The interaction between stevenleaf and human serum albumin(HSA) in buffer solution(pH=7.40) were studied by fluorescence spectroscopy.It was found that Stevenleaf quenched the fluorescence of HSA via a dynamic quenching process.The binding constant and number of binding sites were found.Values of thermodynamic parameters were calculated.These dates indicated that hydrophobic played a major role in the binding of Stevenleaf and HSA.Synchronous fluorescence spectroscopy was used in the study of the effect of Stevenleaf on the configuration of HSA.