Human Antimicrobial Peptide Hepcidin 25-Induced Apoptosis in <i>Candida albicans</i>
Hepcidin 25 (hep 25) is a cysteine-rich 25-amino acid antimicrobial peptide containing the amino-terminal Cu(II)/Ni(II)-binding (ATCUN) motif. Upon metal binding, the ATCUN motif is known to be involved in the generation of reactive oxygen species (ROS), especially hydrogen peroxide and hydroxyl rad...
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MDPI AG
2020-04-01
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| Series: | Microorganisms |
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| Online Access: | https://www.mdpi.com/2076-2607/8/4/585 |
| _version_ | 1797570341083545600 |
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| author | Ruei-Ching Chen Chung-Yu Lan |
| author_facet | Ruei-Ching Chen Chung-Yu Lan |
| author_sort | Ruei-Ching Chen |
| collection | DOAJ |
| description | Hepcidin 25 (hep 25) is a cysteine-rich 25-amino acid antimicrobial peptide containing the amino-terminal Cu(II)/Ni(II)-binding (ATCUN) motif. Upon metal binding, the ATCUN motif is known to be involved in the generation of reactive oxygen species (ROS), especially hydrogen peroxide and hydroxyl radicals, which act against different bacterial species. However, the antifungal activity and its correlation to the Cu(II)-ATCUN complex of Hep 25 are still poorly understood. Here, we found that ROS accumulation plays an important role in the fungicidal activity of hep 25 against <i>Candida albicans</i>. In addition, Annexin V-FITC staining and TUNEL assay results provide clues about the apoptosis induced by hep 25. Moreover, hep 25 also increases the generation of ROS, possibly because of copper binding to the ATCUN motif, which is relevant to its activity against <i>C. albicans</i>. Finally, the <i>C. albicans</i> killing action of hep 25 is an energy- and temperature-dependent process that does not involve targeting the membrane. Taken together, our results provide new insights into the mechanisms of hep 25 against <i>C. albicans</i> cells and the potential use of hep 25 and its derivatives as novel antifungal agents. |
| first_indexed | 2024-03-10T20:23:35Z |
| format | Article |
| id | doaj.art-c8fd6e16749d42fa99dd832b2e66db97 |
| institution | Directory Open Access Journal |
| issn | 2076-2607 |
| language | English |
| last_indexed | 2024-03-10T20:23:35Z |
| publishDate | 2020-04-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Microorganisms |
| spelling | doaj.art-c8fd6e16749d42fa99dd832b2e66db972023-11-19T21:59:28ZengMDPI AGMicroorganisms2076-26072020-04-018458510.3390/microorganisms8040585Human Antimicrobial Peptide Hepcidin 25-Induced Apoptosis in <i>Candida albicans</i>Ruei-Ching Chen0Chung-Yu Lan1Institute of Molecular and Cellular Biology, National Tsing Hua University, Hsinchu 30013, TaiwanDepartment of Life Science, National Tsing Hua University, Hsinchu 30013, TaiwanHepcidin 25 (hep 25) is a cysteine-rich 25-amino acid antimicrobial peptide containing the amino-terminal Cu(II)/Ni(II)-binding (ATCUN) motif. Upon metal binding, the ATCUN motif is known to be involved in the generation of reactive oxygen species (ROS), especially hydrogen peroxide and hydroxyl radicals, which act against different bacterial species. However, the antifungal activity and its correlation to the Cu(II)-ATCUN complex of Hep 25 are still poorly understood. Here, we found that ROS accumulation plays an important role in the fungicidal activity of hep 25 against <i>Candida albicans</i>. In addition, Annexin V-FITC staining and TUNEL assay results provide clues about the apoptosis induced by hep 25. Moreover, hep 25 also increases the generation of ROS, possibly because of copper binding to the ATCUN motif, which is relevant to its activity against <i>C. albicans</i>. Finally, the <i>C. albicans</i> killing action of hep 25 is an energy- and temperature-dependent process that does not involve targeting the membrane. Taken together, our results provide new insights into the mechanisms of hep 25 against <i>C. albicans</i> cells and the potential use of hep 25 and its derivatives as novel antifungal agents.https://www.mdpi.com/2076-2607/8/4/585<i>C. albicans</i>antimicrobial peptidehepcidin-25apoptosis |
| spellingShingle | Ruei-Ching Chen Chung-Yu Lan Human Antimicrobial Peptide Hepcidin 25-Induced Apoptosis in <i>Candida albicans</i> Microorganisms <i>C. albicans</i> antimicrobial peptide hepcidin-25 apoptosis |
| title | Human Antimicrobial Peptide Hepcidin 25-Induced Apoptosis in <i>Candida albicans</i> |
| title_full | Human Antimicrobial Peptide Hepcidin 25-Induced Apoptosis in <i>Candida albicans</i> |
| title_fullStr | Human Antimicrobial Peptide Hepcidin 25-Induced Apoptosis in <i>Candida albicans</i> |
| title_full_unstemmed | Human Antimicrobial Peptide Hepcidin 25-Induced Apoptosis in <i>Candida albicans</i> |
| title_short | Human Antimicrobial Peptide Hepcidin 25-Induced Apoptosis in <i>Candida albicans</i> |
| title_sort | human antimicrobial peptide hepcidin 25 induced apoptosis in i candida albicans i |
| topic | <i>C. albicans</i> antimicrobial peptide hepcidin-25 apoptosis |
| url | https://www.mdpi.com/2076-2607/8/4/585 |
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