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合成了一种新化合物2-甲基-2,4-二乙氧羰基-6-三氟甲氧基-1,2-二氢喹啉(M DTDQ),采用共振光散射法(RLS)、荧光光谱法、紫外光谱法以及电化学阻抗法(EIS)研究了MDTDQ与人血清白蛋白(HSA)的作用机理。电化学阻抗及共振光散射光谱分析表明HSA与MDTDQ发生结合形成了复合物;MDTDQ对HSA有荧光猝灭作用,由Stern-Volmer方程以及紫外吸收光谱判断其猝灭过程主要为静态猝灭;通过双对数方程计算出298 K,304 K,310 K时两者的结合常数及其相应的结合位点数;根据热力学参数方程计算出△H、△S和△G的值分别为-64.28 k J/mol,-131.70 J·mol-1·K-1,-24.95k J/mol,推断两者之间的作用力类型主要是氢键和范德华力;由Frster非辐射能量转移理论得到MDTDQ与HSA的结合距离为2.85 nm;同步荧光光谱数据表明MDTDQ引起了HSA构象的变化。采用分子模拟对接分析了MDTDQ与HSA的结合,所得结论与实验研究结果一致。
A new compound, 2-methyl-2,4-diethoxycarbonyl-6-trifluoromethoxy-1,2-dihydroquinoline (M DTDQ), was synthesized by resonance light scattering (RLS) Fluorescence spectroscopy, UV spectroscopy and electrochemical impedance spectroscopy (EIS) MDTDQ and human serum albumin (HSA) mechanism of action. Electrochemical impedance spectroscopy (ELC) and resonance light scattering (FTIR) spectroscopy showed that HSA and MDTDQ were combined to form a complex. MDTDQ had a fluorescence quenching effect on HSA. The quenching process was mainly quenched by Stern-Volmer equation and UV absorption spectroscopy. Double logarithmic equation was used to calculate the binding constants and their corresponding binding sites at 298 K, 304 K and 310 K. The values of △ H, △ S and △ G were -64.28 kJ / mol, -131.70 J · mol-1 · K-1, -24.95k J / mol. It is concluded that the type of interaction between the two is mainly hydrogen bond and van der Waals forces; MDTDQ is obtained from the theory of Frster non-radiative energy transfer The binding distance to HSA was 2.85 nm. Synchronous fluorescence spectroscopy data showed that MDTDQ caused the conformational change of HSA. The binding of MDTDQ to HSA was analyzed by molecular simulation docking, and the conclusion was consistent with the experimental results.