Bond-Based 2D Quadratic Fingerprints in QSAR Studies. Virtual and In Vitro Tyrosinase Inhibitory Activity Elucidation

Tyrosinase inhibition is an important approach towards controlling hyper pigmentation. We aimed to screen alcoholic extracts of 11 plants extract for their tyrosinase inhibitory activity. These plants have been used traditionally in the treatment of skin ailments and for the improvement of skin complexion. The extracts were quantified for total phenols, alkaloids and tannins. In vitro tyrosinase inhibition was performed with kojic acid as the positive control. Cell viability was tested on B16 F0 melanoma cells. The extracts of Rosa berberifolia, Punica granatum and Casiia angustifolia showed more than 80% inhibition at 500 mg/ml concentration. Nine of the extracts were also shown to have a high phenolic content greater than 200 mg/g of the plant material. The tyrosinase inhibitory activity of the extracts of Cassia angustifolia, Punica granatum and Rosa berberifolia were comparable with that of the control, kojic acid. The three extracts also showed lesser than 50% cytotoxicity at the concentrations tested. From the screening assays, it is seen that three plants have appreciable tyrosinase inhibitory activity. Hence, these plants may be further evaluated for their use in cosmetics and hyper pigmentation.

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In vitro inhibitory potential of methanolic extract of Celosia argentea var. cristata on tyrosinase, acetylcholinesterase and butyrylcholinesterase enzymes

Bangladesh Journal of Pharmacology ◽

10.3329/bjp.v10i2.22880 ◽

2015 ◽

Vol 10 (2) ◽

pp. 449 ◽

Cited By ~ 3

Author(s):

Fatima Saqib ◽

Khalid Hussain Janbaz ◽

Maryam Khan Sherwani

Keyword(s):

Neurodegenerative Disorders ◽

Inhibitory Activity ◽

Methanol Extract ◽

Methanolic Extract ◽

Microtiter Plate ◽

Tyrosinase Inhibitory Activity ◽

Skin Hyperpigmentation ◽

Celosia Argentea ◽

Inhibitory Potential

In the current study, methanol extract of Celosia argentea var. cristata was tested for its inhibitory potential against tyrosinase, acetylcholinesterase and butyrylcholinesterase enzymes at the concentration of 0.5 mM by ELISA microtiter plate assays. A significant tyrosinase inhibitory activity (63.6%), acetylcholinesterase inhibitory activity (80.3%) and butyrylcholinesterse inhibitory activity (68.24%) was shown by crude methanolic extract of C. argentea var. cristata with respective IC50 values of 268.5 ± 0.2 µg/mL, 73.6 ± 0.1 µg/mL and 132.8 ± 0.9 µg/mL. The result of this study reveals the use of C. argentea var. cristata in skin hyperpigmentation, Parkinson’s disease and neurodegenerative disorders like Alzheimer’s disease and dementia.

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In vitro and in vivo evidence of tyrosinase inhibitory activity of a synthesized(Z)‐5‐(3‐hydroxy‐4‐methoxybenzylidene)‐2‐thioxothiazolidin‐4‐one (5‐HMT)

Experimental Dermatology ◽

10.1111/exd.13863 ◽

2019 ◽

Vol 28 (6) ◽

pp. 734-737 ◽

Cited By ~ 1

Author(s):

EunJin Bang ◽

Eun Kyeong Lee ◽

Sang‐Gyun Noh ◽

Hee Jin Jung ◽

Kyoung Mi Moon ◽

...

Keyword(s):

Inhibitory Activity ◽

Tyrosinase Inhibitory Activity

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Azastilbene Analogs as Tyrosinase Inhibitors: New Molecules with Depigmenting Potential

The Scientific World JOURNAL ◽

10.1155/2013/274643 ◽

2013 ◽

Vol 2013 ◽

pp. 1-7 ◽

Cited By ~ 10

Author(s):

Larissa Lavorato Lima ◽

Rebeca Mól Lima ◽

Annelisa Farah da Silva ◽

Antônio Márcio Resende do Carmo ◽

Adilson David da Silva ◽

...

Keyword(s):

Inhibitory Activity ◽

Tyrosinase Inhibitor ◽

Tyrosinase Inhibition ◽

Tyrosinase Inhibitory Activity ◽

Qualitative And Quantitative ◽

Phenolic Ring ◽

Tyrosinase Inhibitors ◽

Resveratrol Analogs ◽

Better Than

This research has been an effort to develop synthetic resveratrol analogs in order to improve the depigmenting potential of natural resveratrol. Six resveratrol analogs were synthesized and tested for tyrosinase inhibitory activityin vitro, by qualitative and quantitative steps. The results showed the analogCas being the most powerful tyrosinase inhibitor (IA50= 65.67 ± 0.60 μg/mL), followed by the analogsB,E,F,A, andD, respectively. The analogCpresented a tyrosinase inhibition potential better than natural resveratrol (P<0.001). The best depigmenting activity was provided by the presence of hydroxyl in the orthoposition on the second phenolic ring.

