Synergistic Antipseudomonal Effects of Synthetic Peptide AMP38 and Carbapenems

The aim was to explore the antimicrobial activity of a synthetic peptide (AMP38) and its synergy with imipenem against imipenem-resistant Pseudomonas aeruginosa. The main mechanism of imipenem resistance is the loss or alteration of protein OprD. Time-kill and minimal biofilm eradication concentrati...

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Autores principales: Rudilla, Héctor, Fusté, Ester, Cajal, Yolanda, Rabanal, Francesc, Vinuesa, Teresa, Viñas, Miguel
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2016
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6273456/
https://www.ncbi.nlm.nih.gov/pubmed/27626405
http://dx.doi.org/10.3390/molecules21091223
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author Rudilla, Héctor
Fusté, Ester
Cajal, Yolanda
Rabanal, Francesc
Vinuesa, Teresa
Viñas, Miguel
author_facet Rudilla, Héctor
Fusté, Ester
Cajal, Yolanda
Rabanal, Francesc
Vinuesa, Teresa
Viñas, Miguel
author_sort Rudilla, Héctor
collection PubMed
description The aim was to explore the antimicrobial activity of a synthetic peptide (AMP38) and its synergy with imipenem against imipenem-resistant Pseudomonas aeruginosa. The main mechanism of imipenem resistance is the loss or alteration of protein OprD. Time-kill and minimal biofilm eradication concentration (MBEC) determinations were carried out by using clinical imipenem-resistant strains. AMP38 was markedly synergistic with imipenem when determined in imipenem-resistant P. aeruginosa. MBEC obtained for the combination of AMP38 and imipenem was of 62.5 μg/mL, whereas the MBEC of each antimicrobial separately was 500 μg/mL. AMP38 should be regarded as a promising antimicrobial to fight MDR P. aeruginosa infections. Moreover, killing effect and antibiofilm activity of AMP38 plus imipenem was much higher than that of colistin plus imipenem.
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spelling pubmed-62734562018-12-28 Synergistic Antipseudomonal Effects of Synthetic Peptide AMP38 and Carbapenems Rudilla, Héctor Fusté, Ester Cajal, Yolanda Rabanal, Francesc Vinuesa, Teresa Viñas, Miguel Molecules Article The aim was to explore the antimicrobial activity of a synthetic peptide (AMP38) and its synergy with imipenem against imipenem-resistant Pseudomonas aeruginosa. The main mechanism of imipenem resistance is the loss or alteration of protein OprD. Time-kill and minimal biofilm eradication concentration (MBEC) determinations were carried out by using clinical imipenem-resistant strains. AMP38 was markedly synergistic with imipenem when determined in imipenem-resistant P. aeruginosa. MBEC obtained for the combination of AMP38 and imipenem was of 62.5 μg/mL, whereas the MBEC of each antimicrobial separately was 500 μg/mL. AMP38 should be regarded as a promising antimicrobial to fight MDR P. aeruginosa infections. Moreover, killing effect and antibiofilm activity of AMP38 plus imipenem was much higher than that of colistin plus imipenem. MDPI 2016-09-12 /pmc/articles/PMC6273456/ /pubmed/27626405 http://dx.doi.org/10.3390/molecules21091223 Text en © 2016 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC-BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Rudilla, Héctor
Fusté, Ester
Cajal, Yolanda
Rabanal, Francesc
Vinuesa, Teresa
Viñas, Miguel
Synergistic Antipseudomonal Effects of Synthetic Peptide AMP38 and Carbapenems
title Synergistic Antipseudomonal Effects of Synthetic Peptide AMP38 and Carbapenems
title_full Synergistic Antipseudomonal Effects of Synthetic Peptide AMP38 and Carbapenems
title_fullStr Synergistic Antipseudomonal Effects of Synthetic Peptide AMP38 and Carbapenems
title_full_unstemmed Synergistic Antipseudomonal Effects of Synthetic Peptide AMP38 and Carbapenems
title_short Synergistic Antipseudomonal Effects of Synthetic Peptide AMP38 and Carbapenems
title_sort synergistic antipseudomonal effects of synthetic peptide amp38 and carbapenems
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6273456/
https://www.ncbi.nlm.nih.gov/pubmed/27626405
http://dx.doi.org/10.3390/molecules21091223
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