Interaction of two flavonols with fat mass and obesity-associated protein investigated by fluorescence quenching and molecular docking
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 104 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.
Publisher URL: http://www.tandfonline.com/doi/full/10.1080/07391102.2017.1388287
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