ArticleScientific reports2017
A novel pathway for amyloids self-assembly in aggregates at nanomolar concentration mediated by the interaction with surfaces.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 59 citations in OpenAlex.
- Amyloid β-Cholesterol Interplay: Removal of Cholesterol From the Membranes to Catalyze Aggregation and Amyloid Pathology.Journal of neurochemistry · 2026Article
- Catalytic Effect of Amyloid-β on Native Tau Aggregation at Physiologically Relevant Concentrations.International journal of molecular sciences · 2025Article
- Nucleation dynamics in amyloid-beta dimerization revealed by single-molecule fingerprinting.Cell reports. Physical science · 2025Article
- Molecular dynamics simulations of amyloid-β(29-42) aggregation in bulk water and at the air-water interface.Biophysics and physicobiology · 2025Article
- Biophysical insights into the molecular mechanisms of beta amyloid aggregation and its toxic effects in Alzheimer's disease.Frontiers in molecular biosciences · 2025Review
- Damage of the Phospholipid Bilayer by Aβ42 at Physiologically Relevant Peptide Concentrations.ACS chemical neuroscience · 2024Article
- Article
- α-synuclein-assisted oligomerization of β-amyloid (1-42).Archives of biochemistry and biophysics · 2022Article
- Free Cholesterol Accelerates Aβ Self-Assembly on Membranes at Physiological Concentration.International journal of molecular sciences · 2022Article
- Dynamics of Amyloid Formation from Simplified Representation to Atomistic Simulations.Methods in molecular biology (Clifton, N.J.) · 2022Article
- An Alzheimer's Disease Mechanism Based on Early Pathology, Anatomy, Vascular-Induced Flow, and Migration of Maximum Flow Stress Energy Location with Increasing Vascular Disease.Journal of Alzheimer's disease : JAD · 2022Article
- Frustrated peptide chains at the fibril tip control the kinetics of growth of amyloid-β fibrils.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Shear-Induced Amyloid Aggregation in the Brain: V. Are Alzheimer's and Other Amyloid Diseases Initiated in the Lower Brain and Brainstem by Cerebrospinal Fluid Flow Stresses?Journal of Alzheimer's disease : JAD · 2021Article
- Fast Purification of Recombinant Monomeric Amyloid-β fromACS chemical neuroscience · 2020Article
- Two C-terminal sequence variations determine differential neurotoxicity between human and mouse α-synuclein.Molecular neurodegeneration · 2020Article
- Interaction of Aβ42 with Membranes Triggers the Self-Assembly into Oligomers.International journal of molecular sciences · 2020Article
- Interactions between Soluble Species of β-Amyloid and α-Synuclein Promote Oligomerization while Inhibiting Fibrillization.Biochemistry · 2020Article
- Amyloid B-Protein Aggregation at Physiologically Relevant Concentrations. A Critical Role of Membranes.Alzheimer's research & therapy open access · 2020Article
- AFM Probing of Amyloid-Beta 42 Dimers and Trimers.Frontiers in molecular biosciences · 2020Article
- Assembly of α-synuclein aggregates on phospholipid bilayers.Biochimica et biophysica acta. Proteins and proteomics · 2019Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
A limitation of the amyloid hypothesis in explaining the development of neurodegenerative diseases is that the level of amyloidogenic polypeptide in vivo is below the critical concentration required to form the aggregates observed in post-mortem brains. We discovered a novel, on-surface aggregation pathway of amyloidogenic polypeptide that eliminates this long-standing controversy. We applied atomic force microscope (AFM) to demonstrate directly that on-surface aggregation takes place at a concentration at which no aggregation in solution is observed. The experiments were performed with the full-size Aβ protein (Aβ42), a decapeptide Aβ(14-23) and α-synuclein; all three systems demonstrate a dramatic preference of the on-surface aggregation pathway compared to the aggregation in the bulk solution. Time-lapse AFM imaging, in solution, show that over time, oligomers increase in size and number and release in solution, suggesting that assembled aggregates can serve as nuclei for aggregation in bulk solution. Computational modeling performed with the all-atom MD simulations for Aβ(14-23) peptide shows that surface interactions induce conformational transitions of the monomer, which facilitate interactions with another monomer that undergoes conformational changes stabilizing the dimer assembly. Our findings suggest that interactions of amyloidogenic polypeptides with cellular surfaces play a major role in determining disease onset.
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