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目的研究不同温度下间尼索地平(m-nisoldipine,m-Nis)与人血清白蛋白(human serum albumin,HSA)相互作用。方法采用紫外光谱法和荧光光谱法在模拟人体生理pH=7.4的0.1mol/L磷酸缓冲溶液中研究不同温度下m-Nis与HSA相互作用的光谱行为。结果 m-Nis没有使HSA的构象发生变化。293K、301 K和310K时的猝灭常数为分别为1.03×10~5mol/L,1.25×10~5mol/L和1.31×10~5mol/L;结合点数n近似为1,反应的焓变值为3.695kJ/mol,且ΔG<0,ΔS>0;m-Nis在HSA上的结合位置距色氨酸残基的距离(r)=2.96nm。结论 m-Nis对HSA的荧光猝灭作用不是简单的动态猝灭或静态猝灭,而是形成了1:1的复合物,造成荧光猝灭;m-Nis与HSA之间发生的是非辐射能量转移过程,二者之间的主要作用力是疏水力。
Objective To study the interaction between m-nisoldipine (m-Nis) and human serum albumin (HSA) at different temperatures. Methods The spectral behaviors of m-Nis and HSA at different temperatures were studied by UV spectroscopy and fluorescence spectroscopy in a 0.1 mol / L phosphate buffer solution simulating human physiological pH = 7.4. Results m-Nis did not change the conformation of HSA. The quenching constants were 1.03 × 10 ~ 5mol / L, 1.25 × 10 ~ 5mol / L and 1.31 × 10 ~ 5mol / L for 293K, 301 K and 310K, respectively. Is 3.695 kJ / mol and ΔG <0, ΔS> 0; the distance (r) from the tryptophan residue of the m-Nis binding site on HSA = 2.96 nm. Conclusion The fluorescence quenching of HSA by m-Nis is not a simple quenching or static quenching. Instead, it forms a 1: 1 complex and causes fluorescence quenching. Non-radiative energy occurs between m-Nis and HSA Transfer process, the main force between the two is hydrophobic.