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Published on: March 28, 2017
Interaction of thyroxine with 7 hydroxycoumarin: a fluorescence quenching study
Elmas Gök1, Canan Oztürk, Nuriye Akbay
1Department of Chemistry, Hacettepe University, 06800, Beytepe, Ankara, Turkey. gokoglu@hacettepe.edu.tr
Journal of Fluorescence
|June 5, 2008
Summary
Thyroxine hormone interacts with 7 hydroxycoumarin (7HC), quenching its fluorescence via static quenching. This interaction, driven by hydrogen bonds and van der Waals forces, allows for sensitive thyroxine detection.
Area of Science:
- Biochemistry
- Analytical Chemistry
Background:
- Thyroxine is a crucial thyroid hormone regulating metabolism.
- 7 hydroxycoumarin (7HC) is a fluorescent compound with potential applications in molecular sensing.
Purpose of the Study:
- To investigate the interaction between thyroxine and 7HC.
- To develop a fluorescence-based method for thyroxine detection.
Main Methods:
- Fluorescence quenching spectroscopy was employed to study the binding interaction.
- The 7HC-thyroxine complex formation was analyzed using static quenching mechanism.
- Thermodynamic parameters were calculated to elucidate binding forces.
Main Results:
- Thyroxine induced static quenching of 7HC fluorescence, indicating complex formation.
- Binding constants (K) were determined at different temperatures (1.51 x 10^4 at 297 K, 9.06 x 10^3 at 310 K).
- The interaction is primarily mediated by hydrogen bonding and van der Waals forces.
- A linear calibration curve for thyroxine was established in the range of 2.0 x 10^-8 to 3.0 x 10^-7 mol/l.
- The method demonstrated good precision (RSD 2.58%) and a low limit of detection (3.42 x 10^-8 mol/l) in CTAB medium.
Conclusions:
- The fluorescence quenching method provides a sensitive and reliable approach for thyroxine determination.
- The study elucidates the molecular interaction mechanism between thyroxine and 7HC.

