Physiologically-relevant modes of membrane interactions by the human antimicrobial peptide, LL-37, revealed by SFG experiments

Ding, Bei, Soblosky, Lauren, Nguyen, Kho, Geng, Junqing, Yu, Xinglong, Ramamoorthy, Ayyalusamy and Chen, Zhan (2013) Physiologically-relevant modes of membrane interactions by the human antimicrobial peptide, LL-37, revealed by SFG experiments. Scientific Reports, 3 1854.1-1854.8. doi:10.1038/srep01854


Author Ding, Bei
Soblosky, Lauren
Nguyen, Kho
Geng, Junqing
Yu, Xinglong
Ramamoorthy, Ayyalusamy
Chen, Zhan
Title Physiologically-relevant modes of membrane interactions by the human antimicrobial peptide, LL-37, revealed by SFG experiments
Journal name Scientific Reports   Check publisher's open access policy
ISSN 2045-2322
Publication date 2013
Sub-type Article (original research)
DOI 10.1038/srep01854
Open Access Status DOI
Volume 3
Start page 1854.1
End page 1854.8
Total pages 8
Place of publication London, United Kingdom
Publisher Nature Publishing
Language eng
Abstract Antimicrobial peptides (AMPs) could become the next generation antibiotic compounds which can overcome bacterial resistance by disrupting cell membranes and it is essential to determine the factors underlying its mechanism of action. Although high-resolution NMR and other biological studies have provided valuable insights, it has been a major challenge to follow the AMP-membrane interactions at physiologically-relevant low peptide concentrations. In this study, we demonstrate a novel approach to overcome this major limitation by performing Sum Frequency Generation (SFG) vibrational spectroscopic experiments on lipid bilayers containing an AMP, LL-37. Our results demonstrate the power of SFG to study non-linear helical peptides and also infer that lipid-peptide interaction and the peptide orientation depend on the lipid membrane composition. The observed SFG signal changes capture the aggregating process of LL-37 on membrane. In addition, our SFG results on cholesterol-containing lipid bilayers indicate the inhibition effect of cholesterol on peptide-induced membrane permeation process.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Chemical Engineering Publications
 
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