Position: Home > Articles > Binding Mechanism and Molecular Docking between Aflatoxin G_1 and Human Serum Albumin
FOOD SCIENCE
2017,38
(5)
86-91
黄曲霉毒素G_1与人血清白蛋白的结合机理及分子对接
作 者：
钟红;王佳曼;马良;江涛
单 位：
西南大学食品科学学院
关键词：
黄曲霉毒素G_1;人血清白蛋白;光谱;分子对接;结合反应
摘 要：
在模拟人体血液p H 7.4的条件下,用分子对接及其荧光光谱、3D荧光、圆二色谱等方法研究黄曲霉毒素G1(aflatoxin G_1,AFG_1)与人血清白蛋白(human serum albumin,HSA)的相互作用。结果发现,根据双对数方程得出AFG1与HSA结合反应猝灭机制为静态猝灭,4个温度条件下结合常数数量级均为104,结合位点数近似为1。通过分子对接和热力学参数计算,AFG1结合在HSA的ⅠB疏水腔中,二者结合力主要为疏水作用和氢键。通过研究体内金属离子对AFG1-HSA反应的影响,Fe~(3+)、Mg~(~(2+))能增大AFG1对HSA的亲和力,而Zn~(2+)、Cu~(2+)、Mn~(2+)离子则能大大降低AFG1与HSA的亲和力。基于F?rster’s能量转移,二者反应距离为3.26 nm。3D荧光结果显示,二者的结合反应使HSA生色团氨基酸残基疏水性增加,二级结构发生改变;圆二色谱结果表明,加入AFG1使得HSA的α-螺旋含量增加。
译 名：
Binding Mechanism and Molecular Docking between Aflatoxin G_1 and Human Serum Albumin
作 者：
ZHONG Hong;WANG Jiaman;MA Liang;JIANG Tao;College of Food Science, Southwest University;
关键词：
aflatoxin G_1(AFG_1);;human serum albumin(HSA);;spectrum;;molecular docking;;binding interaction
摘 要：
The interaction between the mycotoxin aflatoxin G_1(AFG_1) and human serum albumin(HSA) was investigated by molecular docking, fluorescence spectroscopy, 3D fluorescence spectrum, and circular dichroism(CD) under simulated physiological conditions(p H 7.4). According to the double logarithmic equation, the major binding mechanism between AFG_1 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 AFG_1 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 AFG_1-HSA reaction, the affinity of AFG_1 to HSA could be increased by Mg~(2+) and Fe~(3+ )but greatly reduced by Zn~(2+), Mn~(2+) and Cu~(2+). The binding distance between AFG_1 and HSA was calculated to be 3.26 nm based on F?rster's non-radiation energy transfer theory. The 3D florescence spectra revealed that the microenvironment 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.
导出引用
计量
文章访问数: 17
HTML全文浏览量: 0
PDF下载量: 0
所属期刊
