Purification and characterization of antimicrobial peptides from the Caribbean frog, Leptodactylus validus (Anura: Leptodactylidae)

Jay D. King, Jérôme Leprince, Hubert Vaudry, Laurent Coquet, Thierry Jouenne, J. Michael Conlon

Research output: Contribution to journalArticlepeer-review

16 Citations (Scopus)

Abstract

Peptidomic analysis of norepinephrine-stimulated skin secretions from the Caribbean frog Leptodactylus validus Garman, 1888 led to the identification of three peptides with previously undescribed sequences that were structurally similar to those of antimicrobial peptides isolated from other species of leptodactylid frogs. These paralogs have been termed ocellatin-V1 (GVVDILKGAGKDLLAHALSKLSEKV.NH2), ocellatin-V2 (GVLDILKGAGKDLLAHALSKISEKV.NH2), and ocellatin-V3 (GVLDILTGAGKDLLAHALSKLSEKV.NH2). The very low antimicrobial potency (MIC > 200 μM) against Escherichia coli and Staphylococcus aureus associated with the peptides is probably a consequence of their lack of amphipathicity and reduced cationicity compared with active members of the ocellatin family from related species.

Original languageEnglish
Pages (from-to)1287-1292
Number of pages6
JournalPeptides
Volume29
Issue number8
DOIs
Publication statusPublished - Aug 2008
Externally publishedYes

Keywords

  • Amphipathic α-helix
  • Antimicrobial
  • Frog skin
  • Ocellatin

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Endocrinology
  • Cellular and Molecular Neuroscience

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