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Mushroom tyrosinase inhibitory activity and major fatty acid constituents of Amazonian native flora oils

Brazilian Journal of Pharmaceutical Sciences ◽

10.1590/s1984-82502012000300006 ◽

2012 ◽

Vol 48 (3) ◽

pp. 399-404 ◽

Cited By ~ 8

Author(s):

Raquel da Silva Teixeira ◽

Paula Rafaela Rocha ◽

Hudson Caetano Polonini ◽

Marcos Antônio Fernandes Brandão ◽

Maria das Graças Afonso Miranda Chaves ◽

...

Keyword(s):

Fatty Acid ◽

Inhibitory Activity ◽

Major Fatty Acid ◽

Mushroom Tyrosinase ◽

Melanin Biosynthesis ◽

Tyrosinase Inhibitory Activity ◽

Native Flora ◽

Global Trend ◽

Main Components

In order to treat hyperpigmentation-related problems, there has been a global trend in developing cosmetics claiming to have skin-whitening properties, which act by inhibiting melanin biosynthesis. The objective of this work was to evaluate the in vitro mushroom tyrosinase inhibitory activity of five Amazonian native flora oils, and so to verify the possibility of their incorporation into cosmetic products. In addition, the fatty acid composition of the essential oils was determined by gas chromatography-flame ionisation detection in order to determine the main components of these oils. The tyrosinase inhibitory activity of the tested oils was found to be in the following order: açaí (IA50 = 66.08 µg mL-1) > tucumã > patauá > pracaxi > castanha do Brasil. This study suggests that açaí oil has great potential in the treatment of hyperpigmentation and other related disorders, due to its considerable tyrosinase inhibitory activity.

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Molecular Docking, Synthesis, and Tyrosinase Inhibition Activity of Acetophenone Amide: Potential Inhibitor of Melanogenesis

BioMed Research International ◽

10.1155/2022/1040693 ◽

2022 ◽

Vol 2022 ◽

pp. 1-10

Author(s):

Yasir Nazir ◽

Hummera Rafique ◽

Sadia Roshan ◽

Shazia Shamas ◽

Zaman Ashraf ◽

...

Keyword(s):

Hydrogen Bond ◽

Cinnamic Acid ◽

Inhibitory Activity ◽

Reversible Inhibitor ◽

Binding Modes ◽

Mushroom Tyrosinase ◽

Cinnamic Acids ◽

Tyrosinase Inhibitory Activity ◽

In Silico Docking

Tyrosinase and its related proteins are responsible for pigmentation disorders, and inhibiting tyrosinase is an established strategy to treat hyperpigmentation. The carbonyl scaffolds can be effective inhibitors of tyrosinase activity, and the fact that both benzoic and cinnamic acids are safe natural substances with such a scaffolded structure, it was speculated that hydroxyl-substituted benzoic and cinnamic acid derivatives may exhibit potent tyrosinase inhibitory activity. These moieties were incorporated into new chemotypes that displayed in vitro inhibitory effect against mushroom tyrosinase with a view to explore antimelanogenic ingredients. The most active compound, 2-((3-acetylphenyl)amino)-2-oxoethyl(E)-3-(2,4-dihydroxyphenyl)acrylate (5c), inhibited mushroom tyrosinase with an IC50 of 0.0020 ± 0.0002 μ M , while 2-((3-acetylphenyl)amino)-2-oxoethyl 2,4-dihydroxybenzoate (3c) had an IC50 of 27.35 ± 3.6 μ M in comparison to the positive control arbutin and kojic acid with a tyrosinase inhibitory activity of IC50 of 191.17 ± 5.5 μ M and IC50 of 16.69 ± 2.8 μ M , respectively. Analysis of enzyme kinetics revealed that 5c is a competitive and reversible inhibitor with dissociation constant (Ki) value 0.0072 μM. In silico docking studies with mushroom tyrosinase (PDB ID 2Y9X) predicted possible binding modes in the enzymatic pocket for these compounds. The orthohydroxyl of the cinnamic acid moiety of 5c is predicted to form hydrogen bond with the active site side chain carbonyl of Asn 260 (2.16 Å) closer to the catalytic site Cu ions. The acetyl carbonyl is picking up another hydrogen bond with Asn 81 (1.90 Å). The inhibitor 5c passed the panassay interference (PAINS) alerts. This study presents the potential of hydroxyl-substituted benzoic and cinnamic acids and could be beneficial for various cosmetic formulations.

