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
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: 23 July 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.
Keshavarzi S., Atefi A., Familiar with antioxidants. Center for Blood Research, cancer and genetics martyr Yazd University of Medical Sciences.
Mohamadi Samani S., 2007. A review of health products. Shiraz University of Medical Sciences.
Dadkhah M., 2010. Tyrosinaz enzymes produced by the fungus review Neurospora crassa. Thesis. PNU.
Radhakarishnan N., Ashok S., Kaviha V., Eshkumar G.Ra. Gnanamani A., 2013. Molecular Docking Studies of Emblin (simple natural benzoquinone) and its derivatives as a potent Tyrosi-nase inhibitor. J Chem Pharm Res. 5(10), 320-326.
Pekkarinen S.S., Heinonen I.M., Hopia A.I., 1999. Flavonoids quercetin, myricetin, kaempferol and (+) catechin as antioxidants in methyl linoleate. J Sci Food Agri. 79, 499âââ506.
Guo C., Yang J., 2003. Antioxidant activities of peel, puipand seed fractions of common fruits as determined by FRAP assay. Nutr Res. 23,1719-1726.
Smit N., Vicanova J., Pavel S., 2009. The Hunt for Natural Skin Whitening AgentsInt J Mol Sci. 10(12), 5326-5349.
Vardhana A., Shabina Khanb Bhawana P., 2014. Screening of plant parts for anti-tyrosinase activity by tyrosinase assay using mushroom tyrosinase. Indian J Sci Res. 4(1), 134-139.
Sariri R., Sabbaghzadeh R., Poumohamad F., 2011. In-Vitro Antioxidant and Anti-Tyrosinase Activity of Methanol Extracts from Crocus Sativus Flowers Pharmacologyonline 3, 1-11.
Ribeird lima C., Rogerio J., silva A., De tassia E., Cardoso C., silva edilene O., 2014. Combined kinetic studies and computational analysis on kojic acid analogs as tyrosinase inhibitors. Molecules. 19, 9591-9605.
Rauniyar R., Talkad M.S., Sahoo S., Singh A., Harlalka P., 2014. Anti-Tyrosinase Activity of Stachytarpheta Cayennensis in Vitro. Int J Innovative Res Sci Engin Technol. 3(7), 14259-14266.
Salleh W., Ahmad F., Heng Yen K., 2014. Antioxidant and Anti-tyrosinase Activities from Piper officinarum. J Appl Pharma Sci. 4(5), 87-91.
Alam N., Nam Yoon K., Rim Lee K., Gyun Shin P., Chun Cheong J., 2010. Antioxidant Activities and Tyrosinase Inhibitory Effects of Different Extracts from Pleurotus ostreatus Fruiting Bodies. Microbiology. 38(4), 295-301.
Si Y.X., Yin S.J., Park D., Chung H.Y., Yan L., Lü Z.R., Zhou H.M., Yang J.M., Qian G.Y., Park Y.D, 2011. Tyrosinase inhibition by isophthalic acid: Kinetics and computational simulation. Int J Biol Macromol. 48, 700âââ704.
Si X., Wang Z.J., Park D., Chung H.Y., Wang S.F., Yan L., Yang J.M., Qian G.Y., Yin S.J., Park Y.D, 2012. Effect of hesperetin on tyrosinase: Inhibition kinetics integrated computational simulation study. Int J Biol Macromol. 50, 257âââ262.
Liu X.X., Sun S.Q., Wang Y.J., Xu W., Wang Y.F., Park D., Zhou H.M., Han H.Y, 2013. Kinetics and computational docking studies on the inhibition of tyrosinase induced by oxymatrine. Appl Biochem Biotechnol. 169, 145âââ158.
Ismaya W.T., Rozeboom H.J., Weijn A., Mes J.J., Fusetti F., Wichers H.J., Dijkstra B.W 2011. Crystal Structure of Agaricus Bisporus Mushroom Tyrosinase: Identity of the Tetramer Subunits and Interaction with Tropolone. Biochemistry. 50, 5477.
The Molinspiration Database. [http://www.molinspiration.com].
Gasteiger J., Marsili M., 1980. Iterative partial equalization of orbital electronegativityâââa rapid access to atomic charges. Tetrahedron. 36, 3219âââ3228.
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