Recent advance in the discovery of tyrosinase inhibitors from natural sources via separation methods

Zhang, Xiaowei; Bian, Guang-li; Kang, Pei-Ying; Cheng, Xin-jie; Yan, Kai; Liu, Yongli; Gao, Yan-xia; Li, Deqiang

doi:10.1080/14756366.2021.1983559

Cited by 24 publications

(9 citation statements)

References 74 publications

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“…To date several TYRIs had been identified; some of them are extracted or generated from natural sources [8,9] . Ex‐novo synthesized TYRIs emerged from in silico approaches of drug discovery.…”

Section: Introductionmentioning

confidence: 99%

Design, Synthesis, and in Vitro Evaluation of 4‐(4‐Hydroxyphenyl)piperazine‐Based Compounds Targeting Tyrosinase

et al. 2022

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Melanin biosynthesis is enzymatically regulated by tyrosinase (TYR, EC 1.14.18.1), which is efficiently inhibited by natural and synthetic phenols, demonstrating potential therapeutic application for the treatment of several human diseases. Herein we report the inhibitory effects of a series of (4‐(4‐hydroxyphenyl)piperazin‐1‐yl)arylmethanone derivatives, that were designed, synthesised and assayed against TYR from Agaricus bisporus (AbTYR). The best inhibitory activity was predominantly found for compounds bearing selected hydrophobic ortho‐substituents on the aroyl moiety (IC50 values in the range of 1.5–4.6 μM). They proved to be more potent than the reference compound kojic acid (IC50=17.8 μM) and displayed competitive mechanism of inhibition of diphenolase activity of AbTYR. Docking simulation predicted their binding mode into the catalytic cavities of AbTYR and the modelled human TYR. In addition, these compounds displayed antioxidant activity combined with no cytotoxicity in MTT tests. Notably, the best inhibitor affected tyrosinase activity in α‐MSH‐stimulated B16F10 cells, thus demonstrating anti‐melanogenic activity.

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Section: Introductionmentioning

confidence: 99%

Design, Synthesis, and in Vitro Evaluation of 4‐(4‐Hydroxyphenyl)piperazine‐Based Compounds Targeting Tyrosinase

et al. 2022

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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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“…Thus, it is associated with skin health and undesirable enzymatic browning of fruits and vegetables (Zhou et al, 2021). Therefore, the inhibitors of tyrosinase which can be considered antioxidants, are extensively used in cosmetics and medical industries as depigmenting agents and in food and agriculture industries as antibrowning agents (Zhang et al, 2021). Tyrosinase inhibitors developing for novel food preservatives have attracted the attention of more and more scholars.…”

Section: Introductionmentioning

confidence: 99%

Preparation of low molecular weight Enteromorpha prolifera polysaccharide and its antioxidant and tyrosinase inhibitory activities

Que

Wang

et al. 2022

Food Sci. Technol

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Enteromorpha prolifera polysaccharide (EP) is a water-soluble sulfated polysaccharide with many types of biological activities. In this study, the crude polysaccharide was extracted from Enteromorpha prolifera and degraded by different physical, chemical, and biological methods. The results showed that the enzymatic degradation products displayed the best tyrosinase inhibitory activity. The optimal enzymatic degradation conditions were as follows: 30 °C, pH 5.5, 750 U/mL enzyme dosage for 2 h. The enzymatic hydrolysates were then divided into six EP fractions (EPFs) by an ultrafiltration membrane. The in vitro tyrosinase inhibitory activity of these fractions showed that the smaller the molecular weight of EPF, the better the inhibitory effect on tyrosinase. The antioxidant and tyrosinase inhibitory effect of the most effective EPF, a molecular weight below 5 kDa, (EPF5), was further confirmed on B16 cells. A kinetic study of tyrosinase inhibitory activity revealed that EPF5 is a competitive-uncompetitive mixed-type inhibitor of tyrosinase. These findings suggested that EPF5 has significant potential as a skin-whitening agent in cosmetics as well as an antibrowning agent in the food and agriculture industries.

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Recent advance in the discovery of tyrosinase inhibitors from natural sources via separation methods

Cited by 24 publications

References 74 publications

Design, Synthesis, and in Vitro Evaluation of 4‐(4‐Hydroxyphenyl)piperazine‐Based Compounds Targeting Tyrosinase

Design, Synthesis, and in Vitro Evaluation of 4‐(4‐Hydroxyphenyl)piperazine‐Based Compounds Targeting Tyrosinase

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

Preparation of low molecular weight Enteromorpha prolifera polysaccharide and its antioxidant and tyrosinase inhibitory activities

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