应用化学

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花旗松素与牛血清白蛋白相互作用的光谱和电化学

陈彩莲,朱庆仁*,孙登明*   

  1. (淮北师范大学化学与材料科学学院 淮北 235000)
  • 收稿日期:2013-07-09 修回日期:2013-09-22 出版日期:2014-05-10 发布日期:2014-05-10
  • 通讯作者: 朱庆仁,教授; Tel:0561-3803429; E-mail:zhuqingren@ahedu.gov.cn; 研究方向:光学分析
  • 作者简介: 
  • 基金资助:
    安徽省高校省级自然科学基金重点项目(KJ2011A255)

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

CHEN Cailian, ZHU Qingren*, SUN Dengming*   

  1. (School of Chemistry and Materials Science,Huaibei Normal University,Huaibei 235000,China)
  • Received:2013-07-09 Revised:2013-09-22 Published:2014-05-10 Online:2014-05-10
  • Contact:

摘要: 采用紫外光谱法、荧光光谱法和循环伏安法,研究了牛血清白蛋白(BSA)与花旗松素(taxifolin)的相互作用。 用荧光法和循环伏安法测得花旗松素与BSA的结合常数K分别为1.3×106和1.6×106 L/mol,结合位点数均接近1.3。花旗松素对牛血清白蛋白是静态猝灭。BSA荧光强度的降低与花旗松素浓度在一定范围内呈线性关系,其线性范围为6.00×10-7~2.00×10-5 mol/L,检出限为2.00×10-7 mol/L。花旗松素氧化峰电流的下降与BSA浓度在一定范围内呈线性关系,其线性范围为7.00×10-7~1.00×10-4 mol/L,检出限为3.00×10-7 mol/L。用于合成样品中花旗松素和BSA的测定,结果满意。

关键词: 花旗松素, 牛血清白蛋白, 相互作用, 荧光光谱, 电化学

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

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