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https://hdl.handle.net/2440/99150
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dc.contributor.author | Li, W. | - |
dc.contributor.author | O'Brien-Simpson, N. | - |
dc.contributor.author | Tailhades, J. | - |
dc.contributor.author | Pantarat, N. | - |
dc.contributor.author | Dawson, R. | - |
dc.contributor.author | Otvos, L. | - |
dc.contributor.author | Reynolds, E. | - |
dc.contributor.author | Separovic, F. | - |
dc.contributor.author | Hossain, M. | - |
dc.contributor.author | Wade, J. | - |
dc.date.issued | 2015 | - |
dc.identifier.citation | Chemistry and Biology, 2015; 22(9):1250-1258 | - |
dc.identifier.issn | 1074-5521 | - |
dc.identifier.issn | 1879-1301 | - |
dc.identifier.uri | http://hdl.handle.net/2440/99150 | - |
dc.description.abstract | A3-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. | - |
dc.description.statementofresponsibility | Wenyi 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. Wade | - |
dc.language.iso | en | - |
dc.publisher | Elsevier (Cell Press) | - |
dc.rights | © 2015 Elsevier Ltd. All rights reserved. | - |
dc.source.uri | http://dx.doi.org/10.1016/j.chembiol.2015.08.011 | - |
dc.subject | Escherichia coli | - |
dc.subject | Proline | - |
dc.subject | Peptides | - |
dc.subject | Antimicrobial Cationic Peptides | - |
dc.subject | Membrane Proteins | - |
dc.subject | Microscopy, Fluorescence | - |
dc.subject | Flow Cytometry | - |
dc.subject | Microbial Sensitivity Tests | - |
dc.subject | Structure-Activity Relationship | - |
dc.subject | Dimerization | - |
dc.subject | Proline-Rich Protein Domains | - |
dc.title | Multimerization of a proline-rich antimicrobial peptide, Chex-Arg20, alters its mechanism of interaction with the Escherichia coli membrane | - |
dc.type | Journal article | - |
dc.identifier.doi | 10.1016/j.chembiol.2015.08.011 | - |
dc.relation.grant | http://purl.org/au-research/grants/arc/DP150103522 | - |
dc.relation.grant | http://purl.org/au-research/grants/nhmrc/1029878 | - |
dc.relation.grant | http://purl.org/au-research/grants/nhmrc/1008106 | - |
pubs.publication-status | Published | - |
Appears in Collections: | Aurora harvest 3 Medicine publications |
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