ArticleJournal of advanced research2025
Optimizing therapeutic efficacy of antifungal peptides via strategic terminal amino acid modification.
Article in Journal of advanced research, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- WHO Critical Priority Fungi: A Comprehensive Review of Antifungal Resistance, Emerging Therapeutic Strategies, and the Potential of Antifungal Peptides.International journal of molecular sciences · 2026Review
- Boronic acid derivatives inhibit Candida albicans growth by compromising energy metabolism.Journal of advanced research · 2026Article
- Antifungal activity of the antimicrobial peptide RP557 against priority fungal pathogens.Microbiology (Reading, England) · 2026Article
- Self-assembled nanonetworks of highly stable gemini surfactant-like peptides: antibacterial mechanisms, self-assembly characteristics, and in vivo anti-infection potential.Journal of nanobiotechnology · 2026Article
- Next-generation antifungal peptide discovery: the synergy of artificial intelligence and omics technologies.World journal of microbiology & biotechnology · 2025Review
- The rise of ultrashort cationic β-peptides as promising antimicrobial therapeutics.RSC medicinal chemistry · 2025Review
- Novel Strategies for Preventing Fungal Infections-Outline.Pathogens (Basel, Switzerland) · 2025Review
- A cell wall-targeting urease-derived peptide as a potential antifungal agent againstCurrent research in microbial sciences · 2025Article
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
introductionAntifungal peptides (AFPs) have the potential to treat antifungal-resistant infections; however, their structure-function relationship remains unknown, hindering their rapid development. Therefore, it is imperative to investigate and clarify the structure-function relationships of AFPs.
objectivesThis study aimed to investigate the impact of end-tagging single hydrophobic amino acids and capping the N-terminus with glycine (Gly) on the antifungal activity of peptide W4.
methodsThe antifungal efficacy of the engineered peptides was initially assessed by determining the minimum inhibitory concentration (MIC) /minimal fungicidal concentration (MFC), killing kinetics, and drug resistance induction, in addition to evaluating the biocompatibility and stability. Subsequently, the antifungal mechanism was investigated using fluorescence labeling, electron microscopy, reactive oxygen species (ROS) detection, and measurement of mitochondrial membrane potential and apoptosis. The impact of the engineered peptides on Candida albicans (C. albicans) biofilm and their potential application in the scratch keratomycosis model were investigated.
resultsThe antifungal activity of W4 was significantly enhanced by capping Gly at the N-terminus, resulting in a decrease in average activity from 11.86 μM to 6.25 μM (GW4) and an increase in TI values by 1.9-fold (TI
conclusionCapping Gly at the N-terminus increased residue length while significantly enhancing the helical propensity of W4, thereby augmenting its antifungal activity. Our exploratory study demonstrated the potential strategies and avenues for optimizing the structure-function relationships of AFPs and developing highly effective antifungal drugs.
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