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Antimicrobial activity of Ib-M peptides against Escherichia coli O157: H7
The development of new antimicrobial peptides has become an attractive alternative to conventional antibiotics due to the increasing rates of microbial drug resistance. Ib-M corresponds to a family of cationic synthetic peptides, 20 amino acids in length, that have shown inhibitory effect against th...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7018034/ https://www.ncbi.nlm.nih.gov/pubmed/32053687 http://dx.doi.org/10.1371/journal.pone.0229019 |
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author | Prada-Prada, Sergio Flórez-Castillo, Johanna Farfán-García, Ana Guzmán, Fanny Hernández-Peñaranda, Indira |
author_facet | Prada-Prada, Sergio Flórez-Castillo, Johanna Farfán-García, Ana Guzmán, Fanny Hernández-Peñaranda, Indira |
author_sort | Prada-Prada, Sergio |
collection | PubMed |
description | The development of new antimicrobial peptides has become an attractive alternative to conventional antibiotics due to the increasing rates of microbial drug resistance. Ib-M corresponds to a family of cationic synthetic peptides, 20 amino acids in length, that have shown inhibitory effect against the non-pathogenic strain Escherichia coli K-12. This work evaluated the antimicrobial potential of Ib-M peptides against the pathogenic E. coli O157: H7 using a reference strain and a clinical isolate. The Ib-M peptides showed antibacterial activity against both strains of E. coli O157: H7; the minimum inhibitory concentration of Ib-M peptides ranged from 1.6 to 12.5 μM and the minimum bactericidal concentration ranged from 3.7 to 22.9 μM, being Ib-M1 and Ib-M2 the peptides that presented the highest inhibitory effect. Time-kill kinetics assay showed a reduction of the bacterial population by more than 95% after 4 hours of exposure to 1xMIC of Ib-M1. Low cytotoxicity was observed in VERO cells with 50% cytotoxic concentration in the range from 197.5 to more than 400 μM. All peptides showed a random structure in hydrophilic environments, except Ib-M1, and all of them transitioned to an α-helical structure when the hydrophobicity of the medium was increased. In conclusion, these findings support the in vitro antimicrobial effect of Ib-M peptides against the pathogenic bacteria E. coli O157: H7 and prove to be promising molecules for the development of new therapeutic alternatives. |
format | Online Article Text |
id | pubmed-7018034 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-70180342020-02-26 Antimicrobial activity of Ib-M peptides against Escherichia coli O157: H7 Prada-Prada, Sergio Flórez-Castillo, Johanna Farfán-García, Ana Guzmán, Fanny Hernández-Peñaranda, Indira PLoS One Research Article The development of new antimicrobial peptides has become an attractive alternative to conventional antibiotics due to the increasing rates of microbial drug resistance. Ib-M corresponds to a family of cationic synthetic peptides, 20 amino acids in length, that have shown inhibitory effect against the non-pathogenic strain Escherichia coli K-12. This work evaluated the antimicrobial potential of Ib-M peptides against the pathogenic E. coli O157: H7 using a reference strain and a clinical isolate. The Ib-M peptides showed antibacterial activity against both strains of E. coli O157: H7; the minimum inhibitory concentration of Ib-M peptides ranged from 1.6 to 12.5 μM and the minimum bactericidal concentration ranged from 3.7 to 22.9 μM, being Ib-M1 and Ib-M2 the peptides that presented the highest inhibitory effect. Time-kill kinetics assay showed a reduction of the bacterial population by more than 95% after 4 hours of exposure to 1xMIC of Ib-M1. Low cytotoxicity was observed in VERO cells with 50% cytotoxic concentration in the range from 197.5 to more than 400 μM. All peptides showed a random structure in hydrophilic environments, except Ib-M1, and all of them transitioned to an α-helical structure when the hydrophobicity of the medium was increased. In conclusion, these findings support the in vitro antimicrobial effect of Ib-M peptides against the pathogenic bacteria E. coli O157: H7 and prove to be promising molecules for the development of new therapeutic alternatives. Public Library of Science 2020-02-13 /pmc/articles/PMC7018034/ /pubmed/32053687 http://dx.doi.org/10.1371/journal.pone.0229019 Text en © 2020 Prada-Prada et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Research Article Prada-Prada, Sergio Flórez-Castillo, Johanna Farfán-García, Ana Guzmán, Fanny Hernández-Peñaranda, Indira Antimicrobial activity of Ib-M peptides against Escherichia coli O157: H7 |
title | Antimicrobial activity of Ib-M peptides against Escherichia coli O157: H7 |
title_full | Antimicrobial activity of Ib-M peptides against Escherichia coli O157: H7 |
title_fullStr | Antimicrobial activity of Ib-M peptides against Escherichia coli O157: H7 |
title_full_unstemmed | Antimicrobial activity of Ib-M peptides against Escherichia coli O157: H7 |
title_short | Antimicrobial activity of Ib-M peptides against Escherichia coli O157: H7 |
title_sort | antimicrobial activity of ib-m peptides against escherichia coli o157: h7 |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7018034/ https://www.ncbi.nlm.nih.gov/pubmed/32053687 http://dx.doi.org/10.1371/journal.pone.0229019 |
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