Structural features of helical antimicrobial peptides: their potential to modulate activity on model membranes and biological cells.

@article{Dathe1999StructuralFO,
  title={Structural features of helical antimicrobial peptides: their potential to modulate activity on model membranes and biological cells.},
  author={Margitta Dathe and Torsten Wieprecht},
  journal={Biochimica et biophysica acta},
  year={1999},
  volume={1462 1-2},
  pages={
          71-87
        }
}
Antibacterial, membrane-lytic peptides belong to the innate immune system and host defense mechanism of a multitude of animals and plants. The largest group of peptide antibiotics comprises peptides which fold into an amphipathic alpha-helical conformation when interacting with the target. The activity of these peptides is thought to be determined by global structural parameters rather than by the specific amino acid sequence. This review is concerned with the influence of structural parameters… CONTINUE READING

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