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

Resveratrol (RES), a natural polyphenol with diverse pharmacological properties, has shown potential in modulating lipid metabolism through interactions with lipase (LPS). This study employed multispectral techniques and molecular docking to characterize the RES-LPS interaction mechanism quantitatively. Fluorescence quenching analysis revealed static quenching with a binding constant (<i>K_A</i>) of 7.499 × 10⁵ L·mol^-1 at 298 K, supported by thermodynamic parameters (Δ<i>G</i> = -40.43 kJ·mol^-1, Δ<i>H</i> = -44.26 kJ·mol^-1, Δ<i>S</i> = -135.5 J·mol^-1·K^-1), indicating spontaneous, exothermic binding driven by hydrogen bonds and van der Waals forces. UV-vis spectroscopy demonstrated a 2 nm redshift in LPS's absorption peak, confirming complex formation. Circular dichroism revealed RES-induced secondary structural changes in LPS, with α-helix content decreasing from 17.2% to 17.0% and random coils increasing from 41.6% to 42.9%. Molecular docking identified key binding residues (ARG256, ASP79, TRP252) and a binding free energy of -3.86 kcal·mol^-1, validating the experimental findings. These results provide a mechanistic basis for RES's role in lipid metabolism regulation and its potential therapeutic applications.