SOLUBILITY / SOLUTION STABILITY: The product forms a clear, very dark yellow solution in methanol (0.1% w/v). It has been tested by TLC at 50 mg/mL in glacial acetic acid:water (1:1).2 Thioflavin T is reportedly soluble in cold water, very soluble in ho Thioflavin T (ThT, Thioflavine T, Basic Yellow 1) is a benzothiazole dye that exhibits enhanced fluorescence upon binding to amyloid fibrils and is commonly used to diagnose amyloid fibrils. * Please note that Selleck tests the solubility of all compounds in-house, and the actual solubility may differ slightly from published values. This is.
Thioflavin T is a cell-permeable benzothiazole dye that exhibits enhanced fluorescence upon binding to amyloid fibrils. Thioflavin T is useful in monitoring stacked β sheet aggregates. Soluble in water (5 mg/ml), alcohol (100 mg/ml), methanol (0.1% w/v), and glacial acetic acid:water (1:1) (50 mg/ml). For Research Use Only Thioflavin T is a benzothiazole dye that exhibits enhanced fluorescence upon binding to amyloid fibrils and is commonly used to diagnose amyloid fibrils, both ex vivo and in vitro. In aqueous solutions, thioflavin T was found to exist as micelles..
Thioflavin T. SPECIFICATION SHEET. Thioflavin T; CAS number: 2390-54-7: Properties; Molecular formula: C 17 H 19 ClN 2 S: Molar mass: Solubility in / Miscibility with Water: Insoluble. Transport information. Not a hazardous material for transportation. DOT regulations: Hazard class: None. Binding induces a shift in excitation maximum (385 nm to 450 nm) and emission maximum (445 nm to 482 nm). Highly soluble in water. Limited ability to cross the blood-brain barrier Thioflavin T Revision Date 19-Jan-2018 Mobility Will likely be mobile in the environment due to its water solubility. 13. Disposal considerations Waste Disposal Methods Chemical waste generators must determine whether a discarded chemical is classified as a hazardous waste. Chemical waste generators must also consult local, regional, an
Protocol for assaying active alpha-synuclein monomer and aggregate binding to thioflavin T. 1. Prepare 1 mM stock solution of Thioflavin T (ThT) in dH 2 O (prepare fresh and filter through a 0.2 μm syringe filter). 2. Dilute the ThT in PBS (pH 7.4) so that the final ThT concentration in each well is 25 μM. 3 Thioflavin T. Thioflavin T (Basic Yellow 1, Methylene yellow, CI 49005, or ThT) is a benzothiazole salt obtained by the methylation of dehydrothiotoluidine with methanol in the presence of hydrochloric acid.The dye is widely used to visualize and quantify the presence of misfolded protein aggregates called amyloid, both in vitro and in vivo (e.g., plaques composed of amyloid beta found in the. Useful in monitoring stacked β-sheet aggregates, Thioflavin T has also been used in histology and for protein characterization. Biotium offers high purity grade of Thioflavin T with HPLC purity greater than 97%. Yellow solid soluble in DMF and DMSO Stored desiccated at 4° In this study, a water-soluble fluorogenic dye (i.e., Thioflavin T (ThT)) was employed to recognize RNA G-quadruplex structures using UV-Vis absorption spectra, fluorescence spectra and emission lifetime experiments Abstract Thioflavin T (ThT), a water-soluble fluorescence probe and the conventional dye for the detection of amyloid fibrils has recently been demonstrated to recognize and bind nucleic acids. It induces the formation of G-quadruplex (G4) structure and appears as a sensor by emitting enhanced fluorescence
Thioflavin T (ThT) is prepared by dissolving ~3 mg dry powder in 1 mL water. The solution is filtered through 0.22 μm syringe filters followed by measurement of the concentration by diluting the stock solution in ethanol and using an extinction coefficient of 26,620 M-1 cm-1 at 416 nm. The stock solution is stored at 4 °C covered with foil and used for up to a month to make assay solutions. Shop a large selection of Stains and Dyes products and learn more about Thioflavin T, ACROS Organics. 5g; Glass bottle 3.3. Thioflavin T preparation and fluorescence measurement. ThT (Sigma, product no. T3516) was dissolved in PBS buffer and was filtered through a 0.2 µm syringe filter. Then the concentration of thioflavin T was determined using an extinction coefficient of 36 mM −1 cm −1 at 412 nm [27,28]
