异烟肼与牛血清白蛋白相互作用的光谱和电化学研究

Studies on the Interaction of Isoniazid and Bovine Serum Albumin by Spectroscopic and Electrochemical Methods

本文用自制L-天冬氨酸修饰电极(PLA/GCE),采用循环伏安法研究了牛血清白蛋白(BSA)与异烟肼(INH)的相互作用,并与荧光光谱法、紫外-可见光谱法进行了比较。使用循环伏安法和荧光光谱法,测得异烟肼与牛血清白蛋白的结合常数K分别为1.544×10~4、1.479×10~4 L/mol,结合位点数均接近1.1。实验测得异烟肼对牛血清白蛋白是静态猝灭。异烟肼的浓度与牛血清白蛋白的荧光强度的降低在2.5×10^(-7)~4.5×10^(-4) mol/L范围内呈线性关系,检出限为1.0×10^(-7) mol/L。BSA的浓度与异烟肼的氧化峰电流的下降在1.0×10^(-9)~5.0×10^(-5) mol/L范围内呈线性关系,检出限为5.0×10^(-10) mol/L。该方法可用于样品中异烟肼和牛血清白蛋白的测定。

The interaction between isoniazid（INH）and bovine serum albumin（BSA）was investigated using the self-made modified electrode by cyclic voltammetry and fluorescence.The binding constants of 1.479×104 L/mol and 1.544×104 L/mol were calculated from the data obtained from fluorescence quenching experiments and cyclic voltammetry,respectively.And the number of binding sites was 1.1.The interaction of bovine serum albumin with INH was a single static quenching procedure.The fluorescence intensity change of BSA was linear to the concentration of INH in the range of 2.5×10-7-4.5×10-4 mol/L,and the detection limit was 1.0×10-7 mol/L.The redox peak current of INH was proportional to the concentration of BSA,and the linear range was 1.0×10-9-5.0×10-5 mol/L with a detection limit of 5.0×10-10 mol/L.The method was applied to the determination of BSA and INH in samples with satisfactory results.