ArticleNature communications2024
A structural rationale for reversible vs irreversible amyloid fibril formation from a single protein.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Cofactor-Free Tau Filaments Are Dynamic and Undergo Structural Evolution Driven by Thermodynamic Control.Journal of the American Chemical Society · 2026Article
- The impact of physiological oxidants on triggering amyloid formation of the cell cycle regulator protein p16Protein science : a publication of the Protein Society · 2026Article
- From Disordered to Ordered: Nanoscale Spectroscopy Reveals Structural Evolution of Amyloid Beta 40 Fibrils.Chemphyschem : a European journal of chemical physics and physical chemistry · 2026Article
- Competition Between Liquid-Liquid Crystalline Phase Separation (LLCPS) and Liquid-Liquid Phase Separation (LLPS) in Amyloid Fibril Colloidal Systems.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Piperlonguminine inhibits hen egg white lysozyme amyloid fibril formation and mitigates amyloid fibril-induced hepatocellular damage.Current research in food science · 2026Article
- Photo-reversible amyloid nanoNETs for regenerative antimicrobial therapies.Nature communications · 2025Article
- Impurities in amyloid studies: The power of automated model building within a cautionary tale for structural biologists.Protein science : a publication of the Protein Society · 2025Article
- Intrinsically Disordered Protein Coating for Oral Delivery of Peptide Drugs.bioRxiv : the preprint server for biology · 2025Article
- Endogenous Aβ and Exogenous Wheat Gluten Nanostructures: Understanding Peptide Self-Assembly in Disease.ACS nano · 2025Review
- Amyloid Forming Human Lysozyme Intermediates are Stabilized by Non-Native Amide-π Interactions.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Calcium-Dependent S100A8 Amyloid Fibril Formation via S100A1-Mediated Transient Interaction.ACS chemical neuroscience · 2025Article
- Cold plasma-induced ovalbumin amyloid fibrils: Morphological characteristics and stability on astaxanthin-loaded high internal phase emulsions.Food chemistry: X · 2025Article
- Functional Biomaterials Derived from Protein Liquid-Liquid Phase Separation and Liquid-to-Solid Transition.Advanced materials (Deerfield Beach, Fla.) · 2025Review
- The evolving role of solid state nuclear magnetic resonance methods in studies of amyloid fibrils.Current opinion in structural biology · 2025Review
- On the reversibility of amyloid fibril formation.Biophysics reviews · 2025Review
- Beyond Misfolding: A New Paradigm for the Relationship Between Protein Folding and Aggregation.International journal of molecular sciences · 2024Review
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Authors and funding
14 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Reversible and irreversible amyloids are two diverging cases of protein (mis)folding associated with the cross-β motif in the protein folding and aggregation energy landscape. Yet, the molecular origins responsible for the formation of reversible vs irreversible amyloids have remained unknown. Here we provide evidence at the atomic level of distinct folding motifs for irreversible and reversible amyloids derived from a single protein sequence: human lysozyme. We compare the 2.8 Å structure of irreversible amyloid fibrils determined by cryo-electron microscopy helical reconstructions with molecular insights gained by solid-state NMR spectroscopy on reversible amyloids. We observe a canonical cross-β-sheet structure in irreversible amyloids, whereas in reversible amyloids, there is a less-ordered coexistence of β-sheet and helical secondary structures that originate from a partially unfolded lysozyme, thus carrying a "memory" of the original folded protein precursor. We also report the structure of hen egg-white lysozyme irreversible amyloids at 3.2 Å resolution, revealing another canonical amyloid fold, and reaffirming that irreversible amyloids undergo a complete conversion of the native protein into the cross-β structure. By combining atomic force microscopy, cryo-electron microscopy and solid-state NMR, we show that a full unfolding of the native protein precursor is a requirement for establishing irreversible amyloid fibrils.
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