Molecular docking studies of L-cysteine (a non-essential sulfur containing aminoacid) as a potent Tyrosinase inhibitor

Abstract

L-cysteine enhances resistance (anti-static) and stimulates the growth of hair and nails. In otherwords, it is regard as hair and nails revitalizing agent. In addition, it is required for the biosynthesis of trypanothione, coenzyme -A, hypotaurine, taurine as well as ubiquitous iron-sulfur (Fe-S) clusters, which are involved in electron transfer, redox regulation, nitrogen fixation, and sensing for regulatory processes. In the present study, we calculated molecular physicochemical and drug-likeness properties of L-cysteine using molinspiration online tool. In addition, we evaluated L-cysteine docking behavior with the copper-bound Streptomyces castaneoglobisporus tyrosinase and investigated its putative binding residues using Autodock 4.0. The study results reveal that L-cysteine complies very well with thumb rule of five. With reference to docking studies, L-cysteine exhibits lowest binding energy of -3.15 kcal/mol and its putative binding residues were Arginine, Glutamic acid and Tryptophan (at 55th, 182th & 184th position) respectively. Thus, our present molecular docking studies could contribute for the further, development of tyrosinase inhibitors for the prevention of hyper pigmentation.