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目的:研究中药活性小分子芍药苷、马钱苷与牛血清白蛋白(BSA)之间的相互作用机制。方法:采用荧光光谱法、同步荧光光谱法和紫外光谱法测定芍药苷和马钱苷与BSA的结合常数与结合位点数,根据热力学方程计算作用力类型。结果:2种苷类化合物与BSA的静态结合常数分别为3.56×104和9.06×104L.mol-1,作用位点数n分别为0.624和0.853,猝灭作用主要属于静态猝灭。热力学参数表明该结合过程是一个熵增的自发过程。结论:芍药苷与马钱苷和BSA的结合作用力均为疏水力,两化合物可以嵌插到BSA疏水腔内,与BSA形成复合物。
OBJECTIVE: To study the mechanism of interaction between small active molecules paeoniflorin, loganin and bovine serum albumin (BSA). Methods: The binding constants and binding sites of paeoniflorin and loganin with BSA were determined by fluorescence spectrometry, synchronous fluorescence spectrometry and UV spectrophotometry. The types of force were calculated according to thermodynamic equations. Results: The static binding constants of two glycosides with BSA were 3.56 × 104 and 9.06 × 104L · mol-1, respectively, and the number of active sites was 0.624 and 0.853, respectively. The quenching effect mainly belonged to static quenching. The thermodynamic parameters show that the binding process is an entropy-increasing spontaneous process. CONCLUSION: Paeoniflorin has a hydrophobic interaction with both loganin and BSA. The two compounds can be inserted into BSA hydrophobic cavity to form a complex with BSA.