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Structure and Dynamics of Interfacial Peptides and Proteins from Vibrational Sum-Frequency Generation Spectroscopy

机译：振动和频率产生光谱法的界面肽和蛋白质的结构和动力学

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摘要

Proteins at interfaces play important roles in cell biology, immunology, bioengineering, and biomimetic material design. Many biological processes are based on interfacial protein action, ranging from cellular communication to immune responses and the protein-driven mineralization of bone. Despite the importance of interfacial proteins, comparatively little is known about their structure. The standard methods for studying crystalline or solution-phase proteins (X-ray diffraction and NMR spectroscopy) are not well-suited for studying proteins at interfaces, and for these proteins we still lack a corresponding technique that can provide the same level of structural resolution. This is not surprising in view of the challenges involved in probing the structure of proteins within monomolecular films assembled at a very thin interface in situ. Vibrational sum-frequency generation (SFG) spectroscopy has the potential to overcome this challenge and investigate the structure and dynamics of proteins at interfaces at the molecular level with subpicosecond time resolution. While SFG studies were initially limited to simple model peptides, the past decade has seen a dramatic advancement of experimental techniques and data analysis methods that has made it possible to also study interfacial proteins and their folding, binding, orientation, hydration, and dynamics. In this review, we first explain the principles of SFG spectroscopy and the experimental and theoretical methods to measure and analyze protein SFG spectra. Then we give an extensive overview of the interfacial proteins studied to date with SFG. We highlight representative examples to demonstrate recent advances in probing the structure of proteins at the interfaces of liquids, membranes, minerals, and synthetic materials.
机译：界面处的蛋白质在细胞生物学，免疫学，生物工程和仿生材料设计中起重要作用。许多生物学过程基于界面蛋白质作用，从细胞通信与免疫应答和骨骼的蛋白质驱动的矿化。尽管界面蛋白的重要性，但对其结构具有相对较少的。用于研究结晶或溶液相蛋白（X射线衍射和NMR光谱）的标准方法是非常适合于在界面的研究蛋白质，并且对于这些蛋白质，我们仍然缺乏可以提供相同水平的结构分辨率的相应技术。鉴于探讨在原位的非常薄的界面中组装的单色薄膜内蛋白质结构的挑战，这并不令人惊讶。振动和频生成（SFG）光谱有可能克服这一挑战，并研究分子水平的界面处的蛋白质的结构和动力学，具有亚偶像时间分辨率。虽然SFG研究最初仅限于简单的模型肽，但过去十年已经看出了对实验技术和数据分析方法的戏剧性推进，这使得可以研究界面蛋白及其折叠，结合，取向，水合和动力学。在本综述中，我们首先解释了SFG光谱的原理和测量和分析蛋白质SFG光谱的实验和理论方法。然后我们通过SFG进行了迄今为止学习的界面蛋白质的广泛概述。我们强调了代表性的例子，以证明近期探测液体，膜，矿物质和合成材料嵌段结构的蛋白质结构的进展。

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  • 来源
    《Chemical Reviews》 |2020年第7期|共46页
  • 作者

    Hosseinpour Saman; Roeters Steven J.; Bonn Mischa; Peukert Wolfgang; Woutersen Sander; Weidner Tobias;

  • 作者单位

    Friedrich Alexander Univ Erlangen Nurnberg FAU Inst Particle Technol LFG D-91058 Erlangen Germany;

    Aarhus Univ Dept Chem DK-8000 Aarhus C Denmark;

    Max Planck Inst Polymer Res Mol Spect Dept D-55128 Mainz Germany;

    Friedrich Alexander Univ Erlangen Nurnberg FAU Inst Particle Technol LFG D-91058 Erlangen Germany;

    Univ Amsterdam Vant Hoff Inst Mol Sci NL-1098 EP Amsterdam Netherlands;

    Aarhus Univ Dept Chem DK-8000 Aarhus C Denmark;

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