异烟肼与牛血清蛋白相互作用的光谱研究

用紫外吸收光谱和荧光光谱研究了异烟肼(INH)与牛血清蛋白(BSA)的相互作用.荧光光谱表明,INH对BSA的荧光有较强的猝灭作用.通过结合常数和结合位点数的计算,证明这种荧光猝灭机理符合静态机制,INH和BSA形成了1∶1稳定复合物;考察不同温度和酸度下的猝灭作用,进一步证实其静态猝灭行为和疏水作用机制.紫外吸收光谱和同步荧光光谱表明,INH与BSA的相互作用使蛋白质的分子构象发生变化,而同步荧光光谱显示两者的结合位点更接近于色氨酸.

Spectroscopic studies on the interaction of bovine serum albumin with isoniazid

The interaction of isoniazid with bovine serum albumin(BSA) had been investigated by ultraviolet and fluorescence spectroscopy.Fluorescence spectroscopy showed that BSA fluorescence was quenched regularly with the addition of isoniazid.Isoniazid was capable of binding with BSA to form a 1:1 complex and the quenching mechanism of BSA affected by isoniazid was a static quenching procedure by calculating the binding number and binding constant.The fluorescence quenching mechanisms were also studied at different temperature and under different pH.The results showed that quenching mechanism was a static quenching,and interaction between isoniazid and BSA was driven mainly by hydrophobic force.The intensity of the characteristic absorption peak of BSA decreased gradually with the addition of isoniazid,indicated that the protein conformational changed,resulted from the chemical interaction of isoniazid and BSA.Synchronous fluorescence indicated that the binding sites of isoniazid with BSA was near by tryptophan subunit.