ArticleScientific reports2016
Nucleus factory on cavitation bubble for amyloid β fibril.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 49 citations in OpenAlex.
- Quantitative Analysis of Amyloid Fibril Nucleation by Linking Folding and Nucleation Pathways Using a Robust Ultrasonic Assay.ACS omega · 2026Article
- Ultrasonic frequency and intensity dependence in βUltrasonics sonochemistry · 2025Article
- Ultrasonic detection of α-synuclein amyloid seeds from a highly crowded environment.Biophysical journal · 2025Article
- Altering ROY polymorph crystallization in conventional and microfluidic crystallizers with acoustic cavitation.Scientific reports · 2025Article
- Accelerated amyloid fibril formation at the interface of liquid-liquid phase-separated droplets by depletion interactions.Protein science : a publication of the Protein Society · 2025Article
- Macromolecular crowding and supersaturation protect hemodialysis patients from the onset of dialysis-related amyloidosis.Nature communications · 2022Article
- Supersaturation-Dependent Formation of Amyloid Fibrils.Molecules (Basel, Switzerland) · 2022Review
- Polyphenol-solubility alters amyloid fibril formation of α-synuclein.Protein science : a publication of the Protein Society · 2021Article
- Exploring ligand binding pathways on proteins using hypersound-accelerated molecular dynamics.Nature communications · 2021Article
- Breakdown of supersaturation barrier links protein folding to amyloid formation.Communications biology · 2021Article
- Isoelectric point-amyloid formation of α-synuclein extends the generality of the solubility and supersaturation-limited mechanism.Current research in structural biology · 2020Article
- Heating during agitation of βThe Journal of biological chemistry · 2019Article
- Mechanisms of aggregation and fibril formation of the amyloidogenic N-terminal fragment of apolipoprotein A-I.The Journal of biological chemistry · 2019Article
- Salt-induced formations of partially folded intermediates and amyloid fibrils suggests a common underlying mechanism.Biophysical reviews · 2018Review
- Formation and properties of amyloid fibrils of prion protein.Biophysical reviews · 2018Review
- A specific form of prefibrillar aggregates that functions as a precursor of amyloid nucleation.Scientific reports · 2018Article
- Heparin-dependent aggregation of hen egg white lysozyme reveals two distinct mechanisms of amyloid fibrillation.The Journal of biological chemistry · 2017Article
- Heparin-induced amyloid fibrillation of βProtein science : a publication of the Protein Society · 2017Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Structural evolution from monomer to fibril of amyloid β peptide is related to pathogenic mechanism of Alzheimer disease, and its acceleration is a long-running problem in drug development. This study reveals that ultrasonic cavitation bubbles behave as catalysts for nucleation of the peptide: The nucleation reaction is highly dependent on frequency and pressure of acoustic wave, and we discover an optimum acoustical condition, at which the reaction-rate constant for nucleation is increased by three-orders-of magnitudes. A theoretical model is proposed for explaining highly frequency and pressure dependent nucleation reaction, where monomers are captured on the bubble surface during its growth and highly condensed by subsequent bubble collapse, so that they are transiently exposed to high temperatures. Thus, the dual effects of local condensation and local heating contribute to dramatically enhance the nucleation reaction. Our model consistently reproduces the frequency and pressure dependences, supporting its essential applicability.
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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.