ArticleNaunyn-Schmiedeberg's archives of pharmacology2005
The Penicillium chrysogenum-derived antifungal peptide shows no toxic effects on mammalian cells in the intended therapeutic concentration.
Article in Naunyn-Schmiedeberg's archives of pharmacology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
24 citing papers in PubMed, 45 citations in OpenAlex.
- 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
- A superfamily of bioactive proteins from fungi - are these secondary metabolites?Fungal biology and biotechnology · 2026Article
- Engineering Penicillium expansum antifungal proteins unveils new clues about their mode of action.Applied microbiology and biotechnology · 2026Article
- The role of Npt1 in regulating antifungal protein activity in filamentous fungi.Nature communications · 2025Article
- Small Disulfide Proteins with Antifungal Impact: NMR Experimental Structures as Compared to Models of Alphafold Versions.International journal of molecular sciences · 2025Article
- Navigating the fungal battlefield: cysteine-rich antifungal proteins and peptides from Eurotiales.Frontiers in fungal biology · 2024Review
- Novel findings about the mode of action of the antifungal protein PeAfpA against Saccharomyces cerevisiae.Applied microbiology and biotechnology · 2023Article
- Development of a FungalBraid Penicillium expansum-based expression system for the production of antifungal proteins in fungal biofactories.Microbial biotechnology · 2022Article
- Potential of Antifungal Proteins (AFPs) to ControlJournal of fungi (Basel, Switzerland) · 2021Article
- Two small, cysteine-rich and cationic antifungal proteins from Penicillium chrysogenum: A comparative study of PAF and PAFB.Biochimica et biophysica acta. Biomembranes · 2020Review
- Characterization of a fungal competition factor: Production of a conidial cell-wall associated antifungal peptide.PLoS pathogens · 2020Article
- Biofungicidal Potential ofFrontiers in microbiology · 2020Article
- Nutrient Excess Triggers the Expression of theMicroorganisms · 2019Article
- Cysteine-Rich Antifungal Proteins from Filamentous Fungi are Promising Bioactive Natural Compounds in Anti-Israel journal of chemistry · 2019Review
- Do Antimicrobial Proteins Contribute to Overcoming the Hidden Antifungal Crisis at the Dawn of a Post-Antibiotic Era?Microorganisms · 2019Article
- New Antimicrobial Potential and Structural Properties of PAFB: A Cationic, Cysteine-Rich Protein from Penicillium chrysogenum Q176.Scientific reports · 2018Article
- Calcium binding of the antifungal protein PAF: Structure, dynamics and function aspects by NMR and MD simulations.PloS one · 2018Article
- Three Antifungal Proteins FromFrontiers in microbiology · 2018Article
- Article
- A Penicillium chrysogenum-based expression system for the production of small, cysteine-rich antifungal proteins for structural and functional analyses.Microbial cell factories · 2016Article
Corrections and comments
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Authors and funding
13 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Certain filamentous fungi, such as the penicillin-producing strain Penicillium chrysogenum, secrete small, highly basic and cysteine-rich proteins with antifungal effects. Affected fungi include a number of important zoopathogens, including those infecting humans. Recent studies, however, have pointed to a membrane-perturbing effect of these antifungal compounds, apparent as a potassium efflux from affected fungal cells. If present on mammalian cells, this would severely hinder the potential therapeutic use of these molecules. Here we studied the effects of the P. chrysogenum-derived antifungal peptide (PAF) on a number of mammalian cells to establish whether the protein has any cytotoxic effects, alters transmembrane currents on excitable cells or activates the immune system. PAF, in a concentration range of 2-100 mug/ml, did not cause any cytotoxicity on human endothelial cells from the umbilical vein. Applied at 10 mug/ml, it also failed to modify voltage-gated potassium channels of neurones, skeletal muscle fibers, and astrocytes. PAF also left the hyperpolarization-activated non-specific cationic current (I(h)) and the L-type calcium current unaffected. Finally, up to 2 mug/ml, PAF did not induce the production of pro-inflammatory cytokines such as IL-6, IL-8, and TNF-alpha. These results suggest that PAF should have only minor, if any, effects on mammalian cells in the intended therapeutic concentration range.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.