Thioflavin T. Catalog No. T17073 CAS 2390-54-7. Synonyms: Basic Yellow 1. Purity 97.14% Datasheet. Thioflavin T is a widely used dye for visualizing and is a cationic Benzothiazole dye that shows enhanced fluorescence upon binding to amyloid in tissue sections. Thioflavin T, CAS 2390-54-7 Thioflavin T - CAS 2390-54-7 - Calbiochem A cell-permeable benzothiazole dye that exhibits enhanced fluorescence upon binding to amyloid fibrils. - Find MSDS or SDS, a COA, data sheets and more information
The data of this reaction are both of a qualitative and quantitative nature, including gel images from chemical cross-linking and Western blots, fractional solubility, thioflavin T binding, size exclusion chromatograms, transmission electron microscopy images, circular dichroism spectra, and fluorescence resonance energy transfer efficiencies. Thioflavin T is a fluorescent probe for amyloid fibrils. 1 It displays excitation/emission maxima of 385/445 nm, respectively, and exhibits an increase in fluorescence intensity and a shift in excitation/emission maxima to 450/482 nm upon binding to amyloid fibrils. 1,2 The fluorescence intensity is also pH dependent, increasing in intensity as the pH increases. 2 Thioflavin T binds to. Biophysical comparison of soluble amyloid-β(1-42) protofibrils, oligomers, and protofilaments. Hydrodynamic radius (RH) measurements by DLS and thioflavin T fluorescence measurements indicated that protofibrils and oligomers had commonalities, yet electron microscopy revealed morphological differences between the two. SEC-purified Aβ(1-42. In this study, we examined these soluble oligomers by a variety of biophysical techniques including atomic force microscopy (AFM), circular dichroism, Fourier-transform infrared spectroscopy and thioflavin T fluorescence. We observed that the fibrillation kinetics is affected by the variation in salt and protein concentrations Amyloid fibrils form above the solubility of amyloidogenic proteins or peptides upon breaking supersaturation, followed by a nucleation and elongation mechanism, which is similar to the crystallization of solutes. when monitored by thioflavin T (ThT) fluorescence or transmission electron microscopy (TEM). Nuclear magnetic resonance (NMR.
Thioflavin T is supplied as a crystalline solid. A stock solution may be made by dissolving the thioflavin T in the solvent of choice, which should be purged with an inert gas. Thioflavin T is soluble in organic solvents such as ethanol, DMSO, and dimethyl formamide. The solubility of thioflavin T in these solvents is approximately 1 mg/ml The SPI hydrolysates and fibrils were characterized through AFM, Thioflavin T (ThT) fluorescence, SDS-PAGE, FTIR, solubility, particle size, and DSC. Stable amyloid-like protein fibrils were formed with 8-10 h of hydrolytic heating at 85 °C followed by 3 days of incubation at room temperature, as observed under AFM and confirmed with ThT assay
thioflavin T (ThT) to assay the formation of amyloid fibrils from synthetic Ab peptide. However, based on the high cost of generating pure samples of synthetic or recombinant Ab peptide, large-scale library screen-ing is cost prohibitive. In addition, there are now numerous reports indicating that small, solubl Figure Legend Snippet: Effect of TTR-S on both soluble and fibrillar Aβ42 (A) Thioflavin T (ThT) fluorescence was measured from samples containing 10 μM Aβ42 in the presence and absence of a 3-fold molar excess of TTR-S. TTR-S was added before incubation (green), or after 18 hours of incubation (red). TTR-S alone (purple) and buffer (not. In this study, a water-soluble fluorogenic dye (i.e., Thioflavin T (ThT)) was employed to recognize RNA G-quadruplex structures using UV-Vis absorption spectra, fluorescence spectra and emission lifetime experiments. By stacking on the G-tetrad, the ThT probe exhibited highly specific recognition of RNA G-quadruplex structures with striking. Shop Thioflavin T, ACROS Organics™ at Fishersci.co.u Thioflavin T, CAS: 2390-54-7, is A cell-permeable dye capable of binding amyloid fibrils. MF: C17H19ClN2S, MW: 318.86. Cited in 3 publication
Detection of Aβ 1-40 aggregates using thioflavin T. As described previously , thioflavin T fluorescence was monitored for samples containing 10 μM thioflavin T solution in 40 mM Tris-HCl (pH 8.0). Fluorescence was measured on an LS-45 luminescence spectrometer (Perkin-Elmer, Waltham, MA) with excitation at 450 nm 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.
