氢键
化学
三氯杀螨醇
人血清白蛋白
范德瓦尔斯力
圆二色性
蛋白质二级结构
分子动力学
分子模型
疏水效应
结晶学
荧光
立体化学
计算化学
分子
生物化学
杀螨剂
有机化学
量子力学
物理
作者
Na Li,Xi Yang,Fengping Chen,Guofang Zeng,Like Zhou,Xiaoke Li,Xun Tuo
标识
DOI:10.1016/j.saa.2021.120277
摘要
Dicofol, a broad-spectrum acaricide, has garnered considerable attention because of the potential harm to the environment and various organisms. Herein, this study applied spectroscopic and in silico methods to understand the interaction between human serum albumin (HSA) and dicofol. Fluorescence experiments demonstrated that dicofol formed a stable complex and the binding process occurred in Suldow's site I of HSA. Its binding constant was 2.26 × 105 M-1 at 298 K. Van der Waals forces and hydrogen bond were primarily facilitated the interaction between dicofol and HSA (ΔH < 0, ΔS < 0) according to thermodynamic experiments. Additionally, 3D fluorescence and circular dichroism (CD) spectra revealed a few conformational changes in HSA due to dicofol. Molecular docking analysis indicated that dicofol interacted with Ser192, Gln196, Leu481, Arg218, Leu238, and Phe211 via van der Waals forces and formed a hydrogen bond with His242. Molecular dynamics (MD) simulation showed that Lys195 and Arg218 residues contributed greater energy for forming the HSA-dicofol complex. MD simulation analysis also showed that dicofol can affect the HSA structure with a reduction in α-helix. This research is desired to facilitate a new perspective on the toxicity mechanism of dicofol in the human body.
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