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Activity and Synergy of Cu-ATCUN Antimicrobial Peptides

Antibiotic resistance demands innovative strategies and therapies. The pairs of antimicrobial peptides tested in this work show broad-spectrum synergy and are capable of interacting with diverse bacterial membranes. In most cases, the ATCUN motif enhanced the activity of peptides tested in combinati...

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Detalles Bibliográficos
Autores principales: Greve, Jenna M., Cowan, J. A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9692552/
https://www.ncbi.nlm.nih.gov/pubmed/36430622
http://dx.doi.org/10.3390/ijms232214151
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author Greve, Jenna M.
Cowan, J. A.
author_facet Greve, Jenna M.
Cowan, J. A.
author_sort Greve, Jenna M.
collection PubMed
description Antibiotic resistance demands innovative strategies and therapies. The pairs of antimicrobial peptides tested in this work show broad-spectrum synergy and are capable of interacting with diverse bacterial membranes. In most cases, the ATCUN motif enhanced the activity of peptides tested in combination. Our studies also show CP10A to be a multifaceted peptide, displaying both cell membrane and intracellular activity and acting as a chameleon, improving the activity of other peptides as needed. The results of the synergy experiments demonstrate the importance of varied modes of action and how these changes can affect the ability to combat pathogens, while also illustrating the value of the metal-binding domain in enhancing the activity of antimicrobial peptides in combination.
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spelling pubmed-96925522022-11-26 Activity and Synergy of Cu-ATCUN Antimicrobial Peptides Greve, Jenna M. Cowan, J. A. Int J Mol Sci Article Antibiotic resistance demands innovative strategies and therapies. The pairs of antimicrobial peptides tested in this work show broad-spectrum synergy and are capable of interacting with diverse bacterial membranes. In most cases, the ATCUN motif enhanced the activity of peptides tested in combination. Our studies also show CP10A to be a multifaceted peptide, displaying both cell membrane and intracellular activity and acting as a chameleon, improving the activity of other peptides as needed. The results of the synergy experiments demonstrate the importance of varied modes of action and how these changes can affect the ability to combat pathogens, while also illustrating the value of the metal-binding domain in enhancing the activity of antimicrobial peptides in combination. MDPI 2022-11-16 /pmc/articles/PMC9692552/ /pubmed/36430622 http://dx.doi.org/10.3390/ijms232214151 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/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 (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Greve, Jenna M.
Cowan, J. A.
Activity and Synergy of Cu-ATCUN Antimicrobial Peptides
title Activity and Synergy of Cu-ATCUN Antimicrobial Peptides
title_full Activity and Synergy of Cu-ATCUN Antimicrobial Peptides
title_fullStr Activity and Synergy of Cu-ATCUN Antimicrobial Peptides
title_full_unstemmed Activity and Synergy of Cu-ATCUN Antimicrobial Peptides
title_short Activity and Synergy of Cu-ATCUN Antimicrobial Peptides
title_sort activity and synergy of cu-atcun antimicrobial peptides
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9692552/
https://www.ncbi.nlm.nih.gov/pubmed/36430622
http://dx.doi.org/10.3390/ijms232214151
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