Evaluation of in vitro inhibitory effects of some natural compounds on tyrosinase activity and molecular docking study: Antimelanogenesis potential

Abstract

Tyrosinase enzyme is a functional oxidase that is extensively divided in nature. It is the main enzyme in melanin synthesis and is also involved in designating the color of mammalian hair and skin. Additionally, it is accountable for the unfavorable enzymatic browning that happens in plant‐derived foods, limiting the shelf‐life of new‐cut crops with the resultant economic harm. Recently, there has been a remarkable concern to study the inhibitory activity of the tyrosinase enzyme and some inhibitory molecules isolated from natural sources. For tyrosinase enzyme, afzelin, narcissoside, justiciresinol, thalassiolin B, carpachromene, neobavaisoflavone, and kojic acid (as standard) as natural phenols have IC50 values in the range of 2.37‐7.90 µM. Theoretical methods, such as gaussian software program and molecular modeling, were used to compare the biological and chemical activity values of molecules. To compare the biochemical and chemical activity values of molecules, chemical activities with quantum chemical parameters, and biological activities against tyrosinase with the ID of 5M8L molecules were investigated.

A Rare Dirhamnosyl Flavonoid and Other Radical‐Scavenging Metabolites from Cynophalla mollis (Kunth) J. Presl and Colicodendron scabridum (Kunt) Seem. (Capparaceae) of Ecuador

“…In particular, 9 is able to significantly inhibit some enzymes, such as acetylcholinesterase (AChE), α‐glycosidase and tyrosinase. An anti‐acute myeloid leukemia activity, probably related to the antioxidant properties, has also been claimed [42] . On the other hand, the dirhamnoside 5 exerted a null antioxidant activity in DPPH assay, but a strong scavenging capacity in ABTS test, with SC 50 values >1682 μM and 46.10 μM, respectively.…”

New quinoxalin‐1,3,4‐oxadiazole derivatives: Synthesis, characterization, in vitro biological evaluations, and molecular modeling studies

“…These are key components of cholinergic brain synapses and neuromuscular connections. [ 38–40 ] The main function of AChE and BChE is to catalyze the hydrolysis of the neurotransmitter ACh and nerve impulse termination at cholinergic synapses. Thus, compounds acting as cholinesterase inhibitors can be considered potential drugs in the treatment of AD, other neurological disorders, and as therapeutic agents.…”

Health Potential of Clery Strawberries: Enzymatic Inhibition and Anti-Candida Activity Evaluation

“…The tyrosinase enzyme, catalyzing the initial conversion of L-tyrosine in L-dopa and the subsequent oxidation in dopaquinone, which polymerizes producing melanin, is also involved in degenerative processes [11]. Implicated in the onset of the skin melanomas and in the increase of neuromelanin in nigral dopaminergic neurons, it was observed in higher contents in elderly humans and, moreover, in Parkinson's patients [12].…”

“…Implicated in the onset of the skin melanomas and in the increase of neuromelanin in nigral dopaminergic neurons, it was observed in higher contents in elderly humans and, moreover, in Parkinson's patients [12]. Taslimi et al [11] evaluated the anti-melanogenesis potential of different molecules obtained by natural sources, evidencing that natural phenols exerted significant inhibition activity towards tyrosinase enzyme (IC 50 values ranging between 2.37 and 7.90 µM).…”