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

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 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:

• binding
• flavonols
• FTO
• fluorescence
• molecular docking

Abbreviations:

• FTO, fat mass and obesity-associated protein
• DMSO, dimethyl sulphoxide
• PBS, phosphate buffer saline