[18] Quantification of β-sheet amyloid fibril structures with thioflavin T
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Both compounds L1 and L2 contain a 2-phenylbenzothiazole fragment reminiscent of the fluorescent dye ThT used to detect the β-sheet structure of fibrillar Aβ aggregates.
“Both compounds L1 and L2 contain a 2-phenylbenzothiazole fragment reminiscent of the fluorescent dye ThT used to detect the β-sheet structure of fibrillar Aβ aggregates.45,46”
From Small Bifunctional Chelators That Do Not Disaggregate Amyloid β Fibrils Exhibit Reduced Cellular Toxicity (2014) · cites this paper as [46]
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“Regardless of their origin, all amyloid fibers cause a red shift when mixed with CR (42,43) and cause fluorescence when mixed with thioflavin T (ThT) (45,46).”
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“for quantification of amyloid fibrils in vitro in presence of amyloid precursor proteins and amorphous aggregates (65).”
BackgroundEGCG remodels mature α-synuclein and amyloid-β fibrils and reduces cellular toxicity
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Membrane damage by human islet amyloid polypeptide through fibril growth at the membrane
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“In particular, thioflavin T binding ( Δ ), commonly used for measuring amyloid-like structure 38, generates reaction curves that are delayed compared to the curves from the HPLC sedimentation ( ◆ ) and light scattering ( ○ ) assays (Fig.”
Dependence of α-Synuclein Aggregate Morphology on Solution Conditions
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Small-molecule conversion of toxic oligomers to nontoxic β-sheet–rich amyloid fibrils
Bieschke, J., Herbst, M., Wiglenda, T., Friedrich, R. P., Boeddrich, A., Schiele, F., Kleckers, D., del Amo, J. M. L., Grüning, B. A., Wang, Q., et al. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.719 · Cited by 443 · see citing works
α-Synuclein misfolding and aggregation: Implications in Parkinson’s disease pathogenesis
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Sonication of proteins causes formation of aggregates that resemble amyloid
Stathopulos, P., Scholz, G. A., Hwang, Y., Rumfeldt, J. A., Lepock, J., & Meiering, E. M. (2004) · Protein Science · doi:10.1110/ps.04831804 · Cited by 417 · see citing works
“Thioflavin T and Congo red binding to aggregates ThT (LeVine 1999) and CR (Klunk et al. 1999) are standard dyes used to monitor the formation of amyloid structure.”
MethodLeon, R. M., Garcı́a, A. G., & Marco, J. L. (2011) · Medicinal Research Reviews · doi:10.1002/med.20248 · Cited by 442 · see citing works
Seeding Specificity in Amyloid Growth Induced by Heterologous Fibrils*
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ThT 101: a primer on the use of thioflavin T to investigate amyloid formation
Malmos, K. G., Blancas‐Mejía, L. M., Weber, B., Büchner, J., Ramı́rez-Alvarado, M., Naiki, H., & Otzen, D. E. (2017) · Amyloid · doi:10.1080/13506129.2017.1304905 · Cited by 453 · see citing works
“istic blue shift in the emission spectrum [4,6] from approxi-”
BackgroundAntiparallel β-sheet: a signature structure of the oligomeric amyloid β-peptide
Cerf, E., Sarroukh, R., Tamamizu‐Kato, S., Breydo, L., Derclaye, S., Dufrêne, Y. F., Narayanaswami, V., Goormaghtigh, E., Ruysschaert, J., & Raussens, V. (2009) · Biochemical Journal · doi:10.1042/bj20090379 · Cited by 497 · see citing works
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“Finally, to determine whether the exogenous ApCPEB puncta in sensory neurons are amyloid in nature, we stained these puncta with thioflavin S (Kimura et al., 2003; LeVine, 1999) (Figure 4F).”
InfluentialGlobal analysis of protein structural changes in complex proteomes
Feng, Y., Franceschi, G. D., Kahraman, A., Soste, M., Melnik, A., Boersema, P. J., de Laureto, P. P., Nikolaev, Y., Oliveira, A. P., & Picotti, P. (2014) · Nature Biotechnology · doi:10.1038/nbt.2999 · Cited by 399 · see citing works
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“However, since β-sheet formation correlates with fibril formation, ThT fluorescence is a useful surrogate marker [28].”
BackgroundANS binding reveals common features of cytotoxic amyloid species.
