Publications

characterization and biological activities of ocellatin peptides from the skin secretion of the frog leptodactylus pustulatus.	eight new peptides were isolated from the skin secretion of the frog leptodactylus pustulatus and their amino acid sequences determined by de novo sequencing and by cdna cloning. structural similarities between them and other antimicrobial peptides from the skin secretion of leptodactylus genus frogs were found. ocellatins-pt1 to -pt5 (25 amino acid residues) are amidated at the c-terminus, while ocellatins-pt6 to -pt8 (32 amino acid residues) have free carboxylates. antimicrobial activity, hemo ...	2015	26107622
ocellatin-pt antimicrobial peptides: high-resolution microscopy studies in antileishmania models and interactions with mimetic membrane systems.	although the mechanism of action of antimicrobial peptides (amps) is not clear, they can interact electrostatically with the cell membranes of microorganisms. new ocellatin-pt peptides were recently isolated from the skin secretion of leptodactylus pustulatus. the secondary structure of these amps and their effect on leishmania infantum cells, and on different lipid surface models was characterized in this work. the results showed that all ocellatin-pt peptides have an α-helix structure and five ...	2016	27463422