Mechanism of interactions between organophosphorus insecticides and human serum albumin: Solid-phase microextraction, thermodynamics and computational approach

文献类型： 外文期刊

第一作者： Zhao, Huiyu

作者： Zhao, Huiyu;Wang, Xinquan;Bojko, Barbara;Liu, Fengmao;Peng, Wei;Pawliszyn, Janusz;Peng, Wei

作者机构：

关键词： Interaction mechanism; Solid-phase microextraction; Organophosphorus insecticides; Human serum albumin

期刊名称：CHEMOSPHERE （ 影响因子：7.086； 五年影响因子：6.956 ）

ISSN： 0045-6535

年卷期： 2020 年 253 卷

页码：

收录情况： SCI

摘要： Organophosphates insecticides (OPs) are one of the major environmental pollutants and their interaction with human serum albumin (HSA) has been shown to have significant effects on their bioavailability which is related to toxicokinetics and toxicodynamics in human body. In this research, solid-phase microextraction methods were developed to analyse the free concentrations of three OPs (chlorpyrifos, parathion-methyl and malathion) in buffered HSA solution and that provide a useful method for the determination of binding affinity constants (K-a), binding forces and binding location. Polydimethylsiloxane fibers were selected for analysing the free concentrations of OPs, with an external calibration approach. Good linearities conducted in PBS solution were observed in the range of 0.0025-1.7 mu mol L-1 (R-2 = 0.9975) for chlorpyrifos, 1.0-27 mu mol L-1 (R-2 = 0.9974) for parathion-methyl, and 0.5-70 mu mol L-1 (R-2 = 0.9973)for malathion, respectively. The LODs for instrument response were 1 ng, 5 ng and 10 ng for chlorpyrifos, parathion-methyl and malathion, respectively. The K-a values for chlorpyrifos, parathion-methyl and malathion showed that they were positively correlated with hydrophobicity and negatively correlated with temperature. The OP binding sites on HSA were confirmed by site marker competition test and further proven by computational approaches. The recognition region of parathion-methyl was situated within residues 199-292 in subdomain IIA. Malathion bonded to residues 404-558 in subdomain IIIA. The mode of action between HSA-parathion-methyl and HSA-malathion is found to involve mainly by H-bonds, pi-pi stacking and hydrophobic effects. These results clearly demonstrate the noncovalent binding of OPs with HSA and provide new insight into solid-phase microextraction, thermodynamics and computational approaches. (C) 2020 Elsevier Ltd. All rights reserved.

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