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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...

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Autores principales: 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
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
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.
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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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