纳米金修饰电极对沙丁胺醇与蛋白结合作用的研究

Study on the Binding between Salbutamol and Serum Albumin by Gold Nanoparticles Modified Electrode

利用纳米金修饰碳糊电极研究了沙丁胺醇与牛血清蛋白的结合作用,并对牛血清蛋白进行了定量测定。结果发现,在pH 7. 0 PBS缓冲溶液中,当加入不同浓度牛血清蛋白后,0. 6 V处沙丁胺醇的氧化峰电流降低,牛血清蛋白的线性范围是2. 47×10^(-7)mol/L～2. 00×10^(-5)mol/L,检出限为8. 23×10^(-8)mol/L。沙丁胺醇与牛血清蛋白形成了1:1的结合物,结合常数为2. 84×10~5L/mol。紫外光谱表明沙丁胺醇使牛血清蛋白的紫外吸收峰发生红移且有增色效应。4种常见金属离子Zn^(2+),Mg^(2+),Fe^(3+)和Cu^(2+)对沙丁胺醇与牛血清蛋白的结合起抑制作用。红外光谱表明沙丁胺醇与牛血清蛋白分子中氨基酸残基的硫及氮原子形成键合作用。

The binding between Salbutamol (Sal) and bovine serum albumin (BSA) was investigated using electrochemical and spectroscopic analysis.In pH 7.0 PBS buffer solution,when added of BSA,the oxidation current of Sal at 0.6 V was decreased .The linear range of BSA was 2.47×10^-7 mol/L^2.00×10^-5 mol/L,with a detection limit of 8.23×10^-8 mol/L.The binding constant and binding ratio calculated by electrochemical methods was 2.84×10^5 L/mol and 1:1 respectively.The results of UV absorption spectra showed that the UV absorption peak of BSA could red shift and the maximum absorption value was increased.Four kinds of metal ions inhibited on the binding of Sal and BSA.The results of IR spectroscopy showed that Sal could interact with sulfur-containing and nitrogen-containing groups in BSA molecular.