光谱法结合分子对接研究阿格列汀、利格列汀与乳清蛋白的相互作用
Interaction between alogliptin,linagliptin and lactalbumin by spectroscopy plus molecular docking
李婉璐 1郑红霞 1李静 1邹媛 1张国刚2
作者信息
- 1. 西安交通大学药学院,陕西西安 710061
- 2. 西安交通大学第一附属医院药学部,陕西西安 710061
- 折叠
摘要
目的:在生理条件下使用光谱法和分子对接研究阿格列汀、利格列汀与乳清蛋白的相互作用.方法:实验选取激发波长(λex)280nm,测定不同温度下药物的荧光猝灭光谱;通过相关参数(结合常数、结合位点数等)的计算以及热力学参数判断猝灭机制、药物与乳清蛋白的相互作用特点以及乳清蛋白构象的变化,并通过分子对接方法探究药物与乳清蛋白之间可能存在的作用形式.结果:阿格列汀、利格列汀均可使乳清蛋白发生复合式静态猝灭;以疏水作用力为主要作用力类型;药物与乳清蛋白结合过程中存在非辐射能量转移,促使乳清蛋白的荧光猝灭;药物结合反应对乳清蛋白的构象无明显影响;阿格列汀和利格列汀分别与氨基酸残基形成氢键.结论:阿格列汀、利格列汀与乳清蛋白可自发发生相互作用,建议勿将两种药物用牛奶送服.
Abstract
OBJECTIVE To examine the interaction between alogliptin,linagliptin and lactalbumin through fluorescent spec-troscopy,ultraviolet spectroscopy and molecular docking under physiological conditions.METHODS The excitation wave-length(λex)of 280 nm was selected for measuring the fluorescent quenching spectra at different temperatures.Quenching mecha-nism,interaction characteristics between drugs and lactalbumin and conformation changes of lactalbumin were determined by calcu-lating the related parameters(binding constant & number of binding sites)and thermodynamic parameters.The possible forms of interaction between drugs and lactalbumin were explored by molecular docking.RESULTS Both alogliptin and ligliptin could cause compound static quenching of lactalbumin.Hydrophobic force was a major force.According to ultraviolet absorption spec-trum,synchronous fluorescent spectrum and three-dimensional fluorescent spectrum,drug binding reaction had no obvious effect on the conformation of lactalbumin.Alogliptin and ligliptin formed hydrogen bonds with amino acid residues.CONCLUSION Alogliptin and ligliptin can spontaneously interact with lactalbumin.It is recommended not to take two drugs with milk.
关键词
阿格列汀/利格列汀/乳清蛋白/相互作用/光谱法/分子对接Key words
alogliptin/linagliptin/lactalbumin/interaction/spectrometry/molecular docking引用本文复制引用
基金项目
陕西省重点研发计划(2020ZDLSF05-12)
陕西省重点研发计划(2022ZDLSF05-07)
出版年
2024
NETL
NSTL
万方数据