Interaction between riboflavin and BSA studied by fluorescence spectrum

The interaction between riboflavin and bovine serum albumin(BSA) was studied by fluorescence spectrum.The results indicated that the fluorescence of BSA was quenched by riboflavin,and the combination of them was a static quenching process.The quenching data were analyzed based on Stern-Volmer equation,and the quenching constant,binding constant and binding sites were obtained.After analyzing fluorescence quenching data by Stern-Volmer equation and thermodynamic equation,the value of bonding constant KA,thermodynamic parameters(ΔH,ΔG and ΔS) were obtained.The quenching constant,binding constant and binding sites of the interaction between riboflavin and BSA were influenced in the presence of Cu(Ⅱ).