Cm-p5 Peptide Dimers Inhibit Biofilms of <i>Candida albicans</i> Clinical Isolates, <i>C. parapsilosis</i> and Fluconazole-Resistant Mutants of <i>C. auris</i>
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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| Format: | Article |
| Language: | English |
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MDPI AG
2023-06-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/24/12/9788 |
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| author | Valerie Amann Ann-Kathrin Kissmann Vanessa Mildenberger Imke Krebs Julio A. Perez-Erviti Ernesto M. Martell-Huguet Anselmo J. Otero-Gonzalez Fidel Morales-Vicente Gina P. Rodríguez-Castaño Carolina Firacative Armando Rodríguez Ludger Ständker Tanja Weil Barbara Spellerberg Steffen Stenger Frank Rosenau |
| author_facet | Valerie Amann Ann-Kathrin Kissmann Vanessa Mildenberger Imke Krebs Julio A. Perez-Erviti Ernesto M. Martell-Huguet Anselmo J. Otero-Gonzalez Fidel Morales-Vicente Gina P. Rodríguez-Castaño Carolina Firacative Armando Rodríguez Ludger Ständker Tanja Weil Barbara Spellerberg Steffen Stenger Frank Rosenau |
| author_sort | Valerie Amann |
| collection | DOAJ |
| 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 <i>Candida auris</i> biofilms. Here we show that these derivatives are also dose-dependently effective against de novo biofilms that are formed by the widespread pathogenic yeasts <i>C. albicans</i> and <i>C. parapsilosis</i>. Moreover, the activity of the peptides was demonstrated even against two fluconazole-resistant strains of <i>C. auris</i>. |
| first_indexed | 2024-03-11T02:22:42Z |
| format | Article |
| id | doaj.art-9e6688a4eab744adbc75e388b66890ad |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-11T02:22:42Z |
| publishDate | 2023-06-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-9e6688a4eab744adbc75e388b66890ad2023-11-18T10:44:05ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672023-06-012412978810.3390/ijms24129788Cm-p5 Peptide Dimers Inhibit Biofilms of <i>Candida albicans</i> Clinical Isolates, <i>C. parapsilosis</i> and Fluconazole-Resistant Mutants of <i>C. auris</i>Valerie Amann0Ann-Kathrin Kissmann1Vanessa Mildenberger2Imke Krebs3Julio A. Perez-Erviti4Ernesto M. Martell-Huguet5Anselmo J. Otero-Gonzalez6Fidel Morales-Vicente7Gina P. Rodríguez-Castaño8Carolina Firacative9Armando Rodríguez10Ludger Ständker11Tanja Weil12Barbara Spellerberg13Steffen Stenger14Frank Rosenau15Institute of Pharmaceutical Biotechnology, Ulm University, Albert-Einstein-Allee 11, 89081 Ulm, GermanyInstitute of Pharmaceutical Biotechnology, Ulm University, Albert-Einstein-Allee 11, 89081 Ulm, GermanyInstitute of Pharmaceutical Biotechnology, Ulm University, Albert-Einstein-Allee 11, 89081 Ulm, GermanyInstitute of Pharmaceutical Biotechnology, Ulm University, Albert-Einstein-Allee 11, 89081 Ulm, GermanyCenter for Protein Studies, Faculty of Biology, University of Havana, 25 Str. and I Str., La Habana 10400, CubaCenter for Protein Studies, Faculty of Biology, University of Havana, 25 Str. and I Str., La Habana 10400, CubaCenter for Protein Studies, Faculty of Biology, University of Havana, 25 Str. and I Str., La Habana 10400, CubaSynthetic Peptides Group, Center for Genetic Engineering and Biotechnology, La Habana 10600, CubaVidarium Nutrition, Health and Wellness Research Center, Grupo Nutresa, Calle 8 sur #50-67, Medellín 050023, ColombiaStudies in Translational Microbiology and Emerging Diseases (MICROS) Research Group, School of Medicine and Health Sciences, Universidad de Rosario, Bogota 111221, ColombiaCore Facility for Functional Peptidomics, Ulm Peptide Pharmaceuticals (U-PEP), Faculty of Medicine, Ulm University, 89081 Ulm, GermanyCore Facility for Functional Peptidomics, Ulm Peptide Pharmaceuticals (U-PEP), Faculty of Medicine, Ulm University, 89081 Ulm, GermanyMax Planck Institute for Polymer Research Mainz, Ackermannweg 10, 55128 Mainz, GermanyInstitute for Medical Microbiology and Hygiene, University Hospital Ulm, 89081 Ulm, GermanyInstitute for Medical Microbiology and Hygiene, University Hospital Ulm, 89081 Ulm, GermanyInstitute of Pharmaceutical Biotechnology, Ulm University, Albert-Einstein-Allee 11, 89081 Ulm, GermanyAntimicrobial 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 <i>Candida auris</i> biofilms. Here we show that these derivatives are also dose-dependently effective against de novo biofilms that are formed by the widespread pathogenic yeasts <i>C. albicans</i> and <i>C. parapsilosis</i>. Moreover, the activity of the peptides was demonstrated even against two fluconazole-resistant strains of <i>C. auris</i>.https://www.mdpi.com/1422-0067/24/12/9788antimicrobial peptidesbiofilm inhibition<i>Candida</i> speciesclinical isolatesresistances |
| spellingShingle | Valerie Amann Ann-Kathrin Kissmann Vanessa Mildenberger Imke Krebs Julio A. Perez-Erviti Ernesto M. Martell-Huguet Anselmo J. Otero-Gonzalez Fidel Morales-Vicente Gina P. Rodríguez-Castaño Carolina Firacative Armando Rodríguez Ludger Ständker Tanja Weil Barbara Spellerberg Steffen Stenger Frank Rosenau Cm-p5 Peptide Dimers Inhibit Biofilms of <i>Candida albicans</i> Clinical Isolates, <i>C. parapsilosis</i> and Fluconazole-Resistant Mutants of <i>C. auris</i> International Journal of Molecular Sciences antimicrobial peptides biofilm inhibition <i>Candida</i> species clinical isolates resistances |
| title | Cm-p5 Peptide Dimers Inhibit Biofilms of <i>Candida albicans</i> Clinical Isolates, <i>C. parapsilosis</i> and Fluconazole-Resistant Mutants of <i>C. auris</i> |
| title_full | Cm-p5 Peptide Dimers Inhibit Biofilms of <i>Candida albicans</i> Clinical Isolates, <i>C. parapsilosis</i> and Fluconazole-Resistant Mutants of <i>C. auris</i> |
| title_fullStr | Cm-p5 Peptide Dimers Inhibit Biofilms of <i>Candida albicans</i> Clinical Isolates, <i>C. parapsilosis</i> and Fluconazole-Resistant Mutants of <i>C. auris</i> |
| title_full_unstemmed | Cm-p5 Peptide Dimers Inhibit Biofilms of <i>Candida albicans</i> Clinical Isolates, <i>C. parapsilosis</i> and Fluconazole-Resistant Mutants of <i>C. auris</i> |
| title_short | Cm-p5 Peptide Dimers Inhibit Biofilms of <i>Candida albicans</i> Clinical Isolates, <i>C. parapsilosis</i> and Fluconazole-Resistant Mutants of <i>C. auris</i> |
| title_sort | cm p5 peptide dimers inhibit biofilms of i candida albicans i clinical isolates i c parapsilosis i and fluconazole resistant mutants of i c auris i |
| topic | antimicrobial peptides biofilm inhibition <i>Candida</i> species clinical isolates resistances |
| url | https://www.mdpi.com/1422-0067/24/12/9788 |
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