ArticleBiomolecules2019
Kinetic Transition in Amyloid Assembly as a Screening Assay for Oligomer-Selective Dyes.
Article in Biomolecules, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- A Highly Sensitive Water-Soluble Donor-Acceptor Dye for Early-Stage Amyloid Aggregation Kinetics.The journal of physical chemistry. B · 2026Article
- Inhibition of Human Amylin Aggregation:ACS omega · 2025Article
- High-throughput discovery of fluoroprobes that recognize amyloid fibril polymorphs.Nature chemistry · 2025Article
- Tau Oligomers in Alzheimer's Disease: Modulation Effect of Osmolytes on Amplified Brain-Derived Tau Oligomers.ACS chemical neuroscience · 2025Article
- MAPT mutations associated with familial tauopathies lead to formation of conformationally distinct oligomers that have cross-seeding ability.Protein science : a publication of the Protein Society · 2024Article
- Crystal Violet Selectively Detects Aβ Oligomers but Not Fibrils In Vitro and in Alzheimer's Disease Brain Tissue.Biomolecules · 2024Article
- Conformation of Pyroglutamated Amyloid β (3-40) and (11-40) Fibrils - Extended or Hairpin?The journal of physical chemistry. B · 2024Article
- Amyloid oligomers as on-pathway precursors or off-pathway competitors of fibrils.Frontiers in molecular biosciences · 2023Review
- S100B chaperone multimers suppress the formation of oligomers during Aβ42Frontiers in neuroscience · 2023Article
- Influence of Centrifugation and Shaking on the Self-Assembly of Lysozyme Fibrils.Biomolecules · 2022Article
- Human RAD51 Protein Forms Amyloid-like AggregatesInternational journal of molecular sciences · 2022Article
- Peptide backbone modifications of amyloid β (1-40) impact fibrillation behavior and neuronal toxicity.Scientific reports · 2021Article
- Origin, toxicity and characteristics of two amyloid oligomer polymorphs.RSC chemical biology · 2021Article
- Biomolecules from Different Angles.Biomolecules · 2020Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Assembly of amyloid fibrils and small globular oligomers is associated with a significant number of human disorders that include Alzheimer's disease, senile systemic amyloidosis, and type II diabetes. Recent findings implicate small amyloid oligomers as the dominant aggregate species mediating the toxic effects in these disorders. However, validation of this hypothesis has been hampered by the dearth of experimental techniques to detect, quantify, and discriminate oligomeric intermediates from late-stage fibrils, in vitro and in vivo. We have shown that the onset of significant oligomer formation is associated with a transition in thioflavin T kinetics from sigmoidal to biphasic kinetics. Here we showed that this transition can be exploited for screening fluorophores for preferential responses to oligomer over fibril formation. This assay identified crystal violet as a strongly selective oligomer-indicator dye for lysozyme. Simultaneous recordings of amyloid kinetics with thioflavin T and crystal violet enabled us to separate the combined signals into their underlying oligomeric and fibrillar components. We provided further evidence that this screening assay could be extended to amyloid-β peptides under physiological conditions. Identification of oligomer-selective dyes not only holds the promise of biomedical applications but provides new approaches for unraveling the mechanisms underlying oligomer versus fibril formation in amyloid assembly.
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Registered trials
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