ArticleScience advances2025
Amyloid-β oligomers, curvilinear and annular assemblies, imaged by cryo-ET, cryo-EM, and AFM.
Article in Science advances, 2025. 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.
- Assembling peptides for treating Alzheimer's disease: a supramolecular perspective.RSC advances · 2026Review
- Targeting soluble misfolded oligomers in anti-amyloid research.Nature reviews. Chemistry · 2026Review
- Adhesion Mechanisms of Amyloid-Like Oligomer Monolayers Enabling Stable Surface Modification for Inert Polymers.JACS Au · 2026Article
- Apolipoprotein D acts as a chaperone of Aβ peptide delaying its assembly into amyloid aggregates.Cellular and molecular life sciences : CMLS · 2026Article
- CryAB-driven amyloidogenesis iniScience · 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
- Amyloid β 1-42 Can Form Ion Channels as Small as Gramicidin in Model Lipid Membranes.Membranes · 2025Article
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Authors and funding
11 authors.
Funding
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Abstract
Prefibrillar structures of the amyloid-β (Aβ) peptide are central to cytotoxicity in Alzheimer's disease. Time-resolved imaging of oligomers has enabled quantification of their extension. A snapshot of these prefibrillar assemblies has been characterized using a combination of cryo-electron tomography (cryo-ET), cryo-electron microscopy (cryo-EM) single-particle analysis, and atomic force microscopy (AFM). A highly consistent diameter for all curvilinear protofibrils and oligomers of 2.8 nanometers suggests that these assemblies are structural extensions from the smaller oligomers. In situ AFM confirms that spherical oligomers template and extend over time into curvilinear protofibrils. Furthermore, their basic cross section suggests that amyloid fibrils might be initiated by the lateral binding of two curvilinear protofibrils. Cryo-ET/EM single particles also reveal ring-shaped annular assemblies. These have a central internal channel, ~1.4 nanometers in diameter, which is capable of traversing lipid membranes. Large conductance recorded using patch-clamp electrophysiology matches the internal diameter of the Aβ annular architecture.
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