Origin of low mammalian cell toxicity in a class of highly active antimicrobial amphipathic helical peptides.

@article{Hawrani2008OriginOL,
  title={Origin of low mammalian cell toxicity in a class of highly active antimicrobial amphipathic helical peptides.},
  author={Ayman S Hawrani and Robin A. Howe and Timothy R. Walsh and Christopher E. Dempsey},
  journal={The Journal of biological chemistry},
  year={2008},
  volume={283 27},
  pages={18636-45}
}
We recently described a novel antimicrobial peptide, RTA3, derived from the commensal organism Streptococcus mitis, with strong anti-Gram-negative activity, low salt sensitivity, and minimal mammalian cell toxicity in vitro and in vivo. This peptide conforms to the positively charged, amphipathic helical peptide motif, but has a positively charged amino acid (Arg-5) on the nonpolar face of the helical structure that is induced upon membrane binding. We surmised that disruption of the… CONTINUE READING

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