物理学进展

物理学进展 ›› 2018, Vol. 38 ›› Issue (3): 132-145.

• • 上一篇    

界面蛋白质分子结构与动力学的和频振动光谱研究

魏锋，谈军军，张佳慧，李传召，汪文婷，罗毅，叶树集   

  • 发布日期:2020-10-12

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

Wei Feng, Tan Jun-Jun, Zhang Jia-Hui, Li Chuan-Zhao, Wang Wen-Ting, Luo Yi, Ye Shu-Ji   

  • Published:2020-10-12

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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。

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

Abstract: 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 interfacial proteins in situ and in real-time is the core of revealing the function of interfacial 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 interfacial protein molecules at the molecular level. In this review, the application of SFG-VS in the structure and dynamic characterization of interfacial 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.

Key words: Interfacial proteins; Sum frequency generation vibrational spectroscopy; Amide bands; Conformations; Structure and dynamics