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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Marvian, A. T., Aliakbari, F., Mohammad-Beigi, H., Ahmadi, Z., Mehrpooyan, S., Lermyte, F., Nasouti, M., Collingwood, J., Otzen, D., & Morshedi, D. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.03.238 · Cited by 6
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Galkin, A. P., Velizhanina, M. E., Sopova, J. V., Shenfeld, A. A., & Zadorsky, S. P. (2018) · Biochemistry (Moscow) · doi:10.1134/s0006297918100048 · Cited by 8
Selektiv N‐methylierte lösliche IAPP‐Mimetika als potente IAPP‐Rezeptoragonisten und nanomolare Inhibitoren der Selbstassoziation von IAPP und Aβ40
Yan, L.-M., Velkova, A., Tatarek‐Nossol, M., Rammes, G., Sibaev, A., Andreetto, E., Kracklauer, M., Bakou, M., Malideli, E., Göke, B., et al. (2013) · Angewandte Chemie · doi:10.1002/ange.201302840 · Cited by 6
Hydrogen exchange mass spectrometry as an analytical tool for the analysis of amyloid fibrillogenesis
Scavenius, C., Ghodke, S., Otzen, D., & Enghild, J. (2011) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2010.10.001 · Cited by 6
“ThT fluorescence is one of the most widely used methods for following amyloid fibril formation [23].”
Method
Protein Misfolding Diseases
Gomes, C. M. (2019) · Methods in Molecular Biology · doi:10.1007/978-1-4939-8820-4 · Cited by 6
“For example, by utilizing high-throughput microplate-based thioflavin-T (ThT) fluorescence aggregation assays (a total of 825 replicate assays), our group has recently shown that the rate of aggregation of some ALS-variants of apo-SOD1 is significantly lower than rate of aggregation of WT apo-SOD1 [3], which is in con…”
BackgroundMethodResultInfluential
Bioactive Compounds from Morus indica as Inhibitors of Advanced Glycation End Products
Anandan, S., & Urooj, A. (2019) · Indian Journal of Pharmaceutical Sciences · doi:10.36468/pharmaceutical-sciences.509 · Cited by 6
Overview of Fibrillar and Oligomeric Assemblies of Amyloidogenic Proteins
Rahimi, F., & Bitan, G. (2011) · Springer eBooks · doi:10.1007/978-94-007-2774-8_1 · Cited by 6
Diversity and diversification of light chains in myeloma: the specter of amyloidogenesis by proxy.
Gu, M., Wilton, R., & Stevens, F. (2007) · Contributions to Nephrology · doi:10.1159/000096766 · Cited by 6
Highly sensitive chemiluminescence imaging of misfolded proteins in neurodegenerative models
Zhu, B., Liu, Z., Van, R. S., Wang, H., Kuang, S., Jia, Y., Leon, E. C., Yang, F., Zhang, J., Yang, J., et al. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2513311123 · Cited by 4
“Thioflavin T (ThT) is widely used for in vitro and ex vivo detection (17 –19), and recently showed promise in biofluid - based diagnosis (20 –23).”
Uric Acid, the End-Product of Purine Metabolism, Mitigates Tau-Related Abnormalities: Comparison with DOT, a Non-Antibiotic Oxytetracycline Derivative
de Mattos, B. A., Tomas‐Grau, R. H., Fernandes, T. A. A., González‐Lizárraga, F., Tourville, A., Ciss, I., Brunel, J. M., Chehín, R. N., Lannuzel, A., Ferrié, L., et al. (2025) · Biomolecules · doi:10.3390/biom15070941 · Cited by 6
Development of fluorophores for the detection of oligomeric aggregates of amyloidogenic proteins found in neurodegenerative diseases
Teppang, K. L., Zhao, Q., & Yang, J. (2023) · Frontiers in Chemistry · doi:10.3389/fchem.2023.1343118 · Cited by 5
“Historically, like other amyloid aggregates implicated in NDs such as tau or A β , α - synuclein can be detected by small ﬂ uorescent molecules such as Thio ﬂ avin-T (ThT) and Congo Red (CR) (Naiki et al., 1989; LeVine, 1999; Campioni et al., 2010; Fernandez-Flores, 2011).”
Background
Amyloid-Like Aggregation in Native Protein and its Suppression in the Bio-Conjugated Counterpart
Mukhopadhyay, A., Stoev, I. D., King, D. A., Sharma, K. P., & Eiser, E. (2022) · Frontiers in Physics · doi:10.3389/fphy.2022.924864 · Cited by 6
Phosphorylated resveratrol as a protein aggregation suppressor in vitro and in vivo
Mehringer, J., Navarro, J. A., Touraud, D., Schneuwly, S., & Kunz, W. (2022) · RSC Chemical Biology · doi:10.1039/d1cb00220a · Cited by 6
The Fluorescent Dye 1,6 Diphenyl 1,3,5 Hexatriene Binds to Amyloid Fibrils Formed by Human Amylin and Provides a New Probe of Amylin Amyloid KineticsPreprint
Li, M.-H., Manathunga, L., London, E., & Raleigh, D. (2021) · bioRxiv · doi:10.1101/2021.05.10.443442 · Cited by 5
A Novel SOD1 Intermediate Oligomer, Role of Free Thiols and Disulfide Exchange
Koo, B., Munroe, W. H., Gralla, E., Valentine, J., & Whitelegge, J. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.619279 · Cited by 5
“Protein fibrillary aggregation in vitro requires a significant conformational conversion of proteins thought to be first to the monomer (also known as “nucleus”), to subsequently form oligomers which is a rate-limiting step of the overall aggregation reaction (LeVine, 1999; Banci et al., 2006).”
