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https://hdl.handle.net/2440/99150
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Type: | Journal article |
Title: | Multimerization of a proline-rich antimicrobial peptide, Chex-Arg20, alters its mechanism of interaction with the Escherichia coli membrane |
Author: | Li, W. O'Brien-Simpson, N. Tailhades, J. Pantarat, N. Dawson, R. Otvos, L. Reynolds, E. Separovic, F. Hossain, M. Wade, J. |
Citation: | Chemistry and Biology, 2015; 22(9):1250-1258 |
Publisher: | Elsevier (Cell Press) |
Issue Date: | 2015 |
ISSN: | 1074-5521 1879-1301 |
Statement of Responsibility: | 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 |
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. |
Keywords: | Escherichia coli Proline Peptides Antimicrobial Cationic Peptides Membrane Proteins Microscopy, Fluorescence Flow Cytometry Microbial Sensitivity Tests Structure-Activity Relationship Dimerization Proline-Rich Protein Domains |
Rights: | © 2015 Elsevier Ltd. All rights reserved. |
DOI: | 10.1016/j.chembiol.2015.08.011 |
Grant ID: | http://purl.org/au-research/grants/arc/DP150103522 http://purl.org/au-research/grants/nhmrc/1029878 http://purl.org/au-research/grants/nhmrc/1008106 |
Published version: | http://dx.doi.org/10.1016/j.chembiol.2015.08.011 |
Appears in Collections: | Aurora harvest 3 Medicine publications |
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