A new synthetic peptide having two target of antibacterial action in E. coli ML35

The increased resistance of microorganisms to the different antimicrobials available to today has highlighted the need to find new therapeutic agents, including natural and/or synthetic antimicrobial peptides (AMPs). This study has evaluated the antimicrobial activity of synthetic peptide 35409 (RYRRKKKMKKALQYIKLLKE) against Staphylococcus aureus ATCC 29213, Pseudomonas aeruginosa ATCC 15442 and Escherichia coli ML 35 (ATCC 43827). The results have shown that peptide 35409 inhibited the growth of these three bacterial strains, having 16-fold greater activity against E. coli and P. aeruginosa, but requiring less concentration regarding E. coli (22 μM). When analyzing this activity against E. coli compared to time taken, it was found that this peptide inhibited bacterial growth during the first 60 min and reduced CFU/mL 1 log after 120 min had elapsed. This AMP permeabilized the E. coli membrane by interaction with membrane phospholipids, mainly phosphatidylethanolamine, inhibited cell division and induced filamentation, suggesting two different targets of action within a bacterial cell. Cytotoxicity studies revealed that peptide 35409 had low hemolytic activity and was not cytotoxic for two human cell lines. We would thus propose, in the light of these findings, that the peptide 35409 sequence should provide a promising template for designing broad-spectrum AMPs. © 2016 Barreto-Santamaría, Curtidor, Arévalo-Pinzón, Herrera, Suárez, Pérez and Patarroyo.

• Fecha de publicación: 2016
• Institución: Universidad del Rosario
• Repositorio: Repositorio EdocUR - U. Rosario
• Idioma: eng
• OAI Identifier: oai:repository.urosario.edu.co:10336/19144
• Acceso en línea: http://repository.urosario.edu.co/handle/10336/19144
• Palabra clave: Peptide 35409; Phosphatidylethanolamine; Polypeptide antibiotic agent; Unclassified drug; Antibacterial activity; Bacterial growth; Cell division; Circular dichroism; Colony forming unit; Controlled study; Cytotoxicity; DNA binding; Biología; Peptidos; Microorganismos
• License: Abierto (Texto Completo)