Rationalisation of antifungal properties of α-helical pore-forming peptide, mastoparan B
The high mortality associated with invasive fungal infections, narrow spectrum of available antifungals, and increasing evolution of antifungal resistance necessitate the development of alternative therapies. Host defense peptides are regarded as the first line of defense against microbial invasion...
| Main Authors: | , , , , , , , , |
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| Format: | Journal Article |
| Language: | English |
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2022
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| Online Access: | https://hdl.handle.net/10356/160143 |
| _version_ | 1824456144753524736 |
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| author | Lim, Edward Jianyang Goh, Eunice Tze Leng Tram, Nhan Dai Thien Periayah, Mercy Halleluyah Ee, Rachel Pui Lai Barkham, Timothy Mark Sebastian Poh, Zhi Sheng Verma, Navin Kumar Lakshminarayanan, Rajamani |
| author2 | Lee Kong Chian School of Medicine (LKCMedicine) |
| author_facet | Lee Kong Chian School of Medicine (LKCMedicine) Lim, Edward Jianyang Goh, Eunice Tze Leng Tram, Nhan Dai Thien Periayah, Mercy Halleluyah Ee, Rachel Pui Lai Barkham, Timothy Mark Sebastian Poh, Zhi Sheng Verma, Navin Kumar Lakshminarayanan, Rajamani |
| author_sort | Lim, Edward Jianyang |
| collection | NTU |
| description | The high mortality associated with invasive fungal infections, narrow spectrum of available antifungals, and increasing evolution of antifungal resistance necessitate the development of alternative therapies. Host defense peptides are regarded as the first line of defense against microbial invasion in both vertebrates and invertebrates. In this work, we investigated the effectiveness of four naturally occurring pore-forming antimicrobial peptides (melittin, magainin 2, cecropin A, and mastoparan B) against a panel of clinically relevant pathogens, including Candida albicans, Candida parapsilosis, Candida tropicalis, and Candida glabrata. We present data on the antifungal activities of the four pore-forming peptides, assessed with descriptive statistics, and their cytocompatibility with cultured human cells. Among the four peptides, mastoparan B (MB) displayed potent antifungal activity, whereas cecropin A was the least potent. We show that MB susceptibility of phylogenetically distant non-candida albicans can vary and be described by different intrinsic physicochemical parameters of pore-forming α-helical peptides. These findings have potential therapeutic implications for the design and development of safe antifungal peptide-based drugs. |
| first_indexed | 2025-02-19T03:49:26Z |
| format | Journal Article |
| id | ntu-10356/160143 |
| institution | Nanyang Technological University |
| language | English |
| last_indexed | 2025-02-19T03:49:26Z |
| publishDate | 2022 |
| record_format | dspace |
| spelling | ntu-10356/1601432023-03-05T16:52:27Z Rationalisation of antifungal properties of α-helical pore-forming peptide, mastoparan B Lim, Edward Jianyang Goh, Eunice Tze Leng Tram, Nhan Dai Thien Periayah, Mercy Halleluyah Ee, Rachel Pui Lai Barkham, Timothy Mark Sebastian Poh, Zhi Sheng Verma, Navin Kumar Lakshminarayanan, Rajamani Lee Kong Chian School of Medicine (LKCMedicine) Singapore Eye Research Institute National Skin Centre Science::Medicine Antifungal Peptides Drug Resistance The high mortality associated with invasive fungal infections, narrow spectrum of available antifungals, and increasing evolution of antifungal resistance necessitate the development of alternative therapies. Host defense peptides are regarded as the first line of defense against microbial invasion in both vertebrates and invertebrates. In this work, we investigated the effectiveness of four naturally occurring pore-forming antimicrobial peptides (melittin, magainin 2, cecropin A, and mastoparan B) against a panel of clinically relevant pathogens, including Candida albicans, Candida parapsilosis, Candida tropicalis, and Candida glabrata. We present data on the antifungal activities of the four pore-forming peptides, assessed with descriptive statistics, and their cytocompatibility with cultured human cells. Among the four peptides, mastoparan B (MB) displayed potent antifungal activity, whereas cecropin A was the least potent. We show that MB susceptibility of phylogenetically distant non-candida albicans can vary and be described by different intrinsic physicochemical parameters of pore-forming α-helical peptides. These findings have potential therapeutic implications for the design and development of safe antifungal peptide-based drugs. Agency for Science, Technology and Research (A*STAR) Ministry of Education (MOE) Ministry of Health (MOH) National Medical Research Council (NMRC) Published version This research was funded by the Singapore Ministry of Health’s National Medical Research Council (NMRC) under its Centre Grant Program—Optimization of Core Platform Technologies for Ocular Research (INCEPTOR)-NMRC/CG/M010/2017, Open Fund—Large Collaborative Grant (OFLCG18May-0028), the SingHealth Foundation (SHF/FG663P/2017) and the Agency for Science, Technology and Research (A*STAR) under its Wound Care Innovation for the Tropics (WCIT) Industry Alignment Fund Pre-Positioning (IAF-PP) grant (H17/01/a0/0K9). The work was also supported by the Singapore Ministry of Education (MOE) Academic Research Fund (AcRF) Tier 1 grants (2020-T1-001-062 and R-148-000-309-114). The APC was funded by R1875/3/2022. 2022-07-13T07:14:29Z 2022-07-13T07:14:29Z 2022 Journal Article Lim, E. J., Goh, E. T. L., Tram, N. D. T., Periayah, M. H., Ee, R. P. L., Barkham, T. M. S., Poh, Z. S., Verma, N. K. & Lakshminarayanan, R. (2022). Rationalisation of antifungal properties of α-helical pore-forming peptide, mastoparan B. Molecules, 27(4), 1438-. https://dx.doi.org/10.3390/molecules27041438 1420-3049 https://hdl.handle.net/10356/160143 10.3390/molecules27041438 35209228 2-s2.0-85125176765 4 27 1438 en NMRC/CG/M010/2017 OFLCG18May-0028 SHF/FG663P/2017 H17/01/a0/0K9 2020-T1-001-062 R-148-000-309-114 R1875/3/2022 Molecules © 2022 by the authors. 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/). application/pdf |
| spellingShingle | Science::Medicine Antifungal Peptides Drug Resistance Lim, Edward Jianyang Goh, Eunice Tze Leng Tram, Nhan Dai Thien Periayah, Mercy Halleluyah Ee, Rachel Pui Lai Barkham, Timothy Mark Sebastian Poh, Zhi Sheng Verma, Navin Kumar Lakshminarayanan, Rajamani Rationalisation of antifungal properties of α-helical pore-forming peptide, mastoparan B |
| title | Rationalisation of antifungal properties of α-helical pore-forming peptide, mastoparan B |
| title_full | Rationalisation of antifungal properties of α-helical pore-forming peptide, mastoparan B |
| title_fullStr | Rationalisation of antifungal properties of α-helical pore-forming peptide, mastoparan B |
| title_full_unstemmed | Rationalisation of antifungal properties of α-helical pore-forming peptide, mastoparan B |
| title_short | Rationalisation of antifungal properties of α-helical pore-forming peptide, mastoparan B |
| title_sort | rationalisation of antifungal properties of α helical pore forming peptide mastoparan b |
| topic | Science::Medicine Antifungal Peptides Drug Resistance |
| url | https://hdl.handle.net/10356/160143 |
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