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目的:研究(E)-2-[2-(4-甲氧苄基)肼基]-4-苯基噻唑(MHP)与人血清蛋白(HSA)之间的相互作用,为揭示噻唑类衍生物与DNA作用的机制提供实验依据。方法:根据MHP与HSA相互作用的荧光敏化作用,利用Stern-Volmer方程,及非辐射能量转移理论处理实验数据,采用同步荧光光谱探讨了MHP对HSA构象的影响。结果:实验发现MHP可以使HSA的荧光增强,表明两者之间发生了能量转移,能量转移的机理是MHP与HSA结合形成了复合物。荧光增强(敏化)效应主要源于给体-受体间的偶极-偶极作用的能量转移。结论:能量转移的结果为内原发色基团的荧光被猝灭和外源发色基团荧光被敏化,计算得到其敏化常数为-2.620 8×104。同步荧光光谱表明,相互作用引起HSA构象变化,提示结合位点更接近于色氨酸。
OBJECTIVE: To investigate the interaction between (E) -2- [2- (4-methoxybenzyl) hydrazino] -4-phenylthiazole (MHP) and human serum albumin (HSA) The mechanism of interaction between DNA and DNA provides experimental evidence. Methods: According to the sensitization effect of MHP and HSA, the experimental data were processed by Stern-Volmer equation and non-radiative energy transfer theory, and the effect of MHP on the conformation of HSA was investigated by synchronous fluorescence spectroscopy. Results: The results showed that MHP could enhance the fluorescence of HSA, indicating that energy transfer occurred between the two. The mechanism of energy transfer is the combination of MHP and HSA. The fluorescence enhancement (sensitization) effect is mainly due to the energy transfer between the donor-acceptor dipole-dipole interaction. CONCLUSION: The result of energy transfer is that the fluorescence of the endogenous primary chromophore is quenched and the fluorescence of the exogenous chromophore is sensitized, and its sensitization constant is calculated to be -2.620 8 × 104. Synchronous fluorescence spectra showed that the interaction caused a conformational change in HSA, suggesting that the binding site is closer to tryptophan.