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

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.