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 (RYR...

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Autores Principales: Barreto-Santamaría, Adriana, Curtidor, Hernando, Arévalo-Pinzón, Gabriela, Herrera, Chonny, Suárez, Diana, Pérez, Walter H., Patarroyo, Manuel E.
Formato: Artículo (Article)
Lenguaje:Inglés (English)
Publicado: 2016
Materias:
Acceso en línea:http://repository.urosario.edu.co/handle/10336/19144
id ir-10336-19144
recordtype dspace
spelling ir-10336-191442019-09-19T12:37:54Z A new synthetic peptide having two target of antibacterial action in E. coli ML35 Barreto-Santamaría, Adriana Curtidor, Hernando Arévalo-Pinzón, Gabriela Herrera, Chonny Suárez, Diana Pérez, Walter H. Patarroyo, Manuel E. 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 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. 2016 2019-02-26T16:11:19Z info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion 1664-302X http://repository.urosario.edu.co/handle/10336/19144 10.3389/fmicb.2016.02006 eng info:eu-repo/semantics/openAccess application/pdf
institution EdocUR - Universidad del Rosario
collection DSpace
language Inglés (English)
topic 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
spellingShingle 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
Barreto-Santamaría, Adriana
Curtidor, Hernando
Arévalo-Pinzón, Gabriela
Herrera, Chonny
Suárez, Diana
Pérez, Walter H.
Patarroyo, Manuel E.
A new synthetic peptide having two target of antibacterial action in E. coli ML35
description 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.
format Artículo (Article)
author Barreto-Santamaría, Adriana
Curtidor, Hernando
Arévalo-Pinzón, Gabriela
Herrera, Chonny
Suárez, Diana
Pérez, Walter H.
Patarroyo, Manuel E.
author_facet Barreto-Santamaría, Adriana
Curtidor, Hernando
Arévalo-Pinzón, Gabriela
Herrera, Chonny
Suárez, Diana
Pérez, Walter H.
Patarroyo, Manuel E.
author_sort Barreto-Santamaría, Adriana
title A new synthetic peptide having two target of antibacterial action in E. coli ML35
title_short A new synthetic peptide having two target of antibacterial action in E. coli ML35
title_full A new synthetic peptide having two target of antibacterial action in E. coli ML35
title_fullStr A new synthetic peptide having two target of antibacterial action in E. coli ML35
title_full_unstemmed A new synthetic peptide having two target of antibacterial action in E. coli ML35
title_sort new synthetic peptide having two target of antibacterial action in e. coli ml35
publishDate 2016
url http://repository.urosario.edu.co/handle/10336/19144
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score 10,762939