Interaction of two flavonols with fat mass and obesity-associated protein investigated by fluorescence quenching and molecular docking. Issue 13 (3rd October 2018)

• Record Type: Journal Article
• Authors: Wang, Zechun; Wang, Ning; Han, Xinxin; Wang, Ruiyong; Chang, Junbiao
• Is Part Of: Journal of biomolecular structure & dynamics. Volume 36:Issue 13(2018)
• Page Start: 3388
• Page End: 3397
• Publication Date: 2018-10-03
• Subjects: binding -- flavonols -- FTO -- fluorescence -- molecular docking; FTO, fat mass and obesity-associated protein -- DMSO, dimethyl sulphoxide -- PBS, phosphate buffer saline; Biomolecules -- Periodicals; Molecular structure -- Periodicals; Molecular Biology -- Periodicals; Biomechanics -- Periodicals; 572
• DOI: 10.1080/07391102.2017.1388287
• Languages: English
• ISSNs: 0739-1102

Abstract

Abstract : 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.