Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/99148
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dc.contributor.authorSani, M.en
dc.contributor.authorWhitwell, T.en
dc.contributor.authorGehman, J.en
dc.contributor.authorRobins-Browne, R.en
dc.contributor.authorPantarat, N.en
dc.contributor.authorAttard, T.en
dc.contributor.authorReynolds, E.en
dc.contributor.authorO'Brien-Simpson, N.en
dc.contributor.authorSeparovic, F.en
dc.date.issued2013en
dc.identifier.citationAntimicrobial Agents and Chemotherapy, 2013; 57(8):3593-3600en
dc.identifier.issn0066-4804en
dc.identifier.issn1098-6596en
dc.identifier.urihttp://hdl.handle.net/2440/99148-
dc.description.abstractMaculatin 1.1 (Mac1) showed potent activity against Staphylococcus aureus with an MIC of 7 μM. The mode of action of Mac1 was investigated by combining assays with S. aureus cells and lipid vesicles mimicking their membrane composition. A change in Mac1 conformation was monitored by circular dichroism from random coil to ca. 70% α-helix structure in contact with vesicles. Electron micrographs of S. aureus incubated with Mac1 showed rough and rippled cell surfaces. An uptake of 65% of small (FD, 4 kDa [FD-4]) and 35% of large (RD, 40 kDa [RD-40]) fluorescent dextrans by S. aureus was observed by flow cytometry and indicate that Mac1 formed a pore of finite size. In model membranes with both dyes encapsulated together, the full release of FD-4 occurred, but only 40% of RD-40 was reached, supporting the flow cytometry results, and indicating a pore size between 1.4 and 4.5 nm. Finally, solid-state nuclear magnetic resonance showed formation of an isotropic phase signifying highly mobile lipids such as encountered in a toroidal pore structure. Overall, Mac1 is a promising antimicrobial peptide with the potent capacity to form pores in S. aureus membranes.en
dc.description.statementofresponsibilityM.-A. Sani, T. C. Whitwell, J. D. Gehman, R. M. Robins-Browne, N. Pantarat, T. J. Attard, E. C. Reynolds, N. M. O'Brien-Simpson and F. Separovicen
dc.language.isoenen
dc.publisherAmerican Society for Microbiologyen
dc.rights© 2013, American Society for Microbiology. All Rights Reserved.en
dc.subjectCell Membrane; Staphylococcus aureus; Dextrans; Lipid Bilayers; Antimicrobial Cationic Peptides; Amphibian Proteins; Anti-Bacterial Agents; Microscopy, Electron, Scanning; Circular Dichroism; Drug Evaluation, Preclinical; Cell Membrane Permeability; Protein Structure, Secondary; Molecular Weight; Fluorescence; Porosityen
dc.titleMaculatin 1.1 disrupts staphylococcus aureus lipid membranes via a pore mechanismen
dc.typeJournal articleen
dc.identifier.rmid0030048059en
dc.identifier.doi10.1128/AAC.00195-13en
dc.relation.granthttp://purl.org/au-research/grants/arc/DP110101866en
dc.relation.granthttp://purl.org/au-research/grants/nhmrc/1008106en
dc.identifier.pubid248154-
pubs.library.collectionMedicine publicationsen
pubs.library.teamDS08en
pubs.verification-statusVerifieden
pubs.publication-statusPublisheden
Appears in Collections:Medicine publications

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