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Increased Activities against Biofilms of the Pathogenic Yeast Candida albicans of Optimized Pom-1 Derivatives
Antimicrobial peptides (AMPs) are an alternative group for the therapy of infectious diseases, with activity against a wide range of diverse pathogens. However, classical AMPs have significant side effects in human cells due to their unspecific pore formation in biomembranes. Nevertheless, AMPs are...
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/PMC8877593/ https://www.ncbi.nlm.nih.gov/pubmed/35214049 http://dx.doi.org/10.3390/pharmaceutics14020318 |
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author | Amann, Valerie Kissmann, Ann-Kathrin Krämer, Markus Krebs, Imke Perez-Erviti, Julio A. Otero-Gonzalez, Anselmo J. Morales-Vicente, Fidel Rodríguez, Armando Ständker, Ludger Weil, Tanja Rosenau, Frank |
author_facet | Amann, Valerie Kissmann, Ann-Kathrin Krämer, Markus Krebs, Imke Perez-Erviti, Julio A. Otero-Gonzalez, Anselmo J. Morales-Vicente, Fidel Rodríguez, Armando Ständker, Ludger Weil, Tanja Rosenau, Frank |
author_sort | Amann, Valerie |
collection | PubMed |
description | Antimicrobial peptides (AMPs) are an alternative group for the therapy of infectious diseases, with activity against a wide range of diverse pathogens. However, classical AMPs have significant side effects in human cells due to their unspecific pore formation in biomembranes. Nevertheless, AMPs are promising therapeutics and can be isolated from natural sources, which include sea and freshwater molluscs. The AMPs identified in these organisms show promising antimicrobial activities, as pathogens are mainly fought by innate defence mechanisms. An auspicious candidate among molluscs is the Cuban freshwater snail Pomacea poeyana, from which the peptides Pom-1 and Pom-2 have been isolated and studied. These studies revealed significant antimicrobial activities for both AMPs. Based on the activities determined, Pom-1 was used for further optimization. In order to meet the emerging requirements of improved anti-biofilm activity against naturally occurring Candida species, the six derivatives Pom-1A to F were developed and investigated. Analysis of the derivatives acting on the most abundant naturally occurring Candida yeast Candida albicans (C. albicans) revealed a strong anti-biofilm activity, especially induced by Pom-1 B, C, and D. Furthermore, a moderate decrease in the metabolic activity of planktonic yeast cells was observed. |
format | Online Article Text |
id | pubmed-8877593 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-88775932022-02-26 Increased Activities against Biofilms of the Pathogenic Yeast Candida albicans of Optimized Pom-1 Derivatives Amann, Valerie Kissmann, Ann-Kathrin Krämer, Markus Krebs, Imke Perez-Erviti, Julio A. Otero-Gonzalez, Anselmo J. Morales-Vicente, Fidel Rodríguez, Armando Ständker, Ludger Weil, Tanja Rosenau, Frank Pharmaceutics Communication Antimicrobial peptides (AMPs) are an alternative group for the therapy of infectious diseases, with activity against a wide range of diverse pathogens. However, classical AMPs have significant side effects in human cells due to their unspecific pore formation in biomembranes. Nevertheless, AMPs are promising therapeutics and can be isolated from natural sources, which include sea and freshwater molluscs. The AMPs identified in these organisms show promising antimicrobial activities, as pathogens are mainly fought by innate defence mechanisms. An auspicious candidate among molluscs is the Cuban freshwater snail Pomacea poeyana, from which the peptides Pom-1 and Pom-2 have been isolated and studied. These studies revealed significant antimicrobial activities for both AMPs. Based on the activities determined, Pom-1 was used for further optimization. In order to meet the emerging requirements of improved anti-biofilm activity against naturally occurring Candida species, the six derivatives Pom-1A to F were developed and investigated. Analysis of the derivatives acting on the most abundant naturally occurring Candida yeast Candida albicans (C. albicans) revealed a strong anti-biofilm activity, especially induced by Pom-1 B, C, and D. Furthermore, a moderate decrease in the metabolic activity of planktonic yeast cells was observed. MDPI 2022-01-28 /pmc/articles/PMC8877593/ /pubmed/35214049 http://dx.doi.org/10.3390/pharmaceutics14020318 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 | Communication Amann, Valerie Kissmann, Ann-Kathrin Krämer, Markus Krebs, Imke Perez-Erviti, Julio A. Otero-Gonzalez, Anselmo J. Morales-Vicente, Fidel Rodríguez, Armando Ständker, Ludger Weil, Tanja Rosenau, Frank Increased Activities against Biofilms of the Pathogenic Yeast Candida albicans of Optimized Pom-1 Derivatives |
title | Increased Activities against Biofilms of the Pathogenic Yeast Candida albicans of Optimized Pom-1 Derivatives |
title_full | Increased Activities against Biofilms of the Pathogenic Yeast Candida albicans of Optimized Pom-1 Derivatives |
title_fullStr | Increased Activities against Biofilms of the Pathogenic Yeast Candida albicans of Optimized Pom-1 Derivatives |
title_full_unstemmed | Increased Activities against Biofilms of the Pathogenic Yeast Candida albicans of Optimized Pom-1 Derivatives |
title_short | Increased Activities against Biofilms of the Pathogenic Yeast Candida albicans of Optimized Pom-1 Derivatives |
title_sort | increased activities against biofilms of the pathogenic yeast candida albicans of optimized pom-1 derivatives |
topic | Communication |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8877593/ https://www.ncbi.nlm.nih.gov/pubmed/35214049 http://dx.doi.org/10.3390/pharmaceutics14020318 |
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