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Azami, F., Tazikeh-Lemeski, E., Mahmood-Janlou, M. (2017). Kojic Acid Effect on the Inhibitory Potency of Tyrosinase. Journal of Chemical Health Risks, 7(2), -. doi: 10.22034/jchr.2017.544176
Forogh Azami; Elham Tazikeh-Lemeski; Mehr-Ali Mahmood-Janlou. "Kojic Acid Effect on the Inhibitory Potency of Tyrosinase". Journal of Chemical Health Risks, 7, 2, 2017, -. doi: 10.22034/jchr.2017.544176
Azami, F., Tazikeh-Lemeski, E., Mahmood-Janlou, M. (2017). 'Kojic Acid Effect on the Inhibitory Potency of Tyrosinase', Journal of Chemical Health Risks, 7(2), pp. -. doi: 10.22034/jchr.2017.544176
Azami, F., Tazikeh-Lemeski, E., Mahmood-Janlou, M. Kojic Acid Effect on the Inhibitory Potency of Tyrosinase. Journal of Chemical Health Risks, 2017; 7(2): -. doi: 10.22034/jchr.2017.544176

Kojic Acid Effect on the Inhibitory Potency of Tyrosinase

Article 8, Volume 7, Issue 2, Spring 2017  XML PDF (550.14 K)
DOI: 10.22034/jchr.2017.544176
Authors
Forogh Azami email 1; Elham Tazikeh-Lemeski2; Mehr-Ali Mahmood-Janlou1
1Department of Biology, Gorgan Branch, Islamic Azad University, Gorgan, Iran
2Department of Chemistry, Gorgan Branch, Islamic Azad University, Gorgan, Iran
Receive Date: 26 April 2017,  Revise Date: 11 December 2019,  Accept Date: 29 October 2018 
Abstract
In recent years, enzymatic activity of tyrosinase has been the focus of investigation due to its potential applications in medicine, agriculture and cosmetics. Tyrosinase, entitled polyphenol oxidase, is a key enzyme that catalyzes synthesis of melanin in plants, microorganisms and mammalian cells. Presence of some antioxidants can delay or inhibit the activity of this enzyme as well. In this survey, molecular docking calculation method using Autodock 4.0 software for prediction of binding energy of the protein with some antioxidant ligands was executed. The pose with the lowest energy of binding or inhibition constant was extracted at 298.15 K for kojic acid. Number of conformations in the cluster of rank was 13. The first and second boxes free energy and the inhibition constant were as follows: -5.60 kcalmol-1, 78.99 µM and -3.32 kcalmol-1, 3.66 µM, respectively. Since the first box presented a lower value of free energy, it was considered as the best mode of structure of kojic acid and the protein docking for further analysis. Thus, our present study could contribute to development and discernment of tyrosinase inhibitors in order to prevent hyper pigmentation.
Keywords
Tyrosinase; Molecular docking; Kojic acid; Binding Energy; Inhibition Constant
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