Plants as a Promising Reservoir of Tyrosinase Inhibitors

Riaz, Rabia; Batool, Salma; Zucca, Paolo; Rescigno, Antonio; Peddio, Stefania; Rahman, Shah Zaib Saleem

doi:10.2174/1570193x17999201026230245

Cited by 12 publications

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“…It was indicated that EOs and their main constituents had a wild range of bioactivities, such as antibacterial, antifungal, and anti-inflammatory activities ( 5 , 13 ). Herein, we investigated inhibitory effect of 65 EOs on tyrosinase in vitro .…”

Section: Discussionmentioning

confidence: 99%

“…However, the upregulation of tyrosinase activity and excessive accumulation of melanin would cause skin disorders and related diseases, such as freckles, malignant melanoma, and Parkinson’s disease ( 2 – 4 ). In nature, fruits and vegetables browning, related with the increase of tyrosinase activity, was confirmed to shorten the shelf life of fruits and vegetables, which causes an unattractive appearance and unpredicted loss in nutritional quality ( 5 – 7 ). Recent research indicated that kojic acid, widely used for skin whitening and hyperpigmentation preventing, would lead to skin irritation and mutagenic effect on human skin ( 8 – 10 ).…”

Section: Popular Scientific Summarymentioning

confidence: 99%

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Inhibition of plant essential oils and their interaction in binary combinations against tyrosinase

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Chen

et al. 2022

Food & Nutrition Research

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Background Essential oils (EOs), derived from aromatic plants, exhibit properties beneficial to health, such as anti-inflammatory, anti-oxidative, antidiabetic, and antiaging effects. However, the effect of EOs and their interaction in binary combinations against tyrosinase is not yet known. Objective To evaluate the underlying mechanisms of EOs and their interaction in binary combinations against tyrosinas. Design We explored to investigate the inhibitory effect of 65 EOs and the interaction among cinnamon, bay, and magnolia officinalis in their binary combinations against tyrosinase. In addition, the main constituents of cinnamon, bay, and magnolia officinalis were analyzed by gas chromatography–mass spectrometry (GC–MS). Results The results showed that the most potent EOs against tyrosinase were cinnamon, bay, and magnolia officinalis with IC 50 values of 25.7, 30.8, and 61.9 μg/mL, respectively. Moreover, the inhibitory mechanism and kinetics studies revealed that cinnamon and bay were reversible and competitive-type inhibitors, and magnolia officinalis was a reversible and mixed-type inhibitor. In addition, these results, assessed in mixtures of three binary combinations, indicated that the combination of cinnamon with bay at different dose and at dose ratio had a strong antagonistic effect against tyrosinase. Magnolia officinalis combined with cinnamon or bay experienced both antagonistic and synergistic effect in anti-tyrosinase activity. Conclusion It is revealed that natural EOs would be promising to be effective anti-tyrosinase agents, and binary combinations of cinnamon, bay, and magnolia officinalis might not have synergistic effects on tyrosinase under certain condition.

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Section: Discussionmentioning

confidence: 99%

Section: Popular Scientific Summarymentioning

confidence: 99%

Inhibition of plant essential oils and their interaction in binary combinations against tyrosinase

You

Chen

et al. 2022

Food & Nutrition Research

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“…Until now, many compounds have been addressed for their potent tyrosinase inhibitions, such as flavones, [25] peptides, [26] Schiff bases, [27] and sulfonamide chalcones [28] . Also, some plant extracts were evaluated for their tyrosinase inhibition properties [29–31] …”

Section: Introductionmentioning

confidence: 99%

“…[28] Also, some plant extracts were evaluated for their tyrosinase inhibition properties. [29][30][31] Pancreatic lipase (PL) has been accepted as an important agent of the therapeutic target for curing obesity and is a vital enzyme for the hydrolysis of dietary lipids. [32] PL inhibitors have been used in the treatment of obesity due to reducing the absorption of lipids.…”

Section: Introductionmentioning

confidence: 99%

Synthesis, Biological Activity and Molecular Docking Studies of Novel Sulfonate Derivatives Bearing Salicylaldehyde

