两种抗血压类药物的合成及其与牛血清白蛋白的相互作用  

Synthesis and Interaction with Bovine Serum Albumin of Two Anti-Blood Pressure Drugs

作　　者：洪利明 刘林海 朱峰 Hong Liming;Liu Linhai;Zhu Feng(College of Chemistry and Environmental Science,Shangrao Normal University,Shangrao Jiangxi 334001,China)

机构地区：[1]上饶师范学院化学与环境科学学院,江西上饶334001

出　　处：《化学世界》2019年第4期199-206,共8页Chemical World

基　　金：江西省自然科学基金(No.20151BAB203046)资助项目

摘　　要：合成了2,6-二甲基-4-苯基-1,4-二氢吡啶-3,5-二甲酸乙酯(药物分子a)和2,6-二甲基-4-甲基苯基-1,4-二氢吡啶-3,5-二甲酸乙酯(药物分子b),并用红外光谱、质谱和核磁共振氢谱表征了利用荧光光谱法研究了该药物分子与牛血清白蛋白(BSA)分子间的相互作用,并计算出不同温度下药物分子与BSA之间相互作用的动态猝灭常数、结合常数、结合位点数及热力学参数。实验结果表明:药物分子可以使牛血清白蛋白(BSA)发生荧光猝灭,其猝灭机理是形成基态复合物的静态猝灭;药物分子a与BSA的作用力主要是疏水力(ΔH>0,ΔS>0);药物分子b与BSA的作用力为氢键和范德华力(ΔH<0,ΔS<0)。Diethyl 2,6-dimethyl-4-phenyl-1,4-dihydropyridine-3,5-dicarboxylate and diethyl 2,6-dimethyl-4-(p-tolyl)-1,4-dihydropyridine-3,5-dicarboxylate were synthesized and characterized by FT IR, MS and ~1H NMR. The interaction of both drug molecules with bovine serum albumin(BSA) was studied by fluorescence. The dynamic quenching constant, binding constant, number of binding sites and thermodynamic parameter between the drug molecule and BSA at different temperatures were calculated. The results showed that both drug molecules could cause fluorescence quenching of BSA, and the quenching mechanism was static quenching;and the corresponding thermodynamic parameters(ΔH>0,ΔS>0) showed that the interaction between the drug a and BSA was mainly hydrophobic interaction;the interaction forces of the drug b and BSA were attributed to hydrogen bond and Van der Waals force(ΔH<0,ΔS<0).

关 键 词：牛血清白蛋白(BSA) 荧光猝灭 2 6-二甲基-4-苯基-1 4-二氢吡啶-3 5-二甲酸乙酯 2 6-二甲基-4-甲基苯基-1 4-二氢吡啶-3 5-二甲酸乙酯 

分 类 号：O626.3[理学—有机化学]