Probing Orientations and Conformations of Peptides and Proteins at Buried Interfaces

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.

Automated summary

SFG vibrational spectroscopy is a powerful technique for elucidating molecular structures of peptides/proteins at interfaces, and has been successfully applied in various studies. Combined with other analytical techniques and computational simulations, it provides a more comprehensive understanding of the structure-function relationships of interfacial peptides/proteins.