Cited by 1,365Alzheimer's disease research and treatmentsPrion Diseases and Protein MisfoldingAmyloidosis: Diagnosis, Treatment, Outcomes

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[18] Quantification of β-sheet amyloid fibril structures with thioflavin T

LeVine, Harry·1999·Methods in Enzymology

DOI 10.1016/s0076-6879(99)09020-5

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Method
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“ThT has been shown to bind specifically to cross -sheet structures of amyloids (43, 44), thus routinely used to monitor amyloid formation kinetics (45– 48).”
Method
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“Binding of TfT to protein fibrils is accompanied by a characteristic increase in the fluorescence intensity in the vicinity of 482 nm [15].”
Background
Controllable coacervation of recombinantly produced spider silk protein using kosmotropic salts
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“ThT has a specific binding affinity for the b-sheet structures of proteins and can be used as a detection marker [40,41].”
Background
Protein Co-Aggregation Related to Amyloids: Methods of Investigation, Diversity, and Classification
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“A number of such ap roaches are based on the ag regate staining with amyloid-specific dyes, like ThT or CR [59].”
Background
Super-Resolution Imaging of Amyloid Structures over Extended Times Using Transient Binding of Single Thioflavin T Molecules
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Amyloids and Protein Aggregation—Analytical Methods
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“(109,110) Similar to ThT, ThS binds amyloid fibrils but not monomers, and undergoes fluorescence intensity changes and distinct spectral shift upon binding, the hyperchromic shift in the emission maxima of ThS is ∼45 nm.(100) Boshuizen et al.”
Background
Engineered antibody intervention strategies for Alzheimer's disease and related dementias by targeting amyloid and toxic oligomers
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“The fluorescence intensity was measured at an excitation wavelength of 450 nm and an emission wavelength of 482 nm with a spectrofluorometer LSB-50 (Perkin Elmer, Norwalk, CT, USA) with both excitation and emission bandwidths of 5 nm as previously described (LeVine, 1999).”
Method
C-terminal α-synuclein truncations are linked to cysteine cathepsin activity in Parkinson’s disease
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Method
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Method
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Self-citation
Small Bifunctional Chelators That Do Not Disaggregate Amyloid β Fibrils Exhibit Reduced Cellular Toxicity
Sharma, A. K., Kim, J., Prior, J. T., Hawco, N. J., Rath, N. P., Kim, J., & Mirica, L. M. (2014) · Inorganic Chemistry · doi:10.1021/ic500926c · Cited by 48
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“Th-T specifically binds to amyloid aggregates (LeVine, 1999) and its fluorescence is enhanced after binding (Alam et al.”
Background
On the pH-dependence of α-synuclein amyloid polymorphism and the role of secondary nucleation in seed-based amyloid propagationPreprint
Frey, L., Ghosh, D., Qureshi, B. M., Rhyner, D., Guerrero-Ferreira, R. C., Pokharna, A., Kwiatkowski, W., Serdiuk, T., Picotti, P., Riek, R., et al. (2024) · bioRxiv · doi:10.1101/2023.06.25.546428 · Cited by 47
“For these analyses, we monitored the effect of seeding on the kinetics of fibril formation using thioflavin T (ThT) fluorescence 47,48 and probed the structures of the resulting seeded fibrils by cryo-EM.”
Method
Evaluation of fluorescent dyes to measure protein aggregation within mammalian cell culture supernatants
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Formation of functional, non‐amyloidogenic fibres by recombinant Bacillus subtilis TasA
Erskine, E., Morris, R. J., Schor, M., Earl, C., Gillespie, R. M. C., Bromley, K. M., Sukhodub, T., Clark, L., Fyfe, P. K., Serpell, L. C., et al. (2018) · Molecular Microbiology · doi:10.1111/mmi.13985 · Cited by 48
Kinetic Mechanism of Thioflavin T Binding onto the Amyloid Fibril of Hen Egg White Lysozyme
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Amyloids: from pathogenesis to function
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Early detection of insulin fibrillation: a fluorescence lifetime assay to probe the pre-fibrillar regime.
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Non-Conjugated Small Molecule FRET for Differentiating Monomers from Higher Molecular Weight Amyloid Beta Species
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Authors: LeVine, H.
Corresponding author: LeVine, Harry
Venue: Methods in Enzymology
Publisher: Elsevier
Published: 1999
Volume: 309
Pages: 274-284
ISSN: 0076-6879 (ISSN-L)
DOI: 10.1016/s0076-6879(99)09020-5
OpenAlex: W1588296570
Cited by: 1,365
References: 25
Citations by year: 2026: 26 · 2025: 34 · 2024: 56 · 2023: 42 · 2022: 51 · 2021: 54 · 2020: 60 · 2019: 78 · 2018: 86 · 2017: 69 · 2016: 61 · 2015: 67 · 2014: 78 · 2013: 58 · 2012: 66
FWCI: 28.63
Type: book chapter
Language: en
Open access: closed
Locations: Methods in enzymology on CD-ROM/Methods in enzymology (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
Health Sciences › Medicine › Internal Medicine › Amyloidosis: Diagnosis, Treatment, Outcomes
Keywords: thioflavin T, amyloid fibrils, beta-sheet, amyloid quantification, Congo red, amyloid staining, amyloid fibril formation, fluorescence spectroscopy, Congo red birefringence
MeSH terms: Fluorescence, Hydrogen-Ion Concentration, Protein Binding, Spectrum Analysis, Thiazoles, Amyloid beta-Peptides, Protein Structure, Secondary, Benzothiazoles

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[18] Quantification of β-sheet amyloid fibril structures with thioflavin T

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