Egg-Curry: Insights into the Interaction Between Curcumin and Ovalbumin Using Spectroscopic Analyses and Protein-Ligand Docking Simulations

We investigate the interaction between curcumin and ovalbumin using spectroscopic analyses and protein-ligand docking simulations. The fluorescence intensity of ovalbumin decreased upon complexation with curcumin through a static quenching mechanism. The binding constant for curcumin-ovalbumin complex was in the order of 10(4) M-1 suggesting a stable complex with 1:1 stoichiometry. Both FTIR spectroscopy and molecular docking simulations revealed that hydrogen bonding (Lys39) and hydrophobic interactions (Phe35) were the major interaction forces in the binding of curcumin to ovalbumin. The aqueous solubility of curcumin was enhanced (234-fold) by complexation with ovalbumin while the degradation of curcumin in aqueous solutions was significantly diminished (0.25-fold) in the wide range of pH (1.2-8.5). The physicochemical properties of curcumin were stably maintained for 12 h by the complexation. This work provides an insight into the binding mechanism of small chemicals and large biomolecules for medicines and functional foods.

Automated summary

This study investigated the interaction between curcumin and ovalbumin, revealing a stable complex formation with maintained physicochemical properties of curcumin. The complexation with ovalbumin significantly enhanced the aqueous solubility of curcumin and reduced its degradation in aqueous solutions over a wide range of pH. The study provides insights into the binding mechanisms of small chemicals and large biomolecules for medicinal and functional food applications.