In situ molecular level studies on membrane related peptides and proteins in real time using sum frequency generation vibrational spectroscopy

• Published in: Journal of structural biology Vol. 168; no. 1; pp. 61 - 77
• Main Authors: Ye, Shuji, Nguyen, Khoi Tan, Clair, Stéphanie V. Le, Chen, Zhan
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.10.2009
• Subjects: Alamethicin; Animals; Antimicrobial peptide; Cell membrane; G proteins; Humans; Lipid bilayer; Lipid Bilayers - chemistry; Melittin; Membrane protein; Membrane Proteins - chemistry; Peptides - chemistry; Proteins - chemistry; SFG; Spectrum Analysis - methods; Sum frequency generation; Tachyplesin I; Vibration; Membrane protein; Melittin; Cell membrane; SFG; Sum frequency generation; Lipid bilayer; G proteins; Alamethicin; Tachyplesin I; Antimicrobial peptide
• ISSN: 1047-8477; 1095-8657
• DOI: 10.1016/j.jsb.2009.03.006

Sum frequency generation (SFG) vibrational spectroscopy has been demonstrated to be a powerful technique to study the molecular structures of surfaces and interfaces in different chemical environments. This review summarizes recent SFG studies on hybrid bilayer membranes and substrate-supported lipid monolayers and bilayers, the interaction between peptides/proteins and lipid monolayers/bilayers, and bilayer perturbation induced by peptides/proteins. To demonstrate the ability of SFG to determine the orientations of various secondary structures, studies on the interactions between different peptides/proteins (melittin, G proteins, alamethicin, and tachyplesin I) and lipid bilayers are discussed. Molecular level details revealed by SFG in these studies show that SFG can provide a unique understanding on the interactions between a lipid monolayer/bilayer and peptides/proteins in real time, in situ and without any exogenous labeling.