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Mechanism of the interaction between benthiavalicarb-isopropyl and human serum albumin
Spectroscopy Letters ( IF 1.1 ) Pub Date : 2020-04-30 , DOI: 10.1080/00387010.2020.1756343
Jian Zhang 1 , Zishi Wang 1 , Yue Xing 1 , Chenxin Hou 1 , Qin Zhou 1 , Yan Sun 1 , Yuan Sun 1 , Hongliang Xu 1, 2 , Jinsheng Gao 1, 2
Affiliation  

Abstract 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.

中文翻译:

苯噻虫威-异丙基与人血清白蛋白相互作用的机制

摘要 采用紫外-可见吸收、荧光、同步荧光、三维荧光、圆二色光谱和分子对接等方法研究了苯噻菌灵与人血清白蛋白的相互作用。结果表明,苯噻虫威异丙酯对人血清白蛋白的作用是静态猝灭。获得结合位点数、结合常数和结合距离。苯噻虫威-异丙基与人血清白蛋白的相互作用主要是通过氢键和范德华力。人血清白蛋白的构象略有变化。通过分子对接方法研究相互作用的细节。本研究阐明了灭虫威-异丙基与人血清白蛋白相互作用的机制。
更新日期:2020-04-30
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