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dc.contributor.authorShahmiri, M
dc.contributor.authorEnciso, M
dc.contributor.authorAdda, CG
dc.contributor.authorSmith, BJ
dc.contributor.authorPerugini, MA
dc.contributor.authorMechler, A
dc.date.accessioned2020-12-22T02:35:12Z
dc.date.available2020-12-22T02:35:12Z
dc.date.issued2016-11-30
dc.identifierpii: srep38184
dc.identifier.citationShahmiri, 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.
dc.identifier.issn2045-2322
dc.identifier.urihttp://hdl.handle.net/11343/257667
dc.description.abstractMembrane-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.
dc.languageEnglish
dc.publisherNATURE PUBLISHING GROUP
dc.titleMembrane Core-Specific Antimicrobial Action of Cathelicidin LL-37 Peptide Switches Between Pore and Nanofibre Formation
dc.typeJournal Article
dc.identifier.doi10.1038/srep38184
melbourne.affiliation.departmentBiochemistry and Molecular Biology
melbourne.source.titleScientific Reports
melbourne.source.volume6
melbourne.source.issue1
dc.rights.licenseCC BY
melbourne.elementsid1121584
melbourne.contributor.authorPerugini, Matthew
dc.identifier.eissn2045-2322
melbourne.accessrightsOpen Access


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