ArticleProceedings of the National Academy of Sciences of the United States of America2021
Amyloid β 42 fibril structure based on small-angle scattering.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 45 citations in OpenAlex.
- Structural defects in amyloid-β fibrils drive secondary nucleation.Nature communications · 2026Article
- The Importance of Being Imperfect: Structure and Function of Bacterial Amyloid.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Review
- Aducanumab binding to AβProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Rare Earth Element-Induced Condensation of the Block V of the Repeats-in-Toxin Domain from CyaA fromLangmuir : the ACS journal of surfaces and colloids · 2025Article
- Biomimetic supramolecular protein matrix restores structure and properties of human dental enamel.Nature communications · 2025Article
- Aducanumab Binding to AβbioRxiv : the preprint server for biology · 2025Article
- Inducers and modulators of protein aggregation in Alzheimer's disease - Critical tools for understanding the foundations of aggregate structures.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2025Review
- Insights into the Hierarchical Assembly of a Chemically Diverse Peptide Hydrogel Derived from Human Semenogelin I.ACS nano · 2024Article
- IntegratingJournal of the American Chemical Society · 2024Article
- The role of shear forces in primary and secondary nucleation of amyloid fibrils.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Structural characterization of E22G AβPhysical chemistry chemical physics : PCCP · 2024Article
- Resolving the Nanoscale Structure of β-Sheet Peptide Self-Assemblies Using Single-Molecule Orientation-Localization Microscopy.ACS nano · 2024Article
- Synthetic β-sheets mimicking fibrillar and oligomeric structures for evaluation of spectral X-ray scattering technique for biomarker quantification.Cell & bioscience · 2024Article
- Self-replication of AProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Identification of potential aggregation hotspots on Aβ42 fibrils blocked by the anti-amyloid chaperone-like BRICHOS domain.Nature communications · 2024Article
- Ganglioside Micelles Affect Amyloid β Aggregation by Coassembly.ACS chemical neuroscience · 2023Article
- The residual structure of acid-denatured βProtein science : a publication of the Protein Society · 2023Article
- Co-administration of Nanowired DL-3-n-Butylphthalide (DL-NBP) Together with Mesenchymal Stem Cells, Monoclonal Antibodies to Alpha Synuclein and TDP-43 (TAR DNA-Binding Protein 43) Enhance Superior Neuroprotection in Parkinson's Disease Following Concussive Head Injury.Advances in neurobiology · 2023Review
- Measuring the Radius of Gyration and Intrinsic Flexibility of Viral Proteins in Buffer Solution Using Small-Angle X-ray Scattering.ACS measurement science au · 2022Article
- Role of Hydrophobicity at the N-Terminal Region of Aβ42 in Secondary Nucleation.ACS chemical neuroscience · 2022Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amyloid fibrils are associated with a number of neurodegenerative diseases, including fibrils of amyloid β42 peptide (Aβ42) in Alzheimer's disease. These fibrils are a source of toxicity to neuronal cells through surface-catalyzed generation of toxic oligomers. Detailed knowledge of the fibril structure may thus facilitate therapeutic development. We use small-angle scattering to provide information on the fibril cross-section dimension and shape for Aβ42 fibrils prepared in aqueous phosphate buffer at pH = 7.4 and pH 8.0 under quiescent conditions at 37 °C from pure recombinant Aβ42 peptide. Fitting the data using a continuum model reveals an elliptical cross-section and a peptide mass-per-unit length compatible with two filaments of two monomers, four monomers per plane. To provide a more detailed atomistic model, the data were fitted using as a starting state a high-resolution structure of the two-monomer arrangement in filaments from solid-state NMR (Protein Data Bank ID 5kk3). First, a twofold symmetric model including residues 11 to 42 of two monomers in the filament was optimized in terms of twist angle and local packing using Rosetta. A two-filament model was then built and optimized through fitting to the scattering data allowing the two N-termini in each filament to take different conformations, with the same conformation in each of the two filaments. This provides an atomistic model of the fibril with twofold rotation symmetry around the fibril axis. Intriguingly, no polydispersity as regards the number of filaments was observed in our system over separate samples, suggesting that the two-filament arrangement represents a free energy minimum for the Aβ42 fibril.
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