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Ultrafast bond twisting dynamics in amyloid fibril sensor
Prabhat K Singh1, Manoj Kumbhakar, Haridas Pal
1Radiation & Photochemistry Division, Bhabha Atomic Research Centre, Trombay, Mumbai 400 085, India.
The Journal of Physical Chemistry. B
|January 26, 2010
Summary
Ultrafast spectroscopy revealed that Thioflavin T (ThT) uses bond twisting to sense amyloid fibrils. This twisting process, crucial for ThT
Area of Science:
- Photochemistry
- Biophysical Chemistry
- Spectroscopy
Background:
- Thioflavin T (ThT) is a widely used dye for detecting amyloid fibrils.
- Its fluorescence sensing mechanism relies on a fundamental process involving bond twisting.
Purpose of the Study:
- To elucidate the ultrafast bond twisting dynamics of Thioflavin T.
- To understand the role of these dynamics in amyloid fibril sensing.
Main Methods:
- Ultrafast time-resolved fluorescence spectroscopy.
- Wavelength-dependent fluorescence decay kinetics.
- Time-resolved emission spectra (TRES) analysis.
- Quantum chemical calculations.
Main Results:
- Photoexcitation of ThT induces subpicosecond bond twisting, forming a weakly emissive twisted intramolecular charge-transfer state.
- Twisting around the central C-C bond is primarily responsible for the observed dynamics.
- Amyloid fibril incorporation significantly retards this bond twisting process.
Conclusions:
- The study reveals the fundamental bond twisting mechanism underlying Thioflavin T's fluorescence sensing.
- Retarded dynamics in fibrils suggest this process is key to ThT's sensor activity.
- Findings provide molecular insights into amyloid detection using ThT.
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