4.1 Article

Multimerization of a Proline-Rich Antimicrobial Peptide, Chex-Arg20, Alters Its Mechanism of Interaction with the Escherichia coli Membrane

期刊

CHEMISTRY & BIOLOGY
卷 22, 期 9, 页码 1250-1258

出版社

CELL PRESS
DOI: 10.1016/j.chembiol.2015.08.011

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资金

  1. ARC Discovery Project [DP150103522]
  2. NHMRC Project [APP1029878, APP1008106]
  3. MIRS PhD award
  4. Victorian Government's Operational Infrastructure Support Program

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A3-APO, a de novo designed branched dimeric pro-line-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.

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