Shop Thioflavin T, ACROS Organics™ at Fishersci.ca. English Français; Sign Up for Email NEW soluble. Other solubilities: soluble in most organic solvent: Color: Ochre-Yellow to Yellow: Chemical Name or Material: Thioflavin T: Molecular Formula: C17H19ClN2S: Beilstein: 27, 377: Solubility Information: Solubility in water: soluble. Other. Thioflavin T is a widely used dye for visualizing and quantifying the presence of misfolded protein aggregates called amyloid, both in vitro and in vivo. MedKoo Biosciences, Inc. Tel: +1-919-636-5577 Fax: +1-919-980-4831 Email: sales@medkoo.co Thioflavin T Internal Standard for UV-VIS. Thioflavin T Internal Standard for UV-VIS, 18 ppm, CAS # 2390-54-7 in Water, 3.5 mL. $38.00. PART #: UV-413 Thioflavin T fluorescence specifically monitors amyloid fibrillation, whereas light scattering and 8-anilino-1-naphthalenesulfonate fluorescence monitor both amyloid fibrillation and amorphous aggregation. The amyloid fibrils formed via a nucleation-dependent mechanism in a supersaturated solution, analogous to crystallization
Thioflavin T, ACROS Organics™ Manufacturer: Thermo Fisher Scientific AC211761000 Solubility in water: soluble. Other solubilities: soluble in most organic solvent: Color: Ochre-Yellow to Yellow: Chemical Identifiers. CAS: 2390-54-7: Molecular Weight (g/mol) 318.863: InChI Key: JADVWWSKYZXRGX-UHFFFAOYSA-M Shop Thioflavin T, ACROS Organics™ at Fishersci.co.uk. Subject:* missing translation for 'pleaseEnterSubject'. Your Name:* missing translation for 'pleaseEnterYourName'. Your Email Address:* missing translation for 'pleaseEnterValidEmail'. missing translation for 'emailCopy Thioflavin-T binds to and detects amyloid fibrils via fluorescence enhancement. Using a combination of linear dichroism and fluorescence spectroscopies, we report that the relation between the emission intensity and binding of thioflavin-T to insulin fibrils is nonlinear and discuss this in relation to its use in kinetic assays. We demonstrate, from fluorescence lifetime recordings, that the. Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution. Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution Then the oligomers were mixed with variable amounts of freshly monomerized amyloid-β 1-40 with or without seeds (0.5% w/w of total soluble amyloid-β). Thioflavin T (20 μM) was added to.
Shop Thioflavin T, ACROS Organics™ at Fishersci.fi. Antibodies & Protein Biology Antibody Production & Purificatio 100 µM alpha synuclein protein monomer (SPR-321) seeded with 10µM alpha synuclein protein pre-formed fibrils (SPR-322) in 25 µM Thioflavin T (PBS pH 7.4, 100 µl reaction volume) generated a fluorescence intensity of 13,000 Relative Fluorescence Units after incubation at 37°C with shaking at 600 rpm for 24 hours
There remains a number of practical considerations, such as stability and the ability to control their arrangement. In this study, crude crystallin amyloid fibrils are shown to be stable in a range of biological and clean room solvents, with the fibril presence confirmed by transmission electron microscopy and the thioflavin T fluorescent assay We examined the effects of two polyphenols, i.e., epigallocatechin gallate (EGCG) and kaempferol-7-O-glycoside (KG), with high and low solubilities, respectively, on the amyloid formation of α-synuclein (αSN). EGCG and KG inhibited and promoted amyloid formation of αSN, respectively, when monitored by thioflavin T (ThT) fluorescence or. Thioflavin T (ThT) dye fluorescence is used regularly to quantify the formation and inhibition of amyloid fibrils in the presence of anti-amyloidogenic compounds such as polyphenols. However, in this study, it was shown, using three polyphenolics (curcumin, quercetin and resveratrol), that ThT fluorescence should be used with caution in the. Thioflavine S is a fluorescent histochemical marker of dense core senile plaques. Room temperature in continental US; may vary elsewhere. * ≥ means soluble, but saturation unknown. [1]. McLellan ME, et al. In vivo imaging of reactive oxygen species specifically associated with thioflavine S-positive amyloid plaques by multiphoton microscopy
