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：

JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS | 2018年 / 36卷 / 13期

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

页码：3388 / 3397

页数：10

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