Bolognesi, B., Kumita, J., Barros, T. P., Esbjorner, E. K., Luheshi, L. M., Crowther, D., Wilson, M. R., Dobson, C., Favrin, G., & Yerbury, J. (2010) · ACS Chemical Biology · doi:10.1021/cb1001203.s001 · Cited by 376
“tion with ordered -sheet structures (19).”
Conformational Abs recognizing a generic amyloid fibril epitope
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Molecular Rotors: What Lies Behind the High Sensitivity of the Thioflavin-T Fluorescent Marker
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Proline and glycine control protein self-organization into elastomeric or amyloid fibrils.
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“Both peptides formed fibrillar precipitates and were subjected to the thioflavin-T binding assay for amyloid fibril detection (Figure 5) (LeVine, 1999).”
MethodInfluentialSelf‐assembling amphiphilic peptides
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Nitration of Tyrosine 10 Critically Enhances Amyloid β Aggregation and Plaque Formation
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Polyglutamine aggregation behavior in vitro supports a recruitment mechanism of cytotoxicity
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18F-THK523: a novel in vivo tau imaging ligand for Alzheimer's disease
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“Aggregation of b -amyloid 1–42 fibril was confirmed using thioflavin T fluorescence (LeVine, 1999).”
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Self-citationPrinciples, approaches, and challenges for predicting protein aggregation rates and shelf life
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Freeze-frame inhibitor captures acetylcholinesterase in a unique conformation.
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A Three-Stage Kinetic Model of Amyloid Fibrillation
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“Even though histological dyes like thioflavin T (ThT) and Congo Red have been the commonly used as indicators of the presence of amyloid fibrils, the relationship between fluorescence intensity and amount of amyloid fibril remain unclear (18,19).”
The curli nucleator protein, CsgB, contains an amyloidogenic domain that directs CsgA polymerization
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Glycation Induces Formation of Amyloid Cross-β Structure in Albumin*
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“Such fibrillar aggregates can be detected using the fluorophore thioflavin that upon binding to -sheet-rich structures displays enhanced fluorescence intensity (LeVine, 1999; Santa-María et al., 2006).”
BackgroundMethodStathopulos, P. B., Rumfeldt, J., Scholz, G. A., Irani, R. A., Frey, H. E., Hallewell, R. A., Lepock, J. R., & Meiering, E. M. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1237797100 · Cited by 258 · see citing works
Macromolecular Crowding Accelerates Amyloid Formation by Human Apolipoprotein C-II
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Amyloid as a Depot for the Formulation of Long-Acting Drugs
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The changing face of glucagon fibrillation: structural polymorphism and conformational imprinting.
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Study on the binding of Thioflavin T to β-sheet-rich and non- β-sheet cavities
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Bacterial Inclusion Bodies Contain Amyloid-Like Structure
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Heavy metal ions are potent inhibitors of protein folding
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Iron Promotes the Toxicity of Amyloid β Peptide by Impeding Its Ordered Aggregation
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ALS Mutants of Human Superoxide Dismutase Form Fibrous Aggregates Via Framework Destabilization
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Spectral Properties of Thioflavin T and Its Complexes with Amyloid Fibrils
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Cross‐seeding effects of amyloid β‐protein and α‐synuclein
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“We used a well-characterized assay of fibril formation, thioflavin dye binding (LeVine 1999), to determine the effects of fibrils or cross-linked oligomers on peptide assembly.”
MethodAmyloid peptides and proteins in review
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Small Molecule Modulators of Copper-Induced Aβ Aggregation
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Hierarchical Assembly of β2-Microglobulin Amyloid In Vitro Revealed by Atomic Force Microscopy
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“ThT increases fluorescence on binding to b-sheet rich amyloid-like structures [25].”
BackgroundPrion Disease Blood Test Using Immunoprecipitation and Improved Quaking-Induced Conversion
Orrú, C., Wilham, J. M., Raymond, L., Kuhn, F., Schroeder, B., Raeber, A., & Caughey, B. (2011) · mBio · doi:10.1128/mbio.00078-11 · Cited by 195
Amyloid Fibril Formation by Lens Crystallin Proteins and Its Implications for Cataract Formation*
Meehan, S., Berry, Y. J., Luisi, B., Dobson, C., Carver, J., & MacPhee, C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m308203200 · Cited by 195 · see citing works
Camps, P., Formosa, X., Galdeano, C., Gómez, T., Muñoz-Torrero, D., Scarpellini, M., Viayna, E., Badía, A., Clos, M. V., Camins, A., et al. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm8001313 · Cited by 194 · see citing works
Insights into the mechanism of aggregation and fibril formation from bovine serum albumin.
