Zohreh Jamali - Department of Chemistry, Science and Research Branch, Islamic Azad University, Tehran, Iran
Nematollah Gheibi - Cellular and Molecular Research Center, Qazvin University of Medical Sciences, Qazvin, Iran

The esreification chrysin with n-3 poly unsaturated fatty acids (complex I) resulted to design of new MT inhibitor. Thermodynamic parameters of enzyme including melting point (Tm) and ΔG values also obtained from thermal and chemical denaturation curves. Complex I showed a competitive inhibitory effect on mushroom tyrosinase with a Ki of 0.45. The Tm values were calculated 328.6, 322.4 K, and ΔG values of 62.8, 52.9 KJ.mol-1 were recorded for sole enzyme and its interaction with complex I, respectively. The intrinsic and extrinsic fluorescence techniques, showed structural instability of enzyme in concomitance with reduction in regular secondary structure acquired using CD spectrometry. Our data clearly proved that new derivative showed stronger inhibitory effect than the separate compounds. The Molecular docking analysis showed that the interaction between enzyme and complex I obeyed from hydrophobic nature.

Mushroom Tyrosinase, Chrysin, Fatty acid, Molecular docking, Inhibition