A convenient screening method to differentiate phenolic skin whitening tyrosinase inhibitors from leukoderma-inducing phenols

Ito, Shosuke; Wakamatsu, Kazumasa

doi:10.1016/j.jdermsci.2015.07.007

Cited by 36 publications

(35 citation statements)

References 42 publications

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“…The inhibition properties of LCAME were preliminarily investigated on mushroom tyrosinase by spectrophotometric monitoring of dopachrome formation, a method which is routinely used for evaluation of the activity of potential tyrosinase inhibitors [13,21,22]. l -DOPA was used as the substrate to test DO activity while l -tyrosine was used to test TH activity.…”

Section: Resultsmentioning

confidence: 99%

“…Some tyrosinase inhibitors are also substrates of the enzyme and this is a critical issue because their oxidation can lead to the formation of highly reactive, cytotoxic o -quinones [22,41,42]. To rule out this possibility, either LCAME or CAME at 100 μM were exposed to mushroom tyrosinase, in the absence of l -DOPA, and after 10 min, the reaction mixtures were analyzed by HPLC.…”

Section: Resultsmentioning

confidence: 99%

“…A critical issue in the search for tyrosinase inhibitors is that most compounds, tested preliminarily on mushroom tyrosinase, proved to be noneffective on human tyrosinase [13,21,22,23]. Currently only a few tyrosinase inhibitors have been further developed for cosmetic and health care purposes as several factors such as cytotoxicity, solubility, cutaneous absorption, and stability should be considered as well.…”

Section: Introductionmentioning

confidence: 99%

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Conjugation with Dihydrolipoic Acid Imparts Caffeic Acid Ester Potent Inhibitory Effect on Dopa Oxidase Activity of Human Tyrosinase

Micillo

Sirés-Campos

García‐Borrón

et al. 2018

IJMS

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Caffeic acid derivatives represent promising lead compounds in the search for tyrosinase inhibitors to be used in the treatment of skin local hyperpigmentation associated to an overproduction or accumulation of melanin. We recently reported the marked inhibitory activity of a conjugate of caffeic acid with dihydrolipoic acid, 2-S-lipoylcaffeic acid (LCA), on the tyrosine hydroxylase (TH) and dopa oxidase (DO) activities of mushroom tyrosinase. In the present study, we evaluated a more lipophilic derivative, 2-S-lipoyl caffeic acid methyl ester (LCAME), as an inhibitor of tyrosinase from human melanoma cells. Preliminary analysis of the effects of LCAME on mushroom tyrosinase indicated more potent inhibitory effects on either enzyme activities (IC50 = 0.05 ± 0.01 μM for DO and 0.83 ± 0.09 μM for TH) compared with LCA and the reference compound kojic acid. The inhibition of DO of human tyrosinase was effective (Ki = 34.7 ± 1.1 μM) as well, while the action on TH was weaker. Lineweaver–Burk analyses indicated a competitive inhibitor mechanism. LCAME was not substrate of tyrosinase and proved nontoxic at concentrations up to 50 μM. No alteration of basal tyrosinase expression was observed after 24 h treatment of human melanoma cells with the inhibitor, but preliminary evidence suggested LCAME might impair the induction of tyrosinase expression in cells stimulated with α-melanocyte-stimulating hormone. All these data point to this compound as a valuable candidate for further trials toward its use as a skin depigmenting agent. They also highlight the differential effects of tyrosinase inhibitors on the human and mushroom enzymes.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Conjugation with Dihydrolipoic Acid Imparts Caffeic Acid Ester Potent Inhibitory Effect on Dopa Oxidase Activity of Human Tyrosinase

Micillo

Sirés-Campos

García‐Borrón

et al. 2018

IJMS

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“…The combination of 4‐n‐butylresorcinol (C 10 H 14 O 2 ) and a natural monoterpenoid, hinokitiol (C 10 H 12 O 2 ), reduces MITF expression and gave better depigmenting activity compared to the action of only a single compound . The presence of gallic acid (C 7 H 6 O 5 ), chebulinic acid (C 41 H 32 O 27 ), and ellagic acid (C 14 H 6 O 8 ) in a formulated Indian medicine, Triphala, remarkably reduce TYR mRNA expression levels in B16F10 cells . In cosmetic formulation, depigmenting compounds should be combined with UV screen agent such as zinc oxide or titanium dioxide due to the reduction of melanin (ie, eumelanin), which protect skin from DNA damage and skin cancer .…”

Section: Development Of Potent Depigmenting Formulationmentioning

confidence: 99%

“…This assay is suitable for fast screening purposes, kinetic analysis, molecular docking, ligand‐protein analysis, and determination of inhibition competency on TYR catalytic activity . Recent study showed that mushroom TYR with combination of HPLC analysis could be used to identify adverse side effect of depigmenting compounds that promotes leukoderma skin problems . Despite its advantages for fast TYR inhibition screening, they suffer from several drawbacks.…”

Section: Protocol and Assaysmentioning

confidence: 99%

Discovery of new depigmenting compounds and their efficacy to treat hyperpigmentation: Evidence from in vitro study

Lajis

Ariff

2019

J of Cosmetic Dermatology

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Summary Human skin pigmentation is a result of constitutive and facultative pigmentation. Facultative pigmentation is frequently stimulated by UV radiation, pharmacologic drugs, and hormones whereby leads to the development of abnormal skin hyperpigmentation. To date, many state‐of‐art depigmenting compounds have been studied using in vitro model to treat hyperpigmentation problems for cosmetic dermatological applications; little attention has been made to compare the effectiveness of these depigmenting compounds and their mode of actions. In this present article, new and recent depigmenting compounds, their melanogenic pathway targets, and modes of action are reviewed. This article compares the effectiveness of these new depigmenting compounds to modulate several melanogenesis‐regulatory enzymes and proteins such as tyrosinase (TYR), TYR‐related protein‐1 (TRP1), TYR‐related protein‐2 (TRP2), microphthalmia‐associated transcription factor (MITF), extracellular signal—regulated kinase (ERK) and N‐terminal kinases (JNK) and mitogen‐activated protein kinase p38 (p38 MAPK). Other evidences from in vitro assays such as inhibition on melanosomal transfer, proteasomes, nitric oxide, and inflammation‐induced melanogenesis are also highlighted. This article also reviews