, Crystal structure of thioflavin T bound to the peripheral site of Torpedo californica acetylcholinesterase reveals how thioflavin T acts as a sensitive fluorescent reporter of ligand binding to the acylation site. J. Am. Chem. Soc. 130, 7856 - 7861 (2008) The inclusion of thioflavin T (ThT) with p-sulfonatocalix[4]arene (p-SC4) is briefly discussed in solution as well as solid state. The restricted rotation of C−C single bond between indole and benzene ring system is the reason for emission property of ThT solubility. Furthermore, the size of DHLA-CDs is much larger than 6 nm. Different concentrations of these DHLA-CDs were added to human insulin to study the kinetics of its fibrillation. These samples were subsequently characterized by fluorescence spectroscopy of thioflavin T and circular dichroism spectroscopy. The morpholog For thioflavin T staining, we have followed the procedures from the recent publication (Polinski et al., 2018) with minor modifications. Cells were incubated with 20 μ m thioflavin T (Sigma-Aldrich) solution at RT for 30 min and washed in PBS three times. After staining, cell images were randomly captured using fluorescence microscopy (EVOS. In this study, Zaman et al., specifically address the basic aggregation mechanism of individual phenol-soluble modulins (PSMs), the structural scaffold of the pathogen S. aureus biofilms. The aggregation kinetics of individual PSMs (PSMα1-4, PSMβ1-2 and δ-toxin) was determined using the Thioflavin T (ThT) assay
Light-scattering and turbidity values indicate that β-sheet prion protein exists as soluble oligomers that increase thioflavin T fluorescence and bind to 1-anilino 8-naphthalene sulfonic acid (ANS). The oligomers are resistant to proteinase K digestion and during incubation for long periods they form linear amyloids > 5 μm long In fact, protofibrils isolated by size exclusion chromatography were completely stable and gave no disaggregation. A second class of soluble Aβ aggregates was generated rapidly (<10 min) in buffered 2% hexafluoroisopropanol (HFIP). These aggregates showed increased thioflavin T fluorescence and were rich in β-structure by circular dichroism Ultrafast torsional dynamics of Thioflavin-T in an anionic cyclodextrin cavity Journal of Photochemistry and Photobiology A-Chemistry , 298 ( 2015 ) , pp. 40 - 48 Article Download PDF CrossRef View Record in Scopus Google Schola However a small area is Thioflavin S-negative suggesting nonfibrillary protein (arrow). D, E, and F: Hippocampal blood vessel with perivascular Ab 338 staining, which is Thioflavin S-negative (arrow). G, H, and I: Hippocampal blood vessel with a good overlap between Thioflavin S and Ab 338 indicating fibrillar ABri