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Synthesis, Molecular Docking and Tyrosinase Inhibitory Activity of the Decorated Methoxy Sulfonamide Chalcones: in vitro Inhibitory Effects and the Possible Binding Mode

Sains Malaysiana ◽

10.17576/jsm-2021-5009-09 ◽

2021 ◽

Vol 50 (9) ◽

pp. 2603-2614

Author(s):

Thawanrat Kobkeatthawin ◽

Suchada Chantrapromma ◽

Thitipone Suwunwong ◽

Lydia Rhyman ◽

Yee Siew Choong ◽

...

Keyword(s):

Molecular Docking ◽

Inhibitory Activity ◽

Kojic Acid ◽

Spectral Characteristics ◽

Binding Mode ◽

Molecular Docking Study ◽

Standard Drug ◽

Tyrosinase Inhibitory Activity ◽

Chemical Structures

In this study, a series of sulfonamide chalcones derivatives was synthesized and its chemical structures were confirmed by spectral characteristics. The synthesized compounds were evaluated for their tyrosinase inhibitory activities along with molecular docking study. The tyrosinase inhibitory results indicated that compounds 5b, 5c, 5f, 5g and 5h displayed the significant tyrosinase inhibitory activity and comparable to the standard drug (kojic acid). Compound 5c exhibits the most potent tyrosinase inhibition among the synthesized compounds with IC50 = 0.43±0.07 mM, L-DOPA as the substrate, and better than that of the standard kojic acid (IC50 = 0.60±0.20 mM). Molecular docking studies showed that the binding mode of some compounds is in the tyrosinase binding pocket surrounding the copper in the active site. The correlation between the docking results with IC50 values showed that the binding mode prediction of the test compounds would also be convincing. This comprehensive study allows for a possible mechanism for the antityrosinase activity of the sulfonamide chalcones. These sulfonamide chalcones bind to copper atoms of tyrosinase which responsible for the catalytic activity of tyrosinase. These compounds may be used as a lead for rational drug designing for the multi-functional tyrosinase inhibitor.

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(E)-1-(Furan-2-yl)-(substituted phenyl)prop-2-en-1-one Derivatives as Tyrosinase Inhibitors and Melanogenesis Inhibition: An In Vitro and In Silico Study

Molecules ◽

10.3390/molecules25225460 ◽

2020 ◽

Vol 25 (22) ◽

pp. 5460

Author(s):

Hee Jin Jung ◽

Sang Gyun Noh ◽

Il Young Ryu ◽

Chaeun Park ◽

Ji Young Lee ◽

...

Keyword(s):

Inhibitory Activity ◽

Tyrosinase Inhibitory Activity ◽

Melanocyte Stimulating Hormone ◽

B16f10 Cells ◽

In Silico Study ◽

Allosteric Sites ◽

Ic50 Values ◽

Kinetics Of ◽

Mixed Inhibition Type

A series of (E)-1-(furan-2-yl)prop-2-en-1-one derivatives (compounds 1–8) were synthesized and evaluated for their mushroom tyrosinase inhibitory activity. Among these series, compound 8 (2,4-dihydroxy group bearing benzylidene) showed potent tyrosinase inhibitory activity, with respective IC50 values of 0.0433 µM and 0.28 µM for the monophenolase and diphenolase as substrates in comparison to kojic acid as standard compound 19.97 µM and 33.47 µM. Moreover, the enzyme kinetics of compound 8 were determined to be of the mixed inhibition type and inhibition constant (Ki) values of 0.012 µM and 0.165 µM using the Lineweaver-Burk plot. Molecular docking results indicated that compound 8 can bind to the catalytic and allosteric sites 1 and 2 of tyrosinase to inhibit enzyme activity. The computational molecular dynamics analysis further revealed that compound 8 interacted with two residues in the tyrosinase active site pocket, such as ASN260 and MET280. In addition, compound 8 attenuated melanin synthesis and cellular tyrosinase activity, simulated by α-melanocyte-stimulating hormone and 1-methyl-3-isobutylxanthine. Compound 8 also decreased tyrosinase expressions in B16F10 cells. Based on in vitro and computational studies, we propose that compound 8 might be a worthy candidate for the development of an antipigmentation agent.

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