Investigating resveratrol-lipase interactions through multispectral analysis and molecular docking studies

Area of Science:

• Biochemistry
• Molecular Biology
• Pharmacology

Background:

• Resveratrol (RES), a natural polyphenol, exhibits diverse pharmacological effects.
• RES has demonstrated potential in regulating lipid metabolism.
• Lipase (LPS) plays a crucial role in lipid metabolism.

Purpose of the Study:

• To quantitatively characterize the interaction mechanism between Resveratrol and Lipase.
• To elucidate the binding mode and thermodynamic parameters of RES-LPS interaction.
• To provide a mechanistic understanding of RES's role in lipid metabolism.

Main Methods:

• Multispectral techniques including fluorescence quenching and UV-vis spectroscopy.
• Circular dichroism (CD) spectroscopy to analyze protein structural changes.
• Molecular docking simulations to predict binding sites and affinity.

Main Results:

• Fluorescence quenching indicated static binding with a binding constant (KA) of 7.499 × 10^5 L·mol^-1 at 298 K.
• Thermodynamic analysis revealed spontaneous, exothermic binding driven by hydrogen bonds and van der Waals forces.
• Molecular docking identified key binding residues and a binding free energy of -3.86 kcal·mol^-1, consistent with experimental data.

Conclusions:

• Resveratrol binds to Lipase, inducing changes in its secondary structure.
• The interaction is spontaneous and primarily mediated by hydrogen bonds and van der Waals forces.
• This study provides a mechanistic basis for Resveratrol's lipid metabolism-modulating effects and potential therapeutic applications.