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

@article{Li2015MultimerizationOA,
  title={Multimerization of a Proline-Rich Antimicrobial Peptide, Chex-Arg20, Alters Its Mechanism of Interaction with the Escherichia coli Membrane.},
  author={Wenyi Li and Neil M. O’Brien-Simpson and Julien Tailhades and Namfon Pantarat and Raymond Murray Dawson and Laszlo Otvos and Eric C. Reynolds and Frances Separovic and Mohammed Akhter Hossain and John D. Wade},
  journal={Chemistry \& biology},
  year={2015},
  volume={22 9},
  pages={
          1250-8
        }
}
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… 
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A number of unknown and unclassified peptides containing motifs of striking similarity to known PrAMP-based DnaK inhibitors are identified and a series of new sequences for experimental evaluation and subsequent addition to the PrAMP family are proposed.
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