ArticleScience advances2020
Complete aggregation pathway of amyloid β (1-40) and (1-42) resolved on an atomically clean interface.
Article in Science advances, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.
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Who cites it
69 citing papers in PubMed.
- Targeting soluble misfolded oligomers in anti-amyloid research.Nature reviews. Chemistry · 2026Review
- Antiamyloid Antibody Effects on Aβ-42 Protein Aggregates Profiled Using Nanospectroscopy.Chemical & biomedical imaging · 2026Article
- Analysis of Single Particles of Amyloid Beta and α-Synuclein With Seeded Amplification for the Diagnosis of Alzheimer's and Parkinson's Disease.Biotechnology and applied biochemistry · 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
- YIAD-0501 directly dissociates aggregates of full-length and N-terminal pyroglutamate-modified forms of Aβ.Alzheimer's research & therapy · 2026Article
- Novel Small-Molecule Analogues of IU1 Ameliorate Amyloid-β Mediated Toxicity in Alzheimer's Disease Cell and Worm Models.International journal of molecular sciences · 2026Article
- Differentiating Alzheimer's Aβ Isoforms Coaggregated in Cerebrospinal Fluid via Single-Particle Imaging.ACS chemical neuroscience · 2026Article
- A Ru(ii)-arene complex with promising anti-Aβ activity.RSC advances · 2026Article
- Influence of Alzheimer's associated Aβ oligomers and oxidative stress on blood-brain barrier dysfunction.Tissue barriers · 2026Article
- Amyloid β Peptide Modifies Membrane Architecture and Surface Electrostatic Properties of Human Red Blood Cells.International journal of molecular sciences · 2025Article
- Single-fibril Förster resonance energy transfer imaging and deep learning reveal concentration dependence of amyloid β 42 aggregation pathways.PNAS nexus · 2025Article
- Amyloid-β oligomers, curvilinear and annular assemblies, imaged by cryo-ET, cryo-EM, and AFM.Science advances · 2025Article
- In Vitro Assessment of Cholinesterase Inhibition and Neuroprotective Effects of Elaeocarpus angustifolius Blume Against Amyloid-Beta Peptide-Induced Toxicity in SH-SY5Y and BV-2 Cells.Neurochemical research · 2025Article
- Ultrasonic disruption of circulating amyloid β aggregates via phase-change peptide nanoemulsions.Biomaterials · 2025Article
- Spectral Heterogeneity of Thioflavin T Binding to Aβ42:Aβ40 Mixed Fibrils: Implications for Alzheimer's Disease Screening.ACS omega · 2025Article
- On Levodopa Interactions with Brain Disease Amyloidogenic Proteins at the Nanoscale.ACS omega · 2025Article
- Article
- Characterizing heterogeneity in amyloid formation processes.Current opinion in structural biology · 2024Review
- Accelerated Alzheimer's Aβ-42 secondary nucleation chronologically visualized on fibril surfaces.Science advances · 2024Article
- Current perspective on amyloid aggregation accelerating properties of the artificial butter flavoring, diacetyl.Neural regeneration research · 2024Article
9 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To visualize amyloid β (Aβ) aggregates requires an uncontaminated and artifact-free interface. This paper demonstrates the interface between graphene and pure water (verified to be atomically clean using tunneling microscopy) as an ideal platform for resolving size, shape, and morphology (measured by atomic force microscopy) of Aβ-40 and Aβ-42 peptide assemblies from 0.5 to 150 hours at a 5-hour time interval with single-particle resolution. After confirming faster aggregation of Aβ-42 in comparison to Aβ-40, a stable set of oligomers with a diameter distribution of ~7 to 9 nm was prevalently observed uniquely for Aβ-42 even after fibril appearance. The interaction energies between a distinct class of amyloid aggregates (dodecamers) and graphene was then quantified using molecular dynamics simulations. Last, differences in Aβ-40 and Aβ-42 networks were resolved, wherein only Aβ-42 fibrils were aligned through lateral interactions over micrometer-scale lengths, a property that could be exploited in the design of biofunctional materials.
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