Purification and properties of laticeptin, an antimicrobial peptide from skin secretions of the south American frog Leptodactylus laticeps

J. Michael Conlon, Nadia Al-Ghaferi, Bency Abraham, Agnes Sonnevend, Jay D. King, Per F. Nielsen

Research output: Contribution to journalArticlepeer-review

24 Citations (Scopus)

Abstract

Norepinephrine-stimulated skin secretions from the Sante Fe frog Leptodactylus laticeps contained high concentrations of a peptide, termed laticeptin, with the primary structure Gly-Val-Val-Asp-Ile-Leu-Lys-Gly-Ala-Ala- Lys-Asp-Leu-Ala-Gly-His-Leu-Ala-Thr-Lys-Val-Met-Asn-Lys-Leu.NH2. Laticeptin inhibited the growth of selected Gram-negative bacteria but the lack of activity against Gram-positive bacteria and the very low hemolytic activity is probably a consequence of the weak amphipathicity of the peptide in its ́-helical conformation.

Original languageEnglish
Pages (from-to)411-415
Number of pages5
JournalProtein and Peptide Letters
Volume13
Issue number4
DOIs
Publication statusPublished - Apr 2006
Externally publishedYes

Keywords

  • Antimicrobial peptide
  • Fallaxin
  • Frog skin
  • Laticeptin
  • Leptodactylidae

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry

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