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    Membrane Core-Specific Antimicrobial Action of Cathelicidin LL-37 Peptide Switches Between Pore and Nanofibre Formation

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    Author
    Shahmiri, M; Enciso, M; Adda, CG; Smith, BJ; Perugini, MA; Mechler, A
    Date
    2016-11-30
    Source Title
    Scientific Reports
    Publisher
    NATURE PUBLISHING GROUP
    University of Melbourne Author/s
    Perugini, Matthew
    Affiliation
    Biochemistry and Molecular Biology
    Metadata
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    Document Type
    Journal Article
    Citations
    Shahmiri, M., Enciso, M., Adda, C. G., Smith, B. J., Perugini, M. A. & Mechler, A. (2016). Membrane Core-Specific Antimicrobial Action of Cathelicidin LL-37 Peptide Switches Between Pore and Nanofibre Formation. SCIENTIFIC REPORTS, 6 (1), https://doi.org/10.1038/srep38184.
    Access Status
    Open Access
    URI
    http://hdl.handle.net/11343/257667
    DOI
    10.1038/srep38184
    Abstract
    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.

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