Recombinantly expressed SAA1 is soluble and lacks the amyloid structure as shown by weak interaction with amyloid binding dyes, such as thioflavin T or Congo red . The SAA1 batches used did not contain any relevant levels of endotoxin (< 0.2 EU/mg SAA1 protein) as assessed by EndoLISA ® (Hyglos, Bernried, Germany) Molecular analysis of the functional role of beta-adrenergic receptor kinase 1 amino-terminal. Molecular analysis of the functional role of beta-adrenergic receptor kinase 1 amino-terminal Metal ion stabilization of the conformation of a recombinant 19-kDa catalytic fragment of human fibroblast collagenase. Metal ion stabilization of the conformation of a recombinant 19-kDa catalytic fragment of human fibroblast collagenase Soluble In DMSO Chemical Structure Spectral Properties Excitation Wavelength 349 nm Emission Wavelength 454 nm Applications Thioflavin T (ThT), also called Basic Yellow 1 or CI 49005, is a benzothiazole salt. The dye is used to visualize plaques composed of beta-amyloid found in the brains of Alzheimer's disease patients Thioflavin T is a benzothiazole dye that increases in fluorescence upon binding to amyloid. Thioflavin T has been used in histology and for protein characterization. PHYSICAL AND CHEMICAL PROPERTIES. PHYSICAL STATE: yellowish powder: MELTING POINT : BOILING POINT : SPECIFIC GRAVITY : SOLUBILITY IN WATE
Solubility Soluble in DMF and DMSO STORAGE AND HANDLING: Stored desiccated at 4 °C upon receipt. APPLICATION: A cell-permeable benzothiazole dye that exhibits enhanced fluorescence upon binding to amyloid fibrils. Useful in monitoring stacked β sheet aggregates. Thioflavin T has also been used in histology and for protein characterization thioflavin T. focusing on the decrease in stability and solubility of the protein. HEWL, comprising 129 amino acid residues, is a basic protein with isoelectric point (pI) of ∼11.2 and a net charge of +19 at pH < 3 that forms well-defined amyloid fibrils under acidic conditions ated via thioflavin T fluorescence, isolated via centrifuga-g), resuspended in 40 mM Tris-HCl (pH 8.0), and stored at 4°C for up to 1 week. Detection of A 1-40 aggregates using thioflavin T As described previously [6], thioflavin T fluorescence was monitored for samples containing 10 M thioflavin T solution in 40 mM Tris-HCl (pH 8.0. Herein, we utilize thioflavin T (ThT) as an efficient fluorescent ligand for ABA27 to devise a label-free ATP sensor, introducing a novel strategy for the signal readout. ThT is a commercially available water-soluble benzothiazole dye previously used to probe amyloids [ 20, 21 ], with a weak fluorescent emission in the unbound state
Thioflavin T (ThT; 4-(3,6-dimethyl-1,3-benzothiazol-3-ium-2-yl)-N,N-dimethylaniline chloride), is a well-known fluorescence probe used for detecting amyloid fibrils . Upon binding to fibrils, ThT displays a dramatic shift of excitation maximum (from 385 to 450 nm) and emission maximum (from 445 to 492 nm) ( 22 , 23 ), resulting in an increase. Thioflavin T (ThT) was incorporated in amyloid fibers and displays an enhanced fluorescence (Ex 440nm/Em 480nm). ATP-Mg or nonhydrolysable APPCP-Mg prevented formation of amyloid fibers of Aß42 peptide (E) and the prion domain of the yeast Mot3 protein (Mot3-PrD) (F) in a concentration-dependent manner process was monitored via Thioflavin T (ThioT) fluorescence. Interestingly, sumoylation of -synuclein completely abolished fibril formation even after 146 h of incubation (Fig. 2, A-C). In contrast, the presence of equimolar amounts of nonconjugated SUMO did not prevent fibril formation (Fig. 2, A, B, and D) indicated by light scattering, thioflavin T fluorescence, and transmission electron microscopy analysis. Increased 1-anilinonaphthalene-8-sulfonate binding to the proteins was also observed, indicating exposure of hydrophobic surface area. Thus, pressure appears to induce a conformational state of lysozyme that aggregates readily upon.
