ArticlePhysical chemistry chemical physics : PCCP2017
Imaging Aβ(1-42) fibril elongation reveals strongly polarised growth and growth incompetent states.
Article in Physical chemistry chemical physics : PCCP, 2017. 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.
- Single-fibril Förster resonance energy transfer imaging and deep learning reveal concentration dependence of amyloid β 42 aggregation pathways.PNAS nexus · 2025Article
- A single fibril study reveals that ApoE inhibits the elongation of Aβ42 fibrils in an isoform-dependent manner.Communications chemistry · 2025Article
- Competing addition processes give distinct growth regimes in the assembly of 1D filaments.Biophysical journal · 2025Article
- Mesoscopic p53-rich clusters represent a new class of protein condensates.Biophysics reviews · 2025Review
- Characterizing heterogeneity in amyloid formation processes.Current opinion in structural biology · 2024Review
- Single-Molecule Kinetic Observation of Antibody Interactions with Growing Amyloid β Fibrils.Journal of the American Chemical Society · 2024Article
- Peptide Self-Assembly into Amyloid Fibrils: Unbiased All-Atom Simulations.The journal of physical chemistry. B · 2024Review
- Misfolded protein oligomers: mechanisms of formation, cytotoxic effects, and pharmacological approaches against protein misfolding diseases.Molecular neurodegeneration · 2024Review
- Nucleation and Growth of Amyloid Fibrils.The journal of physical chemistry. B · 2023Article
- Direct Observation of Seeded Conformational Conversion of hIAPPJournal of chemical information and modeling · 2023Article
- Direct observation of secondary nucleation along the fibril surface of the amyloidProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Direct Observation of Competing Prion Protein Fibril Populations with Distinct Structures and Kinetics.ACS nano · 2023Article
- Cooperative amyloid fibre binding and disassembly by the Hsp70 disaggregase.The EMBO journal · 2022Article
- Conformational Variability of Amyloid-β and the Morphological Diversity of Its Aggregates.Molecules (Basel, Switzerland) · 2022Review
- Single-molecule fluorescence imaging and deep learning reveal highly heterogeneous aggregation of amyloid-β 42.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- A Palette of Fluorescent AInternational journal of molecular sciences · 2022Article
- General Principles Underpinning Amyloid Structure.Frontiers in neuroscience · 2022Review
- Multiscale Models for Fibril Formation: Rare Events Methods, Microkinetic Models, and Population Balances.Life (Basel, Switzerland) · 2021Article
- Aβ receptors specifically recognize molecular features displayed by fibril ends and neurotoxic oligomers.Nature communications · 2021Article
- Single-molecule orientation localization microscopy for resolving structural heterogeneities between amyloid fibrils.Optica · 2020Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
The major hallmark of Alzheimer's disease is the deposition of plaques of amyloid fibrils formed from amyloid-β (Aβ) peptides. Kinetic studies have contributed significantly towards a mechanistic understanding of amyloid fibril self-assembly, however dynamic features of the aggregation process cannot be captured using ensemble methods. Here we present an assay for imaging Aβ42 aggregation dynamics at the single fibril level, allowing for the quantitative extraction of concentration and temperature dependent kinetic parameters. From direct observation of elongation using TIRF and super-resolution optical microscopy, we find that Aβ42 fibril growth is strongly polarized, with fast and slow growing ends arising from different elongation rates, but also from a growth incompetent state, which dominates the process at the slow growing end. Our findings reveal the surprising complexity of the Aβ42 fibril elongation reaction at the microscopic level.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.