Bhattacharya, M., Jain, N., & Mukhopadhyay, S. (2011) · Journal of Physical Chemistry B · doi:10.1021/jp111528c · Cited by 192
SDS-Induced Fibrillation of α-Synuclein: An Alternative Fibrillation Pathway
Giehm, L., Oliveira, C. L. P., Christiansen, G., Pedersen, J. S., & Otzen, D. E. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.05.060 · Cited by 195 · see citing works
“We quantify fibrillation through the fluorescent probe thioflavin T (ThT) whose emission intensity at 485 nm increases by several orders of magnitude in the presence of fibrils.(43) We incubated 20 μM αSN with 0–10 mM SDS without agitation”
Effects of Grape Seed-derived Polyphenols on Amyloid β-Protein Self-assembly and Cytotoxicity*
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Metabolite-initiated protein misfolding may trigger Alzheimer's disease
Zhang, Q., Powers, E. T., Nieva, J. J., Huff, M. E., Dendle, M. A., Bieschke, J., Glabe, C. G., Eschenmoser, A., Wentworth, P., Lerner, R. A., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400924101 · Cited by 197 · see citing works
α-Synuclein Alters Toll-Like Receptor Expression
Béraud, D., Twomey, M. A., Bloom, B., Mittereder, A., Ton, V., Neitzke, K., Chasovskikh, S., Mhyre, T. R., & Maguire‐Zeiss, K. A. (2011) · Frontiers in Neuroscience · doi:10.3389/fnins.2011.00080 · Cited by 199 · see citing works
“, Liu, F., Pristupa, Z. B., and Niznik, H. B. (2001). Direct binding and functional coupling of alpha-synuclein to the dopamine transporters accelerate dopamine-induced apoptosis. FASEB J. 15, 916–926. Lee, H. J., Patel, S., and Lee, S. J. (2005). Intravesicular localization and exocytosis of alpha-synuclein and its a…”
BackgroundInfluentialNanomaterials: amyloids reflect their brighter side
Mankar, S., Arunagiri, A., Sen, S., & Maji, S. K. (2011) · Nano Reviews · doi:10.3402/nano.v2i0.6032 · Cited by 182 · see citing works
Jacob, R. S., Ghosh, D., Singh, P. K., Basu, S. K., Jha, N. N., Das, S., Sukul, P. K., Patil, S. P., Sathaye, S., Kumar, A., et al. (2015) · Biomaterials · doi:10.1016/j.biomaterials.2015.03.002 · Cited by 200 · see citing works
Structural properties of pore-forming oligomers of alpha-synuclein.
Kim, H.-Y., Cho, M.-K., Kumar, A., Maier, E., Siebenhaar, C., Becker, S., Fernández, C., Lashuel, H., Benz, R., Lange, A., et al. (2009) · Journal of the American Chemical Society · doi:10.1021/ja9077599 · Cited by 185 · see citing works
Klingstedt, T., Åslund, A., Simon, R., Johansson, L. B. G., Mason, J., Nyström, S., Hammarström, P., & Nilsson, K. P. (2011) · Organic and biomolecular chemistry · doi:10.1039/c1ob05637a · Cited by 183 · see citing works
Structural mechanism of serum amyloid A-mediated inflammatory amyloidosis
Lu, J., Yu, Y., Zhu, I., Cheng, Y., & Sun, P. D. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1322357111 · Cited by 180 · see citing works
“1 and carried out fibril formation assays using thioflavin T (ThT) staining (29).”
MethodAβ amyloid fibrils possess a core structure highly resistant to hydrogen exchange
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Multicomponent peptide assemblies
Raymond, D. M., & Nilsson, B. L. (2018) · Chemical Society Reviews · doi:10.1039/c8cs00115d · Cited by 348 · see citing works
Sulatskaya, A. I., Maskevich, A. A., Kuznetsova, I. М., Uversky, V. N., & Константинович, Т. К. (2010) · PLoS ONE · doi:10.1371/journal.pone.0015385 · Cited by 172 · see citing works
- 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)
- 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
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › 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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