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.
- Amphipathic α-helix
- Frog skin
ASJC Scopus subject areas
- Cellular and Molecular Neuroscience