Abstract: The interaction between taxifolin and bovine serum albumin(BSA) was investigated using UV, fluorescence and cyclic voltammetry. The binding constants of 1.3×106 L/mol and 1.6×106 L/mol can be calculated from the data obtained from fluorescence quenching experiments and cyclic voltammetry, respectively. And the number of the binding sites is nearly 1.3. The interaction of bovine serum albumin with taxifolin is a single static quenching procedure. The fluorescence intensity changes of BSA correlate linearly with the concentrations of taxifolin, and the linear range is 6.00×10-7~2.00×10-5 mol/L with a limit of detection at 2.0×10-7 mol/L. The redox peak current of taxifolin is proportional to the concentration of BSA. The linear range is 7.00×10-7~1.00×10-4 mol/L with a limit of detection at 3.0×10-7 mol/L. This method has been applied to the determination of BSA and taxifolin with satisfactory results.

Key words: taxifolin, bovine serum albumin, interaction, fluorescence spectroscopy, electrochemistry