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Interaction between resveratrol and thrombin and its biological implication.

Juan Zhang¹, Wen-Juan Yu, Nana Yang

¹School of Life Sciences, Shanghai University, Shanghai, PR China.

International Journal of Food Sciences and Nutrition

|October 6, 2011

Summary

Resveratrol interacts with thrombin, reducing its fluorescence and altering its structure. This interaction may inhibit platelet aggregation and stimulate apoptosis, highlighting resveratrol

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Area of Science:

Biochemistry
Molecular Biology
Pharmacology

Background:

Resveratrol and thrombin play key roles in platelet aggregation and apoptosis.
Understanding their interaction is crucial for elucidating biological implications.

Purpose of the Study:

To investigate the interaction between resveratrol and thrombin.
To explore the biological consequences of this interaction on platelet function.

Main Methods:

Fluorescence spectroscopy to study quenching mechanisms and binding kinetics.
Analysis of thermodynamic parameters (hydrophobic interactions, hydrogen bonding).
Circular dichroism to assess changes in protein secondary structure (α-helical content).

Main Results:

Resveratrol dynamically quenches thrombin fluorescence via collision.
Complex formation is spontaneous, endothermal, driven by hydrophobic interactions and hydrogen bonds.
Non-radiative energy transfer occurs from thrombin to resveratrol.
Thrombin conformation alters, with a decrease in α-helical structure.
Resveratrol stability is enhanced by thrombin, without preventing isomerization.

Conclusions:

Resveratrol interacts with thrombin, leading to structural changes and altered fluorescence.
This interaction may underlie resveratrol's potential to inhibit platelet aggregation and promote apoptosis.
Findings offer insights into resveratrol's role as a functional food ingredient.