenching process.At four different temperatures,the magnitude of binding constants was 104 and the number of binding sites was approximate to 1.Through the molecular docking and the calculation of thermodynamic parameters,the binding site of AFG1 was in the ⅠB hydrophobic cavity,and hydrophobic interaction and hydrogen bonding were the major forces in the binding process.By studying the effect of metal ions on AFG1-HSA reaction,the affinity of AFG1 to HSA could be increased by Mg2+ and Fe3+ but greatly reduced by Zn2+,Mn2+ and Cu2+.The binding distance between AFG1 and HSA was calculated to be 3.26 nm based on F(o)rster's non-radiation energy transfer theory.The 3D florescence spectra revealed that the microenviroument of amino acid residues became more hydrophobic after the binding reaction.CD spectra revealed that the conformation of HSA was changed during the binding reaction as shown by an increase in α-helix.关键词
黄曲霉毒素G1/人血清白蛋白/光谱/分子对接/结合反应Key words
aflatoxin G1 (AFG1)/human serum albumin (HSA)/spectrum/molecular docking/binding interaction分类
医药卫生引用本文复制引用
钟红,王佳曼,马良,江涛..黄曲霉毒素G1与人血清白蛋白的结合机理及分子对接[J].食品科学,2017,38(5):86-91,6.基金项目
国家重点基础研究发展计划(973计划)项目(2013CB127803) （973计划）
国家自然科学基金青年科学基金项目(31301476) （31301476）
