Mechanism of the interaction between benthiavalicarb-isopropyl and human serum albumin

被引:13
|
作者
Zhang, Jian [1 ]
Wang, Zishi [1 ]
Xing, Yue [1 ]
Hou, Chenxin [1 ]
Zhou, Qin [1 ]
Sun, Yan [1 ]
Sun, Yuan [1 ]
Xu, Hongliang [1 ,2 ]
Gao, Jinsheng [1 ,2 ]
机构
[1] Heilongjiang Univ, Sch Agr Resources & Environm, Harbin 150080, Peoples R China
[2] Heilongjiang Univ, Pesticide Engn Ctr, Harbin, Peoples R China
基金
中国博士后科学基金;
关键词
Benthiavalicarb-isopropyl; mechanism; molecular docking; human serum albumin; spectroscopic studies; MOLECULAR DOCKING; CRYSTAL-STRUCTURE; IN-VITRO; BINDING; SPECTROSCOPY; HSA; HYDROCHLORIDE; COMPLEX; MILK; DRUG;
D O I
10.1080/00387010.2020.1756343
中图分类号
O433 [光谱学];
学科分类号
0703 ; 070302 ;
摘要
The interaction between benthiavalicarb-isopropyl and human serum albumin was studied by ultraviolet-visible absorption, fluorescence, synchronous fluorescence, three-dimensional fluorescence, circular dichroism spectroscopies and molecular docking. The results revealed that the effect of benthiavalicarb-isopropyl on human serum albumin was static quenching. The number of binding sites, binding constants, and binding distance were obtained. The interaction of benthiavalicarb-isopropyl to human serum albumin was mainly through hydrogen bond and van der Waals force. The conformation of human serum albumin changed slightly. The interaction details were studied by molecular docking method. This study elucidated the mechanism of the interaction between benthiavalicarb-isopropyl and human serum albumin.
引用
收藏
页码:360 / 371
页数:12
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