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Updated: May 11, 2026

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein
Published on: January 2, 2015
Thioflavin-T excimer formation upon interaction with amyloid fibers
Raimon Sabate1, Luis Rodriguez-Santiago, Mariona Sodupe
1Institut de Nanociència i nanotecnologia, Departament Fisicoquímica, Universitat de Barcelona, Joan XXIII s/n, E-08028-Barcelona, Spain. rsabate@ub.edu
The mechanism of Thioflavin-T (Th-T) binding to amyloids is unclear. Our study suggests Th-T fluorescence changes result from excimer formation with a ~120-degree angle upon amyloid interaction.
Area of Science:
- Biophysics
- Chemical Biology
- Molecular Biology
Background:
- Amyloid proteins are implicated in neurodegenerative diseases.
- Thioflavin-T (Th-T) is a fluorescent dye used to detect amyloid fibrils.
- The precise mechanism of Th-T's interaction with amyloids is not fully understood.
Purpose of the Study:
- To elucidate the molecular mechanism of Thioflavin-T (Th-T) binding to amyloid structures.
- To explain the observed changes in Th-T fluorescence spectra upon interaction with amyloids.
Main Methods:
- Experimental analysis of Th-T excitation and emission spectra.
- Theoretical calculations to model Th-T-amyloid interactions.
- Spectroscopic studies combined with computational modeling.
Main Results:
- Th-T fluorescence changes upon binding to amyloids.
- Evidence suggests the formation of a Th-T excimer.
- The proposed excimer structure has an oblique angle of approximately 120 degrees.
Conclusions:
- The study proposes a novel mechanism for Th-T fluorescence changes.
- Excimer formation with a specific geometry explains Th-T spectral shifts.
- This finding advances our understanding of amyloid detection methods.
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