ArticleNature communications2022
pH- and concentration-dependent supramolecular assembly of a fungal defensin plectasin variant into helical non-amyloid fibrils.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 16 citations in OpenAlex.
- A histidine switch controls the pH-responsive self-assembly of a helical protein filament.bioRxiv : the preprint server for biology · 2026Article
- Cylindracin, a Fruiting Body-Specific Protein ofToxins · 2025Article
- Self-Assembled Peptide Hydrogels PPI45 and PPI47: Novel Drug Candidates forGels (Basel, Switzerland) · 2025Article
- Non-destructive real-time monitoring and investigation of the self-assembly process using fluorescent probes.Chemical science · 2024Review
- Cysteine Redox Chemistry in Peptide Self-Assembly to Modulate Hydrogelation.Molecules (Basel, Switzerland) · 2023Article
- Amyloid-Based Albumin Hydrogels.Advanced healthcare materials · 2023Article
- Plectasin: from evolution to truncation, expression, and better druggability.Frontiers in microbiology · 2023Article
Corrections and comments
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Authors and funding
15 authors at 6 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Self-assembly and fibril formation play important roles in protein behaviour. Amyloid fibril formation is well-studied due to its role in neurodegenerative diseases and characterized by refolding of the protein into predominantly β-sheet form. However, much less is known about the assembly of proteins into other types of supramolecular structures. Using cryo-electron microscopy at a resolution of 1.97 Å, we show that a triple-mutant of the anti-microbial peptide plectasin, PPI42, assembles into helical non-amyloid fibrils. The in vitro anti-microbial activity was determined and shown to be enhanced compared to the wildtype. Plectasin contains a cysteine-stabilised α-helix-β-sheet structure, which remains intact upon fibril formation. Two protofilaments form a right-handed protein fibril. The fibril formation is reversible and follows sigmoidal kinetics with a pH- and concentration dependent equilibrium between soluble monomer and protein fibril. This high-resolution structure reveals that α/β proteins can natively assemble into fibrils.
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