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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...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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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. |
format | Online Article Text |
id | pubmed-9692552 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT grevejennam activityandsynergyofcuatcunantimicrobialpeptides AT cowanja activityandsynergyofcuatcunantimicrobialpeptides |