Login

Journal Image
Current Topics in Medicinal Chemistry
ISSN (Print): 1568-0266
ISSN (Online): 1873-5294
VOLUME: 14
ISSUE: 12
DOI: 10.2174/1568026614666140610121253      Price:  $58









In Silico Approach to Inhibition of Tyrosinase by Ascorbic Acid Using Molecular Docking Simulations

img
Author(s): F. Sezer Senol, M. Tareq Hassan Khan, Gurdal Orhan, Erdem Gurkas, Ilkay Erdogan Orhan, Nese Subutay Oztekin and Fikri Ak
Pages 1469-1472 (4)
Abstract:
Current evidence suggests that endogenous dopamine may act as a neurotoxin following its oxidation to an oquinone and reaction with cellular thiols, which are neutoxic, which may occur spontaneously or via reaction with tyrosinase or some other enzymes. Tyrosinase (E.C. 1.14.18.1) with two cupper ions coordinated by three histidines is a bifunctional enzyme that catalyses both the hydroxylation of tyrosine to L-DOPA and the consequent oxidation of the resulting catechol-containing species to an o-quinone. Therefore, tyrosinase may play a role in neuromelanin formation in the brain and could be central to dopamine neurotoxicity by contributing to the neurodegeneration associated with Parkinson’s disease. In the present study, inhibitory effect of ascorbic acid against tyrosinase has been investigated and it has shown a remarkable inhibitory effect in in vitro assays. Then, the in silico-based experiments established through molecular docking calculations and scoring, docking search algorithm, and data plotting indicated that ascorbic acid is strong inhibitor of tyrosinase by interacting with four amino acid units (histidine 263, serine 282, phenylalanine 264, and valin 283) in the active site of the enzyme. The compound also had two long distant hydrogen bindings with Cu1 and Cu2 with distances of 3.57 and 3.41 A, respectively, through its O5 atom.
Graphical Abstract:
Keywords:
Ascorbic acid, in silico, in vitro, molecular docking, tyrosinase inhibition, vitamin C.
Affiliation:
Department of Pharmacognosy, Faculty of Pharmacy, Gazi University, 06330 Ankara, Turkey.