A New Synthetic Peptide Having Two Target of Antibacterial Action in E. coli ML35

Adriana Barreto-Santamaría, Hernando Curtidor, Gabriela Arévalo-Pinzón, Chonny Herrera, Diana Suárez, Walter H Pérez, Manuel E Patarroyo

Resultado de la investigación: Contribución a RevistaArtículo

Resumen

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.

Idioma originalEnglish (US)
Número de artículo2006
Número de páginas11
PublicaciónFrontiers in Microbiology
Volumen7
DOI
EstadoPublished - dic 7 2016
Publicado de forma externa

Citar esto

Barreto-Santamaría, A., Curtidor, H., Arévalo-Pinzón, G., Herrera, C., Suárez, D., Pérez, W. H., & Patarroyo, M. E. (2016). A New Synthetic Peptide Having Two Target of Antibacterial Action in E. coli ML35. Frontiers in Microbiology, 7, [2006]. https://doi.org/10.3389/fmicb.2016.02006
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. En: Frontiers in Microbiology. 2016 ; Vol. 7.
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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) 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.",
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Barreto-Santamaría, A, Curtidor, H, Arévalo-Pinzón, G, Herrera, C, Suárez, D, Pérez, WH & Patarroyo, ME 2016, 'A New Synthetic Peptide Having Two Target of Antibacterial Action in E. coli ML35', Frontiers in Microbiology, vol. 7, 2006. https://doi.org/10.3389/fmicb.2016.02006

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.

En: Frontiers in Microbiology, Vol. 7, 2006, 07.12.2016.

Resultado de la investigación: Contribución a RevistaArtículo

TY - JOUR

T1 - A New Synthetic Peptide Having Two Target of Antibacterial Action in E. coli ML35

AU - Barreto-Santamaría, Adriana

AU - Curtidor, Hernando

AU - Arévalo-Pinzón, Gabriela

AU - Herrera, Chonny

AU - Suárez, Diana

AU - Pérez, Walter H

AU - Patarroyo, Manuel E

PY - 2016/12/7

Y1 - 2016/12/7

N2 - 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.

AB - 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.

U2 - 10.3389/fmicb.2016.02006

DO - 10.3389/fmicb.2016.02006

M3 - Article

C2 - 28066341

VL - 7

JO - Frontiers in Microbiology

JF - Frontiers in Microbiology

SN - 1664-302X

M1 - 2006

ER -

Barreto-Santamaría A, Curtidor H, Arévalo-Pinzón G, Herrera C, Suárez D, Pérez WH y otros. A New Synthetic Peptide Having Two Target of Antibacterial Action in E. coli ML35. Frontiers in Microbiology. 2016 dic 7;7. 2006. https://doi.org/10.3389/fmicb.2016.02006