The membrane activity of the antimicrobial peptide caerin 1.1 is pH dependent

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dc.contributor.authorSani, MAen_AU
dc.contributor.authorLe Brun, APen_AU
dc.contributor.authorRajput, Sen_AU
dc.contributor.authorAttard, Ten_AU
dc.contributor.authorSeparovic, Fen_AU
dc.date.accessioned2023-03-26T21:05:03Zen_AU
dc.date.available2023-03-26T21:05:03Zen_AU
dc.date.issued2023-03-21en_AU
dc.date.statistics2023-03-24en_AU
dc.description.abstractAntimicrobial peptides are an important class of membrane-active peptides that can provide alternatives or complements to classic antibiotics. Among the many classes of AMPs, the histidine-rich family is of particular interest since they may induce pH-sensitive interactions with cell membranes. The AMP caerin 1.1 (Cae-1), from Australian tree frogs, has three histidine residues, and thus we studied the pH dependence of its interactions with model cell membranes. Using NMR spectroscopy and molecular dynamics simulations, we showed that Cae-1 induced greater perturbation of the lipid dynamics and water penetrations within the membrane interior in an acidic environment compared with physiological conditions. Using 31P solid-state NMR, the packing, chemical environment, and dynamics of the lipid headgroup were monitored. 2H solid-state NMR showed that Cae-1 ordered the acyl chains of the hydrophobic core of the bilayer. These results supported the molecular dynamics data, which showed that Cae-1 was mainly inserted within the lipid bilayer for both neutral and negatively charged membranes, with the charged residues pulling the water and phosphate groups inward. This could be an early step in the mechanism of membrane disruption by histidine-rich antimicrobial peptides and indicated that Cae-1 acts via a transmembrane mechanism in bilayers of neutral and anionic phospholipid membranes, especially in acidic conditions. © 2023 Elsevier B.V.en_AU
dc.description.sponsorshipThis research was funded by the Australian Research Council (ARC) Discovery Project grants DP190101506 to F.S. and DP210101792 to M.-A.S. and LIEF grant LE160100120 to F.S. and M.-A.S. NMR experiments were performed at the Bio21 Institute NMR facility and the peptide synthesis at the Bio21 Institute Melbourne Protein Characterization facility.en_AU
dc.identifier.citationSani, M.-A., Le Brun, A. P., Rajput, S., Attard, T., & Separovic, F. (2023). The membrane activity of the antimicrobial peptide caerin 1.1 is pH dependent. Biophysical Journal, 122(6), 1058-1067. doi:10.1016/j.bpj.2023.01.021en_AU
dc.identifier.issn0006-3495en_AU
dc.identifier.issue6en_AU
dc.identifier.journaltitleBiophysical Journalen_AU
dc.identifier.pagination1058-1067en_AU
dc.identifier.urihttps://www.sciencedirect.com/science/article/pii/S0006349523000371en_AU
dc.identifier.urihttps://apo.ansto.gov.au/dspace/handle/10238/14730en_AU
dc.identifier.volume122en_AU
dc.language.isoenen_AU
dc.publisherScience Directen_AU
dc.subjectCell membranesen_AU
dc.subjectWateren_AU
dc.subjectEnvironmenten_AU
dc.subjectSpectroscopyen_AU
dc.subjectAntibioticsen_AU
dc.subjectPeptidesen_AU
dc.titleThe membrane activity of the antimicrobial peptide caerin 1.1 is pH dependenten_AU
dc.typeJournal Articleen_AU
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