The NH2-terminal alpha-helical domain 1-18 of dermaseptin is responsible for antimicrobial activity.

@article{Mor1994TheNA,
  title={The NH2-terminal alpha-helical domain 1-18 of dermaseptin is responsible for antimicrobial activity.},
  author={A. Mor and P. Nicolas},
  journal={The Journal of biological chemistry},
  year={1994},
  volume={269 3},
  pages={
          1934-9
        }
}
  • A. Mor, P. Nicolas
  • Published 1994
  • Biology, Medicine
  • The Journal of biological chemistry
Dermaseptin, a 34-amino acid residue cationic peptide, was recently shown to inhibit the growth of pathogenic fungi responsible for severe opportunistic infections accompanying immunodeficiency syndrome and the use of immunosuppressive agents. To improve our understanding of the mechanism by which dermaseptin exerts its potent antimicrobial action, a series of either NH2- or COOH-terminally truncated analogs was synthesized. These analogs were evaluated for their ability to inhibit the growth… Expand
Structure, synthesis, and activity of dermaseptin b, a novel vertebrate defensive peptide from frog skin: relationship with adenoregulin.
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References

ACS Symp . Ser : 222 - 235 ( 1991 )
  • Proc . Natl . Acad . Sci . U . S . A .
  • 1991