Korkmaz

Bursal

2022

Chemistry & Biodiversity

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Enzyme activity alterations have been associated with many metabolism disorders and have crucial roles in the pathogenesis of some diseases. Tyrosinase is a key enzyme in melanin biosynthesis, which is responsible for skin pigmentation to protect the skin from solar radiation. Pancreatic lipase has been considered a key enzyme for the treatment of obesity. Herein, we reported the synthesis and enzyme inhibitions of a series of sulfonates as possible tyrosinase and pancreatic lipase inhibitors. According to the calculated IC50 values, compound 3f (74.1±11.1 μM) and compound 3c (86.6±6.9 μM) were determined to be the best inhibitors among the synthesized compounds for the tyrosinase and pancreatic lipase enzymes, respectively. The approach yielded at extremely high level by creating very flexible structural domains for the chemically modified groups. The structural characterization of the target molecules was implemented by 1H‐NMR, 13C‐NMR, and HR‐MS analyses. Also, molecular docking studies of the synthesized compounds with tyrosinase and pancreatic lipase enzymes were conducted using AutoDock Vina software. Additionally, the studies of the absorption distribution, metabolism, and excretion (ADME) were performed to uncover the target compounds′ pharmacokinetics, drug similarities, and medicinal properties of the novel sulfonate derivatives bearing salicylaldehyde.

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“…There is great interest in the control of tyrosinase activity, especially through the use of inhibitors, which can be natural or synthetic [ 5 , 6 , 7 , 8 , 9 , 10 , 11 ]. This enzyme has two activities: firstly, monophenolase activity, catalysing the passage from L-tyrosine to L-dopa, and secondly, diphenolase activity, which catalyses the passage from L-dopa to L- o -dopaquinone [ 1 , 2 ].…”

Section: Introductionmentioning

confidence: 99%

The Relationship between the IC50 Values and the Apparent Inhibition Constant in the Study of Inhibitors of Tyrosinase Diphenolase Activity Helps Confirm the Mechanism of Inhibition

et al. 2022

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Tyrosinase is the enzyme involved in melanization and is also responsible for the browning of fruits and vegetables. Control of its activity can be carried out using inhibitors, which is interesting in terms of quantitatively understanding the action of these regulators. In the study of the inhibition of the diphenolase activity of tyrosinase, it is intriguing to know the strength and type of inhibition. The strength is indicated by the value of the inhibition constant(s), and the type can be, in a first approximation: competitive, non-competitive, uncompetitive and mixed. In this work, it is proposed to calculate the degree of inhibition (iD), varying the concentration of inhibitor to a fixed concentration of substrate, L-dopa (D). The non-linear regression adjustment of iD with respect to the initial inhibitor concentration [I]0 allows for the calculation of the inhibitor concentration necessary to inhibit the activity by 50%, at a given substrate concentration (IC50), thus avoiding making interpolations between different values of iD. The analytical expression of the IC50, for the different types of inhibition, are related to the apparent inhibition constant (KIapp). Therefore, this parameter can be used: (a) To classify a series of inhibitors of an enzyme by their power. Determining these values at a fixed substrate concentration, the lower IC50, the more potent the inhibitor. (b) Checking an inhibitor for which the type and the inhibition constant have been determined (using the usual methods), must confirm the IC50 value according to the corresponding analytical expression. (c) The type and strength of an inhibitor can be analysed from the study of the variation in iD and IC50 with substrate concentration. The dependence of IC50 on the substrate concentration allows us to distinguish between non-competitive inhibition (iD does not depend on [D]0) and the rest. In the case of competitive inhibition, this dependence of iD on [D]0 leads to an ambiguity between competitive inhibition and type 1 mixed inhibition. This is solved by adjusting the data to the possible equations; in the case of a competitive inhibitor, the calculation of KI1app is carried out from the IC50 expression. The same occurs with uncompetitive inhibition and type 2 mixed inhibition. The representation of iD vs. n, with n=[D]0/KmD, allows us to distinguish between them. A hyperbolic iD vs. n representation that passes through the origin of coordinates is a characteristic of uncompetitive inhibition; the calculation of KI2app is immediate from the IC50 value. In the case of mixed inhibitors, the values of the apparent inhibition constant of meta-tyrosinase (Em) and oxy-tyrosinase (Eox), KI1app and the apparent inhibition constant of metatyrosinase/Dopa complexes (EmD) and oxytyrosinase/Dopa (EoxD), KI2app are obtained from the dependence of iD vs. n, and the results obtained must comply with the IC50 value.

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Plants as a Promising Reservoir of Tyrosinase Inhibitors

Cited by 12 publications

References 0 publications

Inhibition of plant essential oils and their interaction in binary combinations against tyrosinase

Inhibition of plant essential oils and their interaction in binary combinations against tyrosinase

Synthesis, Biological Activity and Molecular Docking Studies of Novel Sulfonate Derivatives Bearing Salicylaldehyde

The Relationship between the IC50 Values and the Apparent Inhibition Constant in the Study of Inhibitors of Tyrosinase Diphenolase Activity Helps Confirm the Mechanism of Inhibition

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