Characterization and Biological Activities of Ocellatin Peptides from the Skin Secretion of the Frog Leptodactylus pustulatus

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• 作者：Mariela Mirta Marani ; Fl谩vio Santos Dourado ; Patrick Veras Quelemes ; Alyne Rodrigues de Araujo ; M谩rcia Luana Gomes Perfeito ; Eder Alves Barbosa ; Leiz Maria Costa V茅ras ; Andreia Lu铆sa Rodrigues Coelho ; Etielle Barroso Andrade ; Peter Eaton ; Jo茫o Paulo Figueir贸 Longo ; Ricardo Bentes Azevedo ; Cristina Delerue-Matos ; Jos茅 Roberto S. A. Leite
• 刊名：Journal of Natural Products
• 出版年：2015
• 出版时间：July 24, 2015
• 年：2015
• 卷：78
• 期：7
• 页码：1495-1504
• 全文大小：587K
• ISSN：1520-6025

文摘

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鈥?40 渭M 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.