目的研究马钱子碱、士的宁与人血清白蛋白(HSA)间非共价结合特性。方法采用荧光猝灭法计算药物与蛋白间的结合常数与结合位点数;根据不同作用温度时药物-蛋白非共价结合复合物的热力学参数变化, 分析药物与蛋白间的主要作用力类型。结果当作用温度分别为25℃和35℃时, 马钱子碱与HSA的结合常数(K)分别为2.12×10⁴L/mol和1.97×10⁴L/mol, 结合位点数(n)分别为1.07和1.07;士的宁与HSA的K分别为6.34×10³L/mol和3.05×10³L/mol, n分别为1.01、0.97。马钱子碱、士的宁与HSA间的作用力主要为氢键和范德华力。结论马钱子碱、士的宁与HSA能自发形成不发荧光的复合物, 这种药物蛋白结合可能对马钱子碱、士的宁的药动学过程产生一定影响。

Objective To investigate the effects of both brucine and strychnine on human serum albumin(HSA).Methods The binding constant K and the binding sites value(n) between drug and protein were gotten by fluorescence quenching method: and depending on the changes of thermodynamic parameters about the drug-protein complex under different temperatures,the main binding forces could be obtained between these two medicines and HSA.Results When the temperatures were 25 ℃ and 35 ℃,the binding constant K between brucine and HSA were 2.12×104 and 1.97×104 L/mol with the binding sites value(n) of 1.07 and 1.07,respectively.To strychnine and HSA,the binding constant K at different temperatures were 6.34×103 and 3.05×103 L/mol.The n were 1.01 and 0.97.Conclusion Brucine,strychnine and HSA can be combined compound which have no fluorescence,and the drug-protein binding may have some impact on the pharmacokinetics of brucine and strychnine.

国家自然科学基金资助项目(30630075)