大黄酚和牛血清蛋白相互作用的电化学性质研究

在pH 4.0的Britton-Robinson（B-R）缓冲体系中,应用循环伏安法和示差脉冲伏安法对大黄酚与牛血清白蛋白（BSA）相互作用的电化学性质进行研究.结果表明,二者结合生成了一种非电活性的超分子化合物,同时对结合反应的机理进行了探讨.BSA的存在导致大黄酚氧化还原峰电流降低,峰电位基本不变,峰电流的下降值同所加入的BSA浓度在一定范围内呈线性关系.线性范围5.0×10^-6mol/L-1.0×10^-7mol/L,检出限3×10^-7mol/L.

Electrochemical Study of the Interaction between Emodin and BSA

In pH 4.0 Britton- Robinson（B- R）buffer solution, electrochemical of the interaction between emodin and bovine serum albumin （BSA） was studied by using cyclic voltammetry（CV） and differential pulse voltammetry（DPV）. The results showed that emodin and bovine serum protein generated a electrochemical inactive supermolecular compound. At the same time, the combined reaction mechanism was discussed. The redox peak current of emodin decreased and the electric potential changed little as a result of the presence of BSA. The relationship between the peak current decline and the concentration of BSA was linear in the range of 5.0×10^-6mol/L-1.0×10^-7mol/L, and the detection limit was 3×10^-7mol/L.