ABSTRACT
Objective: To study the interaction of quercitrin with human serum albumin (HSA) and the influence of glucose. Methods: To investigate the interaction mechanism between quercitrin and HSA by spectroscopic method; to calculate the binding constants, binding sites, and binding distance according to double logarithmic plot and Föster's energy transfer theory, respectively; to explain the type of interaction force between quercitrin with HSA by thermodynamic parameters; to discuss the conformation change of HSA via synchronous fluorescence spectra. Results: The fluorescence quenching mechanism of quercitrin to HSA was static quenching; The binding constants and the number of binding sites decreased with the increasing of temperature and glucose; The distance between the donor and acceptor was less than 7 nm; The hydrophobic forces played a major role in stabilizing quercetrin and HSA complex; The binding reaction had changed the micro-environmention of tryptophan residues. Conclusion: Quercetrin could bind with HSA and change the conformation of HSA; The physiological concentration of glucose increases the binding constants and the number of binding sites of quercetrin with HSA.