title: A New Synthetic Peptide Having Two Target of Antibacterial Action inE. coliML35.
abstract: 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) againstStaphylococcus aureusATCC 29213,Pseudomonas aeruginosaATCC 15442 andEscherichia coliML 35 (ATCC 43827). The results have shown that peptide 35409 inhibited the growth of these three bacterial strains, having 16-fold greater activity againstE. coliandP. aeruginosa, but requiring less concentration regardingE. coli(22 μM). When analyzing this activity againstE. colicompared 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 theE. colimembrane 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.
authors.affiliation: Receptor-Ligand Department, Fundación Instituto de Inmunología de ColombiaBogotá, Colombia; Faculty of Sciences and Education, Universidad Distrital Francisco José de CaldasBogotá, Colombia; School of Medicine and Health sciences, Universidad del RosarioBogotá, Colombia.
authors.forename: Adriana
authors.initials: A
authors.lastname: Barreto-Santamaría
authors.affiliation: Receptor-Ligand Department, Fundación Instituto de Inmunología de ColombiaBogotá, Colombia; School of Medicine and Health sciences, Universidad del RosarioBogotá, Colombia.
authors.forename: Hernando
authors.initials: H
authors.lastname: Curtidor
authors.affiliation: Receptor-Ligand Department, Fundación Instituto de Inmunología de ColombiaBogotá, Colombia; School of Medicine and Health sciences, Universidad del RosarioBogotá, Colombia.
authors.forename: Gabriela
authors.initials: G
authors.lastname: Arévalo-Pinzón
authors.affiliation: Receptor-Ligand Department, Fundación Instituto de Inmunología de ColombiaBogotá, Colombia; School of Medicine and Health sciences, Universidad del RosarioBogotá, Colombia.
authors.forename: Chonny
authors.initials: C
authors.lastname: Herrera
authors.affiliation: Receptor-Ligand Department, Fundación Instituto de Inmunología de ColombiaBogotá, Colombia; School of Medicine and Health sciences, Universidad del RosarioBogotá, Colombia.
authors.forename: Diana
authors.initials: D
authors.lastname: Suárez
authors.affiliation: Escuela Colombiana de Carreras Industriales Bogotá, Colombia.
authors.forename: Walter H
authors.initials: WH
authors.lastname: Pérez
authors.affiliation: Receptor-Ligand Department, Fundación Instituto de Inmunología de ColombiaBogotá, Colombia; Faculty of Medicine, Universidad Nacional de ColombiaBogotá, Colombia.
authors.forename: Manuel E
authors.initials: ME
authors.lastname: Patarroyo
keywords: antimicrobial peptide (AMP); liposome; membrane permeabilization; membrane phospholipid; minimum inhibitory concentration (MIC); synthetic peptide