STD和WaterLOGSY探测蛋白质与配体相互作用的研究进展  

Research Progress of STD and WaterLOGSY in Detecting Protein-Ligand Interaction

作　　者：徐亮[1] 鞠婉婷 安会丽 刘妮萍 吴学签 刘玉峰[1] XU Liang;JU Wan-ting;AN Hui-li;LIU Ni-ping;WU Xue-qian;LIU Yu-feng(School of Pharmaceutical Sciences,Liaoning University,Shenyang 110036,China)

机构地区：[1]辽宁大学药学院,辽宁沈阳110036

出　　处：《辽宁大学学报（自然科学版）》2023年第4期366-372,共7页Journal of Liaoning University：Natural Sciences Edition

基　　金：辽宁省教育厅科技人才培育项目(LQN202016);辽宁省高等学校创新人才支持计划(LR201847)。

摘　　要：蛋白质-配体相互作用对于理解关键生物学过程至关重要,目前已采用多种分析方法对其进行研究.其中,核磁共振(Nuclear magnetic resonance, NMR)波谱法是在原子水平上筛选蛋白质配体和表征蛋白质-配体结合的常用方法.本文介绍了两种基于配体的NMR方法——饱和转移差(Saturation transfer differential, STD)和梯度光谱监测水配体(Water ligand observed via gradient spectroscopy, WaterLOGSY),因不受蛋白质构象的影响并且不需要靶标同位素标记,基于配体的NMR在研究蛋白质-配体相互作用领域具有广泛的应用.本文主要综述了它们的原理、在筛选配体和表征相互作用中的应用以及相关局限性.Protein-ligand interactions are crucial for understanding key biological processes,and many analytical methods have been used to study them.Among them,nuclear magnetic resonance(NMR)spectroscopy is a common method for screening protein ligands and characterizing protein-ligand binding at the atomic level.In this paper,two ligand based NMR methods—saturation transfer differential(STD)and water ligand observed via gradient spectroscopy(WaterLOGSY)are introduced.Because they are not affected by protein conformation and do not need target isotope labeling,ligand based NMR has a wide range of applications in the research of protein-ligand interactions.This article mainly reviews their principles,applications in screening ligands and characterizing interactions,and limitations.

关 键 词：核磁共振波谱法 相互作用 综述 配体 

分 类 号：R917[医药卫生—药物分析学]