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采用荧光光谱研究3-羟基-6-[(4-羧基苯基)偶氮]-苯甲酸(HCPAB)与牛血清蛋白(BSA)的相互作用。通过测定298K和310K下HCPAB与BSA的荧光猝灭光谱,计算得到荧光猝灭常数、反应的结合常数、结合位点数及热力学参数,得出这种荧光猝灭机理符合静态猝灭;由Foerster能量转移机理,计算了当BSA与HCPAB比例为1:1时分子间距离r=3.18nm和能量转移效率E=0.23,并由同步荧光光谱显示HCPAB与BSA的结合位点更接近于色氨酸。
The interaction of 3 - hydroxy - 6 - [(4 - carboxyphenyl) azo] - benzoic acid (HCPAB) with bovine serum albumin (BSA) was studied by fluorescence spectroscopy. By measuring the fluorescence quenching spectra of HCPAB and BSA at 298K and 310K, the fluorescence quenching constants, the binding constants, the number of binding sites and the thermodynamic parameters were calculated, and the fluorescence quenching mechanism was found to be consistent with the static quenching. The Foerster energy Transfer mechanism, the intermolecular distance r = 3.18nm and the energy transfer efficiency E = 0.23 were calculated when the ratio of BSA to HCPAB was 1: 1, and the binding site of HCPAB to BSA was found to be closer to tryptophan by synchronous fluorescence spectroscopy.