Influence of the Ring Size on the Binding Ability of FTO Investigated by Fluorescence Spectroscopy.

Abstract

The fat mass and obesity associated protein (FTO) is a potential target for anti-obesity medicines. In this paper, we have synthesized two potential inhibitors for FTO, three-member-ring compound (W 3 ) and four-member-ring compound (W 4 ). The interactions of fat mass and obesity-associated (FTO) protein with W 3 (or W 4 ) have been studied by spectral method. Results show the intrinsic fluorescence is quenched by the W 3 (or W 4 ). The thermodynamics parameters indicate hydrophobic interaction play a major role in the interactions. The results of synchronous fluorescence spectra demonstrate that the microenvironments of Trp residue of FTO are disturbed by W 3 and W 4 . Results showed that W 3 are stronger quenchers and bind to FTO with the higher affinity than W 4 . The influence of molecular structure on the binding aspects has been investigated.