IN SILICO DESIGINING OF ANTITYROSINASE PEPTIDESJ. USHA RANI, B. SIVA PRASAD, S.S. VUTUKURU, G. JAYASREE AND CHAND PASHA
Tyrosinase enzyme plays crucial role in melanin synthesis. Biological role and signficance of tyrosinase in treating hyperpigmentation disorders, cancer, and neuro degenerative diseases are gaining promincence in medicine and cosmeceutics. In recent times, chemical tyrosinase inhibitors raised questions about their adverse effects on humans. It necessiates the development of natural and unique stable antityrosinase molecules with no toxicity. Natural peptides have the potential to inhibit tyrosinase. Small peptides showed meagre adverse effects on humans. In silico approaches enable in determining inhibitory activity of peptides for a given biological target. In this context, present study is designed to predict the molecular interctions of small peptides to predict their tyrosinase inhibiiton potential using molecular docking. Tertiary structure of human tyrosinase protein is carried out by homology modeling using Discovery Studio 2.1. Kojic acid and and peptides were docked with modeled human tyrosinase. The homology modelling was used to determine the 3D structure of tyrosinase. Kojic acid, peptide1 and peptide 4 (chimer) were docked into active site pocket of human tyrosinase using Lib Dock and ZDOCK modules in Accelry's Discovery studio 2.1. Highest docking score for a chimer peptide showed higher anti-tyrosinase potential when compared to peptide 1 (control). Hence chimeric peptide be used in the designing of effective drugs for hyperpigmentation treatment. Thus 3D structure of human tyrosinase and docking studies of peptides conducted in the present study enable further understanding the tyrosinase inhibition by novel peptides.
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