ArticleRoyal Society open science2017
Thioflavin T as an amyloid dye: fibril quantification, optimal concentration and effect on aggregation.
Article in Royal Society open science, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 326 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
326 citing papers in PubMed, 767 citations in OpenAlex.
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- Surface cues shape procoagulant properties of amyloidogenic microclots.Cell death & disease · 2026Review
- Standardization of cross-site biophysical studies of bovine insulin amyloids is challenged by structural polymorphism.European biophysics journal : EBJ · 2026Article
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- Local Organization of Biological Membranes Modulates Tau-Lipid Interactions and Fibril formation.JACS Au · 2026Article
- Thioflavin-T derivatives with controlled AIE and ACQ properties as potential one-photon and two-photon amyloid markers.Scientific reports · 2026Article
- Exploring Passive Permeability Profiles of Cyclic Heptapeptide Chemical Space Uncovers Bioactivity of Mortiamide Scaffold Driven by Colloidal Aggregation.Chembiochem : a European journal of chemical biology · 2026Article
- Fluorescent non-canonical amino acid as a site-specific conformational probe of prion formation.bioRxiv : the preprint server for biology · 2026Article
266 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Formation of amyloid fibrils underlies a wide range of human disorders, including Alzheimer's and prion diseases. The amyloid fibrils can be readily detected thanks to thioflavin T (ThT), a small molecule that gives strong fluorescence upon binding to amyloids. Using the amyloid fibrils of Aβ40 and Aβ42 involved in Alzheimer's disease, and of yeast prion protein Ure2, here we study three aspects of ThT binding to amyloids: quantification of amyloid fibrils using ThT, the optimal ThT concentration for monitoring amyloid formation and the effect of ThT on aggregation kinetics. We show that ThT fluorescence correlates linearly with amyloid concentration over ThT concentrations ranging from 0.2 to 500 µM. At a given amyloid concentration, the plot of ThT fluorescence versus ThT concentration exhibits a bell-shaped curve. The maximal fluorescence signal depends mostly on the total ThT concentration, rather than amyloid to ThT ratio. For the three proteins investigated, the maximal fluorescence is observed at ThT concentrations of 20-50 µM. Aggregation kinetics experiments in the presence of different ThT concentrations show that ThT has little effect on aggregation at concentrations of 20 µM or lower. ThT at concentrations of 50 µM or more could affect the shape of the aggregation curves, but this effect is protein-dependent and not universal.
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What OpenQuestion holds
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.