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.
Keywords: DMSO, dimethyl sulphoxide; FTO; FTO, fat mass and obesity-associated protein; PBS, phosphate buffer saline; binding; flavonols; fluorescence; molecular docking.