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
中科院分区:
文献类型:
--
作者:
Guo, Wen;Lu, Tieyi;Chen, Zhan
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.