呋喃类违禁兽药与人血清白蛋白作用机制的分子模拟

Molecular Simulation of Interaction between Nitrofurans and Human Serum Albumin

硝基呋喃是目前国际上最受关注的残留兽药之一,采用分子模拟方法研究了3种硝基呋喃药物小分子呋喃唑酮、呋喃它酮、呋喃妥因与人血清白蛋白(HSA)的作用机制。结果表明:呋喃唑酮、呋喃它酮、呋喃妥因都与HSA有很强的相互作用,它们之间通过氢键作用、静电作用结合,与HSA的相互作用能分别为-2005.00、-2120.20、-1949.35kJ/mol;其中,HSA中的氨基酸LYS199、SER202、PHE211、TRP214、ALA215和ARG218与呋喃唑酮、呋喃它酮、呋喃妥因都存在着很强的氢键和静电力作用,是相互作用的关键氨基酸残基。

Nitrofurans have drawn much research attention due to their intensive toxicity and carcinogenic effect. The interaction between nitrofurans and human serum albumin was investigated using molecular mechanics simulations. The results showed that the binding energy between human serum albumin and furazolidone, furaltadone or nitrofurantoin was -2005.00, -2120.20 kJ/mol and -1949.35 kJ/mol, respectively. Strong hydrogen bond force and electrostatic force were formed between nitrofurans and the amino acid residues LYS199, SER202, PHE211, TRP214, ALA215 and ARG218 in the active site. The interaction mechanisms between nitrofunans and human serum albumin were studied at molecular level including binding sites and key groups. Our results will hopefully provide a theoretical basis for further studying in vivo transportation, distribution, toxicity and molecular design of nutrofunans.