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dc.contributor.authorLi, W.en
dc.contributor.authorO'Brien-Simpson, N.en
dc.contributor.authorTailhades, J.en
dc.contributor.authorPantarat, N.en
dc.contributor.authorDawson, R.en
dc.contributor.authorOtvos, L.en
dc.contributor.authorReynolds, E.en
dc.contributor.authorSeparovic, F.en
dc.contributor.authorHossain, M.en
dc.contributor.authorWade, J.en
dc.identifier.citationChemistry and Biology, 2015; 22(9):1250-1258en
dc.description.abstractA3-APO, a de novo designed branched dimeric proline-rich antimicrobial peptide (PrAMP), is highly effective against a variety of in vivo bacterial infections. We undertook a selective examination of the mechanism for the Gram-negative Escherichia coli bacterial membrane interaction of the monomer (Chex-Arg20), dimer (A3-APO), and tetramer (A3-APO disulfide-linked dimer). All three synthetic peptides were effective at killing E. coli. However, the tetramer was 30-fold more membrane disruptive than the dimer while the monomer showed no membrane activity. Using flow cytometry and high-resolution fluorescent microscopy, it was observed that dimerization and tetramerization of the Chex-Arg20 monomer led to an alteration in the mechanism of action from non-lytic/membrane hyperpolarization to membrane disruption/depolarization. Our findings show that the membrane interaction and permeability of Chex-Arg20 was altered by multimerization.en
dc.description.statementofresponsibilityWenyi Li, Neil M. O'Brien-Simpson, Julien Tailhades, Namfon Pantarat, Raymond M. Dawson, Laszlo Otvos, Eric C. Reynolds, Frances Separovic, Mohammed Akhter Hossain, John D. Wadeen
dc.publisherElsevier (Cell Press)en
dc.rights© 2015 Elsevier Ltd. All rights reserved.en
dc.subjectEscherichia coli; Proline; Peptides; Antimicrobial Cationic Peptides; Membrane Proteins; Microscopy, Fluorescence; Flow Cytometry; Microbial Sensitivity Tests; Structure-Activity Relationship; Dimerization; Proline-Rich Protein Domainsen
dc.titleMultimerization of a proline-rich antimicrobial peptide, Chex-Arg20, alters its mechanism of interaction with the Escherichia coli membraneen
dc.typeJournal articleen
pubs.library.collectionMedicine publicationsen
Appears in Collections:Medicine publications

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