Abstract
Theaflavin is a kind of multi-pharmacological and health beneficial black tea factor. The aim of this study is to investigate the mechanisms by which theaflavin interacts with glycosylated and non-glycosylated serum albumins and compares their binding properties. Fluorescence and ultraviolet spectra indicated that theaflavin interacted with native and glycated human serum albumin through a static quenching mechanism and had a higher degree of quenching of human serum albumin. The thermodynamic parameters revealed that the combinations of theaflavin with native and glycated human serum albumin were a spontaneous endothermic reaction, and the hydrophobic force was a major driving force in the interaction process. Zeta potential, particle size, synchronous fluorescence, three-dimensional fluorescence spectroscopy and circular dichroism further clarified the effect of theaflavin on the conformation of human serum albumin structure were more pronounced. In addition, site competition experiments and molecular docking technique confirmed that the binding sites of theaflavin on both native and glycated human serum albumin were bound at site II. This study had investigated the effects of glycation on the binding of HSA with polyphenols and the potential nutriology significance of these effects.