Progress in measuring biophysical properties of membrane proteins with AFM single-molecule force spectroscopy  

作　　者：Mi Li Lianqing Liu Ning Xi Yuechao Wang 

机构地区：[1]State Key Laboratory of Robotics, Shenyang Institute of Automation, Chinese Academy of Sciences [2]University of Chinese Academy of Sciences [3]Department of Mechanical and Biomedical Engineering,City University of Hong Kong

出　　处：《Chinese Science Bulletin》2014年第22期2717-2725,共9页

基　　金：supported by the National Natural Science Foundation of China (61175103);CAS FEA International Partnership Program for Creative Research Teams

摘　　要：Membrane proteins are crucial in cell physiological activities and are the targets for most drugs.Thus,investigating the behaviors of membrane proteins not only provide deeper insights into cell function,but also help disease treatment and drug development.Atomic force microscopy is a unique tool for investigating the structure of membrane proteins.It can both image the morphology of single native membrane proteins with high resolution and,via single-molecule force spectroscopy(SMFS),directly measure their biophysical properties during molecular physiological activities such as ligand binding and protein unfolding.In the context of molecular biomechanics,SMFS has been successfully used to understand the structure and function of membrane proteins,complementing the static three-dimensional structures of proteins obtained by X-ray crystallography.Here,based on the authors’antigen-antibody binding force measurements in clinical tumor cells,the principle and method of SMFS is discussed,the progress in using SMFS to characterize membrane proteins is summarized,and challenges for SMFS are presented.Membrane proteins are crucial in cell physiological activities and are the targets for most drugs. Thus, investigating the behaviors of membrane proteins not only provide deeper insights into cell function, but also help disease treatment and drug development. Atomic force microscopy is a unique tool for investigating the structure of membrane proteins. It can both image the morphology of single native membrane proteins with high resolution and, via singlemolecule force spectroscopy （SMFS）, directly measure their biophysical properties during molecular physiological activities such as ligand binding and protein unfolding. In the context of molecular biomechanics, SMFS has been successfully used to understand the structure and function of membrane proteins, complementing the static three-dimensional structures of proteins obtained by X-ray crystallography. Here, based on the authors＇ antigenantibody binding force measurements in clinical tumor cells, the principle and method of SMFS is discussed, the progress in using SMFS to characterize membrane proteins is summarized, and challenges for SMFS are presented.

关 键 词：原子力显微镜 生物物理特性 单分子力谱 膜蛋白 测量 三维结构 X射线晶体学 肿瘤细胞 

分 类 号：Q51[生物学—生物化学] TH742[机械工程—光学工程]