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在模拟动物生理条件下利用荧光光谱法从分子水平上研究了4-硝基苯胺同牛血清白蛋白(BSA)的相互作用。4-硝基苯胺对BSA的荧光有较强猝灭作用。用Stern-Volmer方程和双对数方程分别处理实验数据发现BSA与4-硝基苯胺发生反应生成了新的复合物,猝灭机理以静态猝灭为主。根据双对数方程求出了不同温度下反应时复合物的形成常数K(298 K:2.18×104L/mol;310 K:1.95×104L/mol)和结合位点数n(298 K:1.09;310 K:1.12)。根据热力学参数得出4-硝基苯胺与BSA之间的主要作用力为氢键和疏水作用力。同步荧光的结果表明4-硝基苯胺使BSA分子构象发生了改变,其分子内的色氨酸和酪氨酸残基疏水作用增强。
The interaction of 4-nitroaniline with bovine serum albumin (BSA) was studied at the molecular level using fluorescence spectroscopy under simulated animal physiological conditions. 4-nitroaniline has a strong quenching effect on the fluorescence of BSA. Stern-Volmer equation and the logarithmic equation were used to deal with the experimental data respectively. It was found that BSA reacts with 4-nitroaniline to form a new complex, and the quenching mechanism is dominated by static quenching. The formation constants K (298 K: 2.18 × 104 L / mol; 310 K: 1.95 × 104 L / mol) and the number of binding sites n (298 K: 1.09; 310 K: 1.12). According to the thermodynamic parameters, the main interaction between 4-nitroaniline and BSA is hydrogen bond and hydrophobic force. The results of synchronous fluorescence show that 4-nitroaniline changes the conformation of BSA molecule, and the intramolecular tryptophan and tyrosine residues enhance the hydrophobic effect.