人血清白蛋白与氯氰菊酯相互作用的分子模拟研究

Molecular modeling studies of interactions between human serum albumin and cypermethrin

运用分子对接、分子动力学、结合自由能计算和丙氨酸扫描等分子模拟方法,研究了人血清白蛋白（human serum albumin,HSA）与氯氰菊酯的结合模式。结果表明：氯氰菊酯与HSA结合形成了稳定的复合物,与其氨基酸残基Arg209形成1个氢键,结合自由能为–83.43 kJ/mol,其中范德华力是结合的主要驱动力,极性溶剂化能是主要抑制力。丙氨酸突变扫描结果显示,氨基酸残基Lys199的ΔΔG_（bind）值为16.78 kJ/mol,是HSA和氯氰菊酯结合的关键氨基酸。该研究结果为阐明氯氰菊酯在人体内的代谢机制提供了理论参考。

The binding pattern of human serum albumin（HSA） and cypermethrin was investigated by Auto Dock molecular docking, molecular dynamics, binding free energy calculation and alanine scanning mutagenesis. The results showed that HSA and cypermethrin could lead to stable complex.And one hydrogen bond between cypermethrin and amino acid residue Arg209 was formed. The binding free energy was -83.43 kJ/mol. The van der Wals force was the main driving forces and the polar solvation energy was the main resistance force of the binding. ΔΔG_（bind） of Lys199 was 16.78 kJ/mol through alanine scanning mutagenesis calculated, which was the key amino acid in the combination between HSA and cypermethrin. These results could provide theoretical references to illustrate the metabolism mechanism of cypermethrin in human body.