Utilize este identificador para referenciar este registo: http://hdl.handle.net/10400.22/7227
Título: Characterization and Biological Activities of Ocellatin Peptides from the Skin Secretion of the Frog Leptodactylus pustulatus
Autor: Marani, Mariela Mirta
Dourado, Flávio Santos
Quelemes, Patrick Veras
Araujo, Alyne Rodrigues de
Perfeito, Márcia Luana Gomes
Barbosa, Eder Alves
Véras, Leiz Maria Costa
Coelho, Andreia Luísa Rodrigues
Andrade, Etielle Barroso
Eaton, Peter
Longo, João Paulo Figueiró
Azevedo, Ricardo Bentes
Delerue-Matos, Cristina
Leite, José Roberto S. A.
Data: Jun-2015
Editora: ACS Publications
Relatório da Série N.º: Journal of Natural Products;Vol. 78, Issue 7
Resumo: 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, hemolytic tests, and cytotoxicity against a murine fibroblast cell line were investigated. All peptides, except for ocellatin-PT2, have antimicrobial activity against at least one Gram negative strain. Ocellatin-PT8 inhibited the growth of Escherichia coli, Staphylococcus aureus, Klebsiella pneumoniae, and Salmonella choleraesuis strains with MICs in the 60−240 μM range. No significant effect was observed in human erythrocytes and in a murine fibroblast cell line after exposure to the peptides at MICs. A comparison between sequences obtained by both direct HPLC-MS de novo sequencing and cDNA cloning demonstrates the secretion of mature peptides derived from a pre-pro-peptide structure.
URI: http://hdl.handle.net/10400.22/7227
DOI: 10.1021/np500907t
Versão do Editor: http://pubs.acs.org/doi/abs/10.1021/np500907t
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