Interaction of two flavonols with fat mass and obesity-associated protein investigated by fluorescence quenching and molecular docking

被引:21
|
作者
Wang, Zechun [1 ]
Wang, Ning [1 ]
Han, Xinxin [1 ]
Wang, Ruiyong [1 ]
Chang, Junbiao [1 ]
机构
[1] Zhengzhou Univ, Coll Chem & Mol Engn, 100 Sci Ave, Zhengzhou 450001, Henan, Peoples R China
来源
基金
中国国家自然科学基金;
关键词
binding; flavonols; FTO; fluorescence; molecular docking; HUMAN SERUM-ALBUMIN; GEMINI SURFACTANT; FTO PROTEIN; IN-VITRO; BOVINE; BINDING; SPECTROSCOPY; DERIVATIVES; GENE; ANTIBACTERIAL;
D O I
10.1080/07391102.2017.1388287
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The binding of two flavonols with fat mass and obesity-associated protein (FTO) was studied using fluorescence spectroscopy, Stern-Volmer kinetics, UV-Vis absorption, and molecular docking. The quenching of FTO fluorescence was determined to be static with binding constants on the order of 10(4) M-1. The interaction was studied over three temperatures, and the binding was found to be exothermic with a positive change in entropy. Thermodynamic analysis and molecular modeling suggest that hydrophobic interaction and hydrogen bonding interaction are the main binding force in stabilizing the flavonol-FTO complex.
引用
收藏
页码:3388 / 3397
页数:10
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