分子对接法研究1-甲基芘及其含氧代谢物与BSA的相互作用
首发时间:2018-01-12
摘要:应用分子对接法研究了1-甲基芘(1-MPyr)及其含氧代谢物1-羟甲基芘(1-OHMP)和1-芘甲酸(1-PCA)与牛血清白蛋白(BSA)的相互作用。结果表明,三种小分子与BSA的亲和能力的强弱顺序为1-OHMP<1-MPyr<1-PCA;1-MPyr结合在BSA的IIA域和IIIA域之间,而1-OHMP和1-PCA均结合在BSA的IB域;结合位点周围与1-MPyr, 1-OHMP和1-PCA距离在0.4 nm之内的氨基酸残基数分别为13, 9和10;1-MPyr和1-OHMP与BSA无氢键形成,而1-PCA则与Pro113, Lys114,和Arg144残基分别形成了键长为3.3, 2.1和2.6 nm的氢键。本研究从分子层面预测了1-甲基芘及其含氧代谢物与BSA的作用强弱,并初步阐释了影响其结合作用的重要因素,为探究1-甲基芘在生物体内的代谢毒性提供了一定的理论支持。
关键词: 环境科学 分子对接法 1-甲基芘 牛血清白蛋白 相互作用。
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Molecular Docking Studies on the Interactions of 1-Methylpyrene and its oxygenated metabolites with BSA
Abstract:The interactions of 1-Methylpyrene (1-MPyr), its oxygenated metabolites 1-hydroxymethylpyrene (1-OHMP) and 1-pyrenecarboxylic acid (1-PCA) with bovine serum albumin (BSA) were investigated using molecular docking methods. The results showed that the binding ability of the three small molecules with BSA was in the order of 1-OHMP<1-MPyr<1-PCA. 1-MPyr was located between the subdomain IIA and IIIA of BSA, while both 1-OHMP and 1-PCA were located in the subdomain IB. The numbers of amino acid residues surrounding (within 0.4 nm) the biding site of 1-MPyr, 1-OHMP and 1-PCA were 13, 9 and 10, respectively. No hydrogen bonds were formed between 1-MPyr/1-OHMP and BSA, while three hydrogen bonds were formed between 1-PCA and Pro113/Lys114/Arg144 residues, with the bond lengths of 3.3, 2.1 and 2.6 nm, respectively. This work predicted the affinity of 1-MPyr and its oxygenated metabolites to BSA at the molecular level, and preliminarily explained the important factor affecting their binding, which provided some theoretical data for understanding the metabolic toxicity of 1-MPyr in organism.
Keywords: Environmental Science Molecular Docking 1-Methylpyrene Bovine Serum Albumin (BSA) Interactions
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