Background
Point mutations affecting yeast prion propagation change the structure of its amyloid fibrils
Sulatskaya, A. I., Bondarev, S., Sulatsky, M., Trubitsina, N. P., Belousov, M., Zhouravleva, G., Llanos, M., Kajava, A., Kuznetsova, I., & Turoverov, K. K. (2020) · Journal of Molecular Liquids · doi:10.1016/j.molliq.2020.113618 · Cited by 5
Amyloidogenic Nanoplaques in Cerebrospinal Fluid: Relationship to Amyloid Brain Uptake and Clinical Alzheimer’s Disease in a Memory Clinic Cohort
Aksnes, M., Müller, E. G., Tiiman, A., Edwin, T. H., Terenius, L. Y., Revheim, M.-E. R., Vukojević, V. B., Bogdanović, N., & Knapskog, A. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-200237 · Cited by 5
“Secondly, ThT is highly specific for amyloidosis, which is a central process in many neurodegenerative diseases [48]; ThT does not react with non-pathological protein monomers [49].”
Background
The flanking peptides issue from the maturation of the human islet amyloid polypeptide (hIAPP) slightly modulate hIAPP-fibril formation but not hIAPP-induced cell death
Vazquez, S. S., Blondeau, B., Cattan, P., Armanet, M., Guillemain, G., & Khemtémourian, L. (2019) · Biochimie · doi:10.1016/j.biochi.2019.12.005 · Cited by 5
“First, we studied the time course of the aggregation of the flanking peptides and mature hIAPP in solution by using thioflavin-T (ThT) binding fluorescence assays, which is a widely used method to monitor amyloid fibril formation [47].”
Method
Analysis of Prairie Vole Amylin Reveals the Importance of the N-terminus and Residue-22 in Amyloidogenicity and Cytotoxicity
Lee, K.-H., Noh, D., Zhyvoloup, A., & Raleigh, D. (2019) · Biochemistry · doi:10.1021/acs.biochem.9b00952 · Cited by 5
Peroxide-mediated oxidative coupling of primary alcohols and disulfides: Synthesis of 2-substituted benzothiazoles
Padilha, N., Penteado, F., Salomão, M. C., Lopes, E. F., Bettanin, L., Hartwig, D., Jacob, R., & Lenardão, E. (2019) · Tetrahedron Letters · doi:10.1016/j.tetlet.2019.05.021 · Cited by 5
Release of Pharmaceutical Peptides in an Aggregated State: Using Fibrillar Polymorphism to Modulate Release Levels
Madsen, J. K., Christiansen, G., Giehm, L., & Otzen, D. (2019) · Colloids and Interfaces · doi:10.3390/colloids3010042 · Cited by 5
“Amyloid formation occurs above the equilibrium solubility of the monomeric species and is usually detected with the dye thioflavin T, which undergoes a marked increase in fluorescence upon binding fibrils [18].”
Background
Cell assay for the identification of amyloid inhibitors in systemic AA amyloidosis
Puşcalău-Gîrţu, I., Scheller, J. S., Claus, S., & Fändrich, M. (2019) · Amyloid: Journal of Protein Folding Disorders · doi:10.1080/13506129.2019.1568978 · Cited by 5
“Fibrilbound ThT exhibits an increased fluorescence emission signal at 490 nm, if excited at 450 nm, compared to unbound ThT [34].”
Background
Role of PAMAM-OH dendrimers against the fibrillation pathway of biomolecules.
Sekar, G., Florance, I., Sivakumar, A., Mukherjee, A., & Chandrasekaran, N. (2016) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2016.09.002 · Cited by 5
An Environmentally Sensitive Fluorescent Dye as a Multidimensional Probe of Amyloid Formation
Yates, E. V., Meisl, G., Knowles, T., & Dobson, C. (2016) · Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.5b09663 · Cited by 5
Thioflavin T effect in diabetic Wistar rats: Reporting the antihyperglycemic property of an amyloid probing dye
Najafian, M., Amini, S., Dehestani, B., Parivar, K., & Ebrahim‐Habibi, A. (2014) · Pharmacological Reports · doi:10.1016/j.pharep.2014.10.013 · Cited by 5
Small Molecules Present in the Cerebrospinal Fluid Metabolome Influence Superoxide Dismutase 1 Aggregation
Cristóvão, J. S., Leal, S. S., Cardoso, I., & Gomes, C. M. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms140919128 · Cited by 5
Synthesis and Evaluation of 4-Aryl-2(1H)-quinolinones as Potent Amyloid β Fibrillogenesis Inhibitors.
Shimokawa, Y., Nakakoshi, M., Saito, S., Suzuki, H., Yokoyama, Y., Ishigami, A., Nishioka, H., & Tsubuki, M. (2012) · doi:10.1002/chin.201249156 · Cited by 5
New Methodology for Estimation of the Prion Protein 106-126 Amyloid Aggregation
Jeong, K., Suh, J., Chung, W., Kye, Y., Kim, D., & Lee, T. Y. (2010) · doi:10.5012/bkcs.2010.31.04.1029 · Cited by 5

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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