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|Title:||Multimerization of a proline-rich antimicrobial peptide, Chex-Arg20, alters its mechanism of interaction with the Escherichia coli membrane|
|Citation:||Chemistry and Biology, 2015; 22(9):1250-1258|
|Publisher:||Elsevier (Cell Press)|
|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.|
|Appears in Collections:||Medicine publications|
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