Among these dyes for G-quadruplex, thioflavin T (ThT) has increasingly attracted the attention of researchers to become a new focus in the construction of G-quadruplex fluorescent biosensors, mainly due to its satisfactory water solubility and low cost.27 Compared to conventional dyes, such a Highly efficient soluble expression, Finally, thioflavin T fluorescence and atomic force microscopy revealed that the recombinant Aβ42 aggregated into long, branched fibrils. Furthermore, the aggregates of the recombinant peptide had a strong cytotoxic effect on PC12 cells. The method described here can therefore be used to efficiently. @article{osti_1005699, title = {Molecular Mechanism of Thioflavin-T Binding to the Surface of [beta]-Rich Peptide Self-Assemblies}, author = {Biancalana, Matthew and Makabe, Koki and Koide, Akiko and Koide, Shohei and UC)}, abstractNote = {A number of small organic molecules have been developed that bind to amyloid fibrils, a subset of which also inhibit fibrillization Thioflavin T is a cell-permeable benzothiazole dye that exhibits enhanced fluorescence upon binding to amyloid fibrils. Thioflavin T is useful in monitoring stacked β sheet aggregates. Solubility. Methanol: soluble1 mg/mL. Composition. Dye content, 65-75%. Safety Information Thioflavin T (ThT) is a fluorescent dye commonly used to stain amyloid plaques, but the binding sites of this dye onto fibrils are poorly characterized. We present molecular dynamics simulations of the binding of ThT and its neutral analog BTA-1 [2-(4′-methylaminophenyl)benzothia-zole] to model protofibrils of the Alzheimer's disease A
RNA G-quadruplexes (G4s) play important roles in translational regulation, mRNA processing events and gene expression. Therefore, a fluorescent probe that is capable of efficiently recognizing RNA G-quadruplex structures among other RNA forms is highly desirable. In this study, a water-soluble fluorogenic dye (i.e., Thioflavin T (ThT)) was employed to recognize RNA G-quadruplex structures. Aggregation studies of α-SN proteins using thioflavin T (ThT) fluorescence α-SN in 10 mM phosphate buffer, pH 7.4, was filtered to ensure removal of preformed aggregates (0.2 μm Minisart RC4 filters, Sartorius, Goettingen, Germany) and then incubated a
Here we describe a simplified polyglutamine assay that uses a soluble, pathological-length polyglutamine construct (62 glutamines [Q62]) fused to glutathione-S-transferase (GST) and measure aggregate formation with fluorescence generated by thioflavin T binding. Controlled release of Q62 from GST using proteolytic cleavage resulted in time. The aptitude of NT* to control β17 fibrillization was measured by fibril formation kinetic assay using the amyloid binding dye Thioflavin T (ThT) as a reporter (Fig. 4A-B). The fluorescence intensity of NT* or thrombin alone was kept at baseline, showing that neither the solubility tag nor the protease bind ThT (data not shown)
class of soluble A aggregates was generated rapidly (<10 min) in buffered 2% hexafluoroisopropanol (HFIP). These aggregates showed increased thioflavin T fluorescence and were rich in -structure by circular dichroism. Elec-tron microscopy and atomic force microscopy revealed initial globular clusters that progressed over several day Aggregation of tau proteins was evaluated with a thioflavin T assay. 10 μM of tau protein was mixed with 20 mM Tris pH 7.5 containing 100 mM NaCl, 1 mM EDTA, 1 mM DTT, 0.03 mg/mL heparin sodium salt and 30 μM thioflavin T. Aggregation signal was measured every 30 min for a total duration of 40 h using a fluorescence plate reader (EX: 450 nm. 2.4. Thioflavin-T Fluorescence Assay. Although much work has been done with Thioflavin-T to study the kinetics of aggregation and fibrillization, we are limited in the use of this dye because of the very strong fluorescent signal emitted by the oil palm phenolics at the wavelength of 535 nm, following excitation at a wavelength of 450 nm
We demonstrate for the first time the application of a water-soluble fluorogenic dye, Thioflavin T (ThT), in a dual role of exclusively inducing quadruplex folding in the 22AG human telomeric DNA, both in the presence and absence of Tris buffer/salt, and sensing the same through its fluorescence light-up having emission enhancement of the order. Thioflavin T dimers linked by short oligoethylene glycol chains were previously found to have enhanced affinity for Aβ40 aggregates. 9 Thioflavin T is charged, which limits biological applications of these compounds, so we have applied this approach to the neutral benzothiazole aniline head group 1 . 10 Benzothiazole anilines (BTA) are.
Thioflavin T. Thioflavin T is a widely used dye for visualizing and is a cationic Benzothiazole dye that shows enhanced fluorescence upon binding to amyloid in tissue sections. Toluidine Blue. Toluidine Blue is a photosensitizer gel, which can make the medicine stay on the diseased part and improve the treatment effect Thioflavin-T, trypsin, DNase I, and cytosine arabinofuranoside (Ara-C) were bought from Sigma (St Louis, MO, USA). NeuroTrace 500/525 green-fluorescent Nissl stain was from Invitrogen (Carlsbad, CA, USA). The other reagents were obtained from standard sources and were of analytical grade or higher. Preparation of A Among these, the benzothiol dye Thioflavin-T (ThT) has been used for decades in the diagnosis of protein-misfolding diseases and in kinetic studies of self-assembly (fibrillization). Despite its importance, efforts to characterize the ThT-binding mechanism at the atomic level have been hampered by the inherent insolubility and heterogeneity of.