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Membrane Core-Specific Antimicrobial Action of Cathelicidin LL-37 Peptide Switches Between Pore and Nanofibre Formation
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Membrane Core-Specific Antimicrobial Action of Cathelicidin LL-37 Peptide Switches Between Pore and Nanofibre Formation
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Journal Article
Membrane Core-Specific Antimicrobial Action of Cathelicidin LL-37 Peptide Switches Between Pore and Nanofibre Formation
2016
Overview
Membrane-disrupting antimicrobial peptides provide broad-spectrum defence against localized bacterial invasion in a range of hosts including humans. The most generally held consensus is that targeting to pathogens is based on interactions with the head groups of membrane lipids. Here we show that the action of LL-37, a human antimicrobial peptide switches the mode of action based on the structure of the alkyl chains, and not the head groups of the membrane forming lipids. We demonstrate that LL-37 exhibits two distinct interaction pathways: pore formation in bilayers of unsaturated phospholipids and membrane modulation with saturated phospholipids. Uniquely, the membrane modulation yields helical-rich fibrous peptide-lipid superstructures. Our results point at alternative design strategies for peptide antimicrobials.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ Anti-Infective Agents - chemistry
/ Anti-Infective Agents - pharmacology
/ Antimicrobial Cationic Peptides - chemistry
/ Antimicrobial Cationic Peptides - pharmacology
/ Cell Membrane - drug effects
/ Cell Membrane - ultrastructure
/ Humanities and Social Sciences
/ Humans
/ Lipids
/ Microscopy, Electron, Transmission
/ Peptides
/ Protein Structure, Secondary
/ Science
