Molecular docking studies of embelin (simple natural benzoquinone) and its derivatives as a potent tyrosinase inhibitor

N. Radhakrishnan, S. Ashok, V.

Abstract

In recent years regulation of the enzymatic activity of tyrosinase has been the main focus of investigation due to its potential applications in medicine, agriculture and cosmetics. In the present study, we evaluated its docking behaviour of nine different ligands (such as Coenzyme Q10, L-DOPA, Embelin, Idebenone, Kojic acid, 5-Methyl embelin, Potassium embelate, L-Tyrosine and Vilangin)with the copper-bound Streptomyces castaneoglobisporus tyrosinase & Agaricus bisporus (Mushroom tyrosinase). Autodock 4.0 tool was used to investigate its putative binding residues. Molecular physicochemical and the drug-likeness studies reveal that L-DOPA, Kojic acid and LTyrosine complies very well with thumb rule of five. With regard to affinity and binding energy calculationswith the targeted protein (Streptomyces castaneoglobisporus tyrosinase), kojic acid showed least affinity value -3.52 kcal/mol, compared to other chosen ligands. Similarly, in case of Agaricus bisporus (Mushroom tyrosinase), embelin showed least affinity value of -6.56 kcal/mol, compared to all other ligands. Thus, our present molecular docking studies could contribute for the further, development and understanding of tyrosinase inhibitors for the prevention of hyper pigmentation.