Rationalisation of Antifungal Properties of α-Helical Pore-Forming Peptide, Mastoparan B

• Published in: Molecules (Basel, Switzerland) Switzerland), 2022-02, Vol.27 (4), p.1438
• Main Authors: Lim, Edward Jianyang, Leng, Eunice Goh Tze, Tram, Nhan Dai Thien, Periayah, Mercy Halleluyah, Ee, Pui Lai Rachel, Barkham, Timothy Mark Sebastian, Poh, Zhi Sheng, Verma, Navin Kumar, Lakshminarayanan, Rajamani
• Format: Article
• Language: English
• Subjects: Antibiotics; Antifungal activity; Antifungal Agents - chemistry; Antifungal Agents - pharmacology; antifungal peptides; Antiinfectives and antibacterials; Antimicrobial agents; Antimicrobial Cationic Peptides - chemistry; Antimicrobial Cationic Peptides - pharmacology; Antimicrobial peptides; Biocompatibility; Cecropin; Cell Line; Cell Line, Tumor; Cell Survival - drug effects; Chemical Phenomena; Drug development; drug resistance; Fibroblasts; Fungicides; Humans; Infections; Intercellular Signaling Peptides and Proteins - chemistry; Intercellular Signaling Peptides and Proteins - pharmacology; invasive fungal infections; Invertebrates; Magainin 2; Mastoparan; Microbial Sensitivity Tests; Microorganisms; Models, Molecular; non-albicans Candida; Pathogens; Peptides; Phylogeny; Pore formation; Protein Conformation; skin wounds; Spectrum Analysis; Structure-Activity Relationship; Vertebrates
• ISSN: 1420-3049; 1420-3049
• DOI: 10.3390/molecules27041438

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 , , , and . 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.