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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 study the non-covalent binding between strychnine, strychnine and human serum albumin (HSA). Methods Fluorescence quenching method was used to calculate the binding constants and binding sites between drugs and proteins. According to the changes of thermodynamic parameters of drug-protein non-covalent binding complexes at different temperatures, the main types of drugs and proteins were analyzed. Results The binding constants (K) of strychnine to HSA were 2.12 × 104 L / mol and 1.97 × 104 L / mol, respectively, and the number of binding sites (n) was 1.07 and 1.07 at 25 and 35 ℃, respectively ; The K of strychnine and HSA were 6.34 × 103 L / mol and 3.05 × 103 L / mol, respectively, and n were 1.01 and 0.97 respectively. Brucine, strychnine and HSA mainly for the hydrogen bonding and van der Waals forces. Conclusions Strychnine, strychnine and HSA spontaneously form a non-fluorescent complex. The binding of this drug may have an impact on the pharmacokinetics of strychnine and strychnine.