文献类型： 外文期刊

作者： Zhang, Mengli ¹ ; Chai, Yiqiu ² ; Han, Baoyu ¹ ;

作者机构： 1.China Jiliang Univ, Hangzhou 310018, Zhejiang, Peoples R China

2.Zhejiang Acad Agr Sci, Inst Subtrop Crops, Wenzhou 325005, Zhejiang, Peoples R China

关键词： Human serum albumin; Myriocin; Interaction; Fluorescence spectroscopy; Molecular docking

期刊名称：JOURNAL OF SOLUTION CHEMISTRY （ 影响因子：1.677； 五年影响因子：1.447 ）

ISSN： 0095-9782

年卷期： 2019 年 48 卷 6 期

页码：

收录情况： SCI

摘要： The interactions between myriocin (ISP-1) and human serum albumin (HSA) were studied by fluorescence spectroscopy, synchronous fluorescence spectroscopy, three-dimensional fluorescence spectroscopy and molecular docking approach. The intrinsic fluorescence of HSA was quenched through a combination of static and dynamic quenching. The binding constants and the number of binding sites were evaluated according to the Stern-Volmer equation. ISP-1 could not bind efficiently to HSA at higher temperatures. The electrostatic force, hydrogen bonding and hydrophobic force were dominant for the binding ISP-1 and HSA. The site I was the primary binding site for the binding ISP-1 and HSA. What's more, the conformational and microenvironmental changes of HSA during the binding process were studied by synchronous fluorescence spectroscopy and three-dimensional fluorescence spectroscopy. Lys-195, Arg-218, Arg-222 and Val-293 were the important amino acid residues involved in the binding process.