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Cm-p5 Peptide Dimers Inhibit Biofilms of Candida albicans Clinical Isolates, C. parapsilosis and Fluconazole-Resistant Mutants of C. auris
Antimicrobial peptides (AMPs) represent a promising class of therapeutic biomolecules that show antimicrobial activity against a broad range of microorganisms, including life-threatening pathogens. In contrast to classic AMPs with membrane-disrupting activities, new peptides with a specific anti-bio...
Autores principales: | , , , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10298552/ https://www.ncbi.nlm.nih.gov/pubmed/37372935 http://dx.doi.org/10.3390/ijms24129788 |
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author | Amann, Valerie Kissmann, Ann-Kathrin Mildenberger, Vanessa Krebs, Imke Perez-Erviti, Julio A. Martell-Huguet, Ernesto M. Otero-Gonzalez, Anselmo J. Morales-Vicente, Fidel Rodríguez-Castaño, Gina P. Firacative, Carolina Rodríguez, Armando Ständker, Ludger Weil, Tanja Spellerberg, Barbara Stenger, Steffen Rosenau, Frank |
author_facet | Amann, Valerie Kissmann, Ann-Kathrin Mildenberger, Vanessa Krebs, Imke Perez-Erviti, Julio A. Martell-Huguet, Ernesto M. Otero-Gonzalez, Anselmo J. Morales-Vicente, Fidel Rodríguez-Castaño, Gina P. Firacative, Carolina Rodríguez, Armando Ständker, Ludger Weil, Tanja Spellerberg, Barbara Stenger, Steffen Rosenau, Frank |
author_sort | Amann, Valerie |
collection | PubMed |
description | Antimicrobial peptides (AMPs) represent a promising class of therapeutic biomolecules that show antimicrobial activity against a broad range of microorganisms, including life-threatening pathogens. In contrast to classic AMPs with membrane-disrupting activities, new peptides with a specific anti-biofilm effect are gaining in importance since biofilms could be the most important way of life, especially for pathogens, as the interaction with host tissues is crucial for the full development of their virulence in the event of infection. Therefore, in a previous study, two synthetic dimeric derivatives (parallel Dimer 1 and antiparallel Dimer 2) of the AMP Cm-p5 showed specific inhibition of the formation of Candida auris biofilms. Here we show that these derivatives are also dose-dependently effective against de novo biofilms that are formed by the widespread pathogenic yeasts C. albicans and C. parapsilosis. Moreover, the activity of the peptides was demonstrated even against two fluconazole-resistant strains of C. auris. |
format | Online Article Text |
id | pubmed-10298552 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-102985522023-06-28 Cm-p5 Peptide Dimers Inhibit Biofilms of Candida albicans Clinical Isolates, C. parapsilosis and Fluconazole-Resistant Mutants of C. auris Amann, Valerie Kissmann, Ann-Kathrin Mildenberger, Vanessa Krebs, Imke Perez-Erviti, Julio A. Martell-Huguet, Ernesto M. Otero-Gonzalez, Anselmo J. Morales-Vicente, Fidel Rodríguez-Castaño, Gina P. Firacative, Carolina Rodríguez, Armando Ständker, Ludger Weil, Tanja Spellerberg, Barbara Stenger, Steffen Rosenau, Frank Int J Mol Sci Communication Antimicrobial peptides (AMPs) represent a promising class of therapeutic biomolecules that show antimicrobial activity against a broad range of microorganisms, including life-threatening pathogens. In contrast to classic AMPs with membrane-disrupting activities, new peptides with a specific anti-biofilm effect are gaining in importance since biofilms could be the most important way of life, especially for pathogens, as the interaction with host tissues is crucial for the full development of their virulence in the event of infection. Therefore, in a previous study, two synthetic dimeric derivatives (parallel Dimer 1 and antiparallel Dimer 2) of the AMP Cm-p5 showed specific inhibition of the formation of Candida auris biofilms. Here we show that these derivatives are also dose-dependently effective against de novo biofilms that are formed by the widespread pathogenic yeasts C. albicans and C. parapsilosis. Moreover, the activity of the peptides was demonstrated even against two fluconazole-resistant strains of C. auris. MDPI 2023-06-06 /pmc/articles/PMC10298552/ /pubmed/37372935 http://dx.doi.org/10.3390/ijms24129788 Text en © 2023 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 | Communication Amann, Valerie Kissmann, Ann-Kathrin Mildenberger, Vanessa Krebs, Imke Perez-Erviti, Julio A. Martell-Huguet, Ernesto M. Otero-Gonzalez, Anselmo J. Morales-Vicente, Fidel Rodríguez-Castaño, Gina P. Firacative, Carolina Rodríguez, Armando Ständker, Ludger Weil, Tanja Spellerberg, Barbara Stenger, Steffen Rosenau, Frank Cm-p5 Peptide Dimers Inhibit Biofilms of Candida albicans Clinical Isolates, C. parapsilosis and Fluconazole-Resistant Mutants of C. auris |
title | Cm-p5 Peptide Dimers Inhibit Biofilms of Candida albicans Clinical Isolates, C. parapsilosis and Fluconazole-Resistant Mutants of C. auris |
title_full | Cm-p5 Peptide Dimers Inhibit Biofilms of Candida albicans Clinical Isolates, C. parapsilosis and Fluconazole-Resistant Mutants of C. auris |
title_fullStr | Cm-p5 Peptide Dimers Inhibit Biofilms of Candida albicans Clinical Isolates, C. parapsilosis and Fluconazole-Resistant Mutants of C. auris |
title_full_unstemmed | Cm-p5 Peptide Dimers Inhibit Biofilms of Candida albicans Clinical Isolates, C. parapsilosis and Fluconazole-Resistant Mutants of C. auris |
title_short | Cm-p5 Peptide Dimers Inhibit Biofilms of Candida albicans Clinical Isolates, C. parapsilosis and Fluconazole-Resistant Mutants of C. auris |
title_sort | cm-p5 peptide dimers inhibit biofilms of candida albicans clinical isolates, c. parapsilosis and fluconazole-resistant mutants of c. auris |
topic | Communication |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10298552/ https://www.ncbi.nlm.nih.gov/pubmed/37372935 http://dx.doi.org/10.3390/ijms24129788 |
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