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: | , , , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2022-02-01
|
| Series: | Molecules |
| Subjects: | |
| Online Access: | https://www.mdpi.com/1420-3049/27/4/1438 |
| _version_ | 1797477568934313984 |
|---|---|
| author | Edward Jianyang Lim Eunice Goh Tze Leng Nhan Dai Thien Tram Mercy Halleluyah Periayah Pui Lai Rachel Ee Timothy Mark Sebastian Barkham Zhi Sheng Poh Navin Kumar Verma Rajamani Lakshminarayanan |
| author_facet | Edward Jianyang Lim Eunice Goh Tze Leng Nhan Dai Thien Tram Mercy Halleluyah Periayah Pui Lai Rachel Ee Timothy Mark Sebastian Barkham Zhi Sheng Poh Navin Kumar Verma Rajamani Lakshminarayanan |
| author_sort | Edward Jianyang Lim |
| collection | DOAJ |
| 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 <i>Candida albicans</i>, <i>Candida parapsilosis</i>, <i>Candida tropicalis</i>, and <i>Candida glabrata</i>. 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 | 2024-03-09T21:19:34Z |
| format | Article |
| id | doaj.art-2e1805d276e84349a0919f1f10dfebd8 |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-03-09T21:19:34Z |
| publishDate | 2022-02-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj.art-2e1805d276e84349a0919f1f10dfebd82023-11-23T21:24:01ZengMDPI AGMolecules1420-30492022-02-01274143810.3390/molecules27041438Rationalisation of Antifungal Properties of α-Helical Pore-Forming Peptide, Mastoparan BEdward Jianyang Lim0Eunice Goh Tze Leng1Nhan Dai Thien Tram2Mercy Halleluyah Periayah3Pui Lai Rachel Ee4Timothy Mark Sebastian Barkham5Zhi Sheng Poh6Navin Kumar Verma7Rajamani Lakshminarayanan8Ocular Infections and Anti-Microbials Research Group, Singapore Eye Research Institute, The Academia, 20 College Road, Discovery Tower, Singapore 169856, SingaporeOcular Infections and Anti-Microbials Research Group, Singapore Eye Research Institute, The Academia, 20 College Road, Discovery Tower, Singapore 169856, SingaporeDepartment of Pharmacy, National University of Singapore, 18 Science Drive 4, Singapore 117543, SingaporeOcular Infections and Anti-Microbials Research Group, Singapore Eye Research Institute, The Academia, 20 College Road, Discovery Tower, Singapore 169856, SingaporeDepartment of Pharmacy, National University of Singapore, 18 Science Drive 4, Singapore 117543, SingaporeDepartment of Laboratory Medicine, Tan Tock Seng Hospital, 11 Jalan Tan Tock Seng, Singapore 308433, SingaporeLee Kong Chian School of Medicine, Nanyang Technological University Singapore, Clinical Sciences Building, 11 Mandalay Road, Singapore 308232, SingaporeOcular Infections and Anti-Microbials Research Group, Singapore Eye Research Institute, The Academia, 20 College Road, Discovery Tower, Singapore 169856, SingaporeOcular Infections and Anti-Microbials Research Group, Singapore Eye Research Institute, The Academia, 20 College Road, Discovery Tower, Singapore 169856, SingaporeThe 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 <i>Candida albicans</i>, <i>Candida parapsilosis</i>, <i>Candida tropicalis</i>, and <i>Candida glabrata</i>. 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.https://www.mdpi.com/1420-3049/27/4/1438antifungal peptidesdrug resistanceinvasive fungal infectionsnon-albicans <i>Candida</i>skin wounds |
| spellingShingle | Edward Jianyang Lim Eunice Goh Tze Leng Nhan Dai Thien Tram Mercy Halleluyah Periayah Pui Lai Rachel Ee Timothy Mark Sebastian Barkham Zhi Sheng Poh Navin Kumar Verma Rajamani Lakshminarayanan Rationalisation of Antifungal Properties of α-Helical Pore-Forming Peptide, Mastoparan B Molecules antifungal peptides drug resistance invasive fungal infections non-albicans <i>Candida</i> skin wounds |
| 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 | antifungal peptides drug resistance invasive fungal infections non-albicans <i>Candida</i> skin wounds |
| url | https://www.mdpi.com/1420-3049/27/4/1438 |
| work_keys_str_mv | AT edwardjianyanglim rationalisationofantifungalpropertiesofahelicalporeformingpeptidemastoparanb AT eunicegohtzeleng rationalisationofantifungalpropertiesofahelicalporeformingpeptidemastoparanb AT nhandaithientram rationalisationofantifungalpropertiesofahelicalporeformingpeptidemastoparanb AT mercyhalleluyahperiayah rationalisationofantifungalpropertiesofahelicalporeformingpeptidemastoparanb AT puilairachelee rationalisationofantifungalpropertiesofahelicalporeformingpeptidemastoparanb AT timothymarksebastianbarkham rationalisationofantifungalpropertiesofahelicalporeformingpeptidemastoparanb AT zhishengpoh rationalisationofantifungalpropertiesofahelicalporeformingpeptidemastoparanb AT navinkumarverma rationalisationofantifungalpropertiesofahelicalporeformingpeptidemastoparanb AT rajamanilakshminarayanan rationalisationofantifungalpropertiesofahelicalporeformingpeptidemastoparanb |