界面蛋白质分子结构与动力学的和频振动光谱研究  

Molecular Structure and Dynamics of Interfacial Protein Molecules Investigated by Sum Frequency Generation Vibrational Spectroscopy

作　　者：魏锋 谈军军 张佳慧 李传召 汪文婷 罗毅 叶树集 Wei Feng;Tan Jun-Jun;Zhang Jia-Hui;Li Chuan-Zhao;Wang Wen-Ting;Luo Yi;Me Shu-Ji(Hefei National Laboratory for Physical Sciences at the Microscale, University of Science and Technology of China, Hefei,Anhui 230026, China;Institution for Interdisciplinary Research,＆Key Laboratory of Optoelectronic Chemical Materials and Devices of Ministry of Education, Jianghan University, Wuhan, Hubei 430056, China)

机构地区：[1]中国科学技术大学合肥微尺度物质科学国家研究中心,安徽合肥230026 [2]江汉大学交叉学科研究院光电化学材料与器件教育部重点实验室,湖武汉北430056

出　　处：《物理学进展》2018年第3期132-145,共14页Progress In Physics

基　　金：国家自然科学基金(21473177,21633007,21790350);国家重点研发计划(2017YFA0303500,2018YFA0208700);中央高校基本科研业务费专项资金(WK2340000064);中国科学院(2016HSC-IU003);安徽量子信息技术先导项目(AHY090000)

摘　　要：蛋白质与界面相互作用是自然界中一种非常普遍但又十分复杂的现象,其在物理、生物技术、化学工程、药物、环境科学等诸多领域中发挥着极其重要的作用。生物膜界面蛋白质的错误折叠引起的功能障碍与许多疾病的发生和发展直接相关。原位、实时、精确地表征界面蛋白质分子构象变化与动力学行为是揭示界面蛋白质功能的核心,对阐明与蛋白质聚集相关的神经退化型疾病的发生和发展机理非常重要。但目前对其结构与动力学的了解相当匮乏,蛋白质折叠仍是分子生物学中心法则中至今尚未解决的一个重大生物学问题。这主要是因为其表征技术不仅要求具有足够高的结构分辨度和时间分辨度,还需满足时间、空间、活体、非介入性等要求,但同时满足这些要求的技术甚少。而和频振动光谱是一种可以在分子层次上探测界面蛋白质分子结构与动力学的表征方法。本文详细介绍了和频振动光谱技术在界面蛋白质结构与动力学表征方面的应用。通过原位实时探测不同蛋白质骨架振动的酰胺Ⅰ,酰胺Ⅲ与酰胺A谱带,可以实现界面蛋白质分子结构、构象变化与动力学特征的精确测量,进而揭示蛋白质–细胞膜相互作用、蛋白质–蛋白质相互作用、蛋白质聚集的分子机理。本综述将为人们研究复杂界面体系物理与化学问题提供新的思路。The interaction of proteins and the interface is a universal but complex phenomenon in nature, which plays an extremely important role in many fields such as physics, biotechnology, chemical engineering, medicine, and environmental science. For example, the structural mutation and dysfunction caused by the misfolding of proteins at the biointerface are directly related to the occurrence and development of various diseases. Precise characterization of the conformations and dynamics of interracial proteins in situ and in real-time is the core of revealing the function of interracial proteins, which is of great importance to elucidate the mechanism of neurodegenerative diseases associated with protein aggregation. Nevertheless, there is still a lack of knowledge about their structure and dynamics at this moment. Protein folding is also an unresolved problem in molecule biology central rules. It is mainly because its characterization technology has to require enough structural and temporal resolution as well as requests for in situ, in real-time, in vivo, and non-invasive measurement, yet few methods can meet all the requirements. Sum frequency generation vibrational spectroscopy （SFG-VS） is a powerful technique that can probe the structure and dynamics of interracial protein molecules at the molecular level. In this review, the application of SFG-VS in the structure and dynamic characterization of interracial proteins were introduced in details. By probing different protein backbone vibrational bands of amide I, amide III and amide A in situ and in real-time, the precise measurements of the structure, conformation transition and dynamic features of interfacial protein molecules can be achieved, which can further reveal the molecular mechanisms of protein-membrane interaction, protein-protein interaction and protein aggregation. This review will provide a new train of thought for people to study the physical and chemical problems of complex interface systems.

关 键 词：界面蛋白质 和频振动光谱 酰胺谱带 构象 结构与动力学 

分 类 号：O412[理学—理论物理]