Probing Orientations and Conformations of Peptides and Proteins at Buried Interfaces

Probing Orientations and Conformations of Peptides and Proteins at Buried Interfaces
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DOI:
10.1021/acs.jpclett.1c02956
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发表时间:
2021-10-12
影响因子:
5.7
通讯作者:
Chen, Zhan
Chen, Zhan
中科院分区:
化学2区
文献类型:
--
作者:
Guo, Wen;Lu, Tieyi;Chen, Zhan

文献摘要

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多肽/蛋白质在界面上的分子结构决定了它们的界面性质,在许多应用中起着重要的作用。由于缺乏合适的工具,探测界面多肽/蛋白质结构是困难的。和频产生(SFG)振动光谱技术已经发展成为一种强有力的技术,可以用来解释埋藏在固/液和液/液界面的多肽/蛋白质的分子结构。SFG已成功地用于研究模型细胞膜与抗菌肽/膜蛋白、表面固定化多肽/酶以及物理吸附在聚合物和2D材料上的多肽/蛋白质之间的分子相互作用。各种其他的分析技术和计算模拟为SFG研究提供了支持信息,导致了对界面多肽/蛋白质结构-功能关系的更全面的了解。随着SFG技术和数据分析方法的进步,以及新开发的辅助工具和模拟方法,SFG对界面多肽/蛋白质的研究将进一步影响化学、生物学、生物物理、工程等领域的研究。
Molecular structures of peptides/proteins at interfaces determine their interfacial properties, which play important roles in many applications. It is difficult to probe interfacial peptide/protein structures because of the lack of appropriate tools. Sum frequency generation (SFG) vibrational spectroscopy has been developed into a powerful technique to elucidate molecular structures of peptides/proteins at buried solid/liquid and liquid/liquid interfaces. SFG has been successfully applied to study molecular interactions between model cell membranes and antimicrobial peptides/membrane proteins, surface-immobilized peptides/enzymes, and physically adsorbed peptides/proteins on polymers and 2D materials. A variety of other analytical techniques and computational simulations provide supporting information to SFG studies, leading to more complete understanding of structure-function relationships of interfacial peptides/proteins. With the advance of SFG techniques and data analysis methods, along with newly developed supplemental tools and simulation methodology, SFG research on interfacial peptides/proteins will further impact research in fields like chemistry, biology, biophysics, engineering, and beyond.