The interaction between resveratrol and human serum albumin (HSA) was studied by using fluorescence quenching spectra,synchronous fluorescence spectra and ultra-violet spectra.The Stern-Volmer curve of the fluorescence quenching of HSA by resveratrol indicated that the quenching mechanism between resveratrol and HSA was mainly static quenching,with nonradiation energy transfer occurring within single molecule.The binding constants (K A) were 2.39×10⁵ (25 ℃),1.25×10⁵ (35 ℃) and 1.10×10⁵ (45 ℃),respectively.According to the Frster theory of nonradiation energy transfer,the binding distances (r) were 3.02 nm (25 ℃),3.46 nm (35 ℃) and 3.79 nm (45 ℃),respectively.The thermodynamic parameters showed that the interaction between resveratrol and HSA was mainly driven by hydrophobic force.Synchronous spectrum was used to investigate the conformational change of HSA.