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Citation: CHEN Cailian, ZHU Qingren, SUN Dengming. Studies on the Interaction of Taxifolin and Bovine Serum Albumin by Spectroscopic and Voltammetric Methods[J]. Chinese Journal of Applied Chemistry, ;2014, 31(5): 617-623. doi: 10.3724/SP.J.1095.2014.30342 shu

Studies on the Interaction of Taxifolin and Bovine Serum Albumin by Spectroscopic and Voltammetric Methods

1.
School of Chemistry and Materials Science, Huaibei Normal University, Huaibei 235000, China

Corresponding author: ZHU Qingren, SUN Dengming,
Received Date: 9 July 2013
Available Online: 23 September 2013
Fund Project: 安徽省高校省级自然科学基金重点项目(KJ2011A255) (KJ2011A255)

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.
- taxifolin,
- bovine serum albumin,
- interaction,
- fluorescence spectroscopy,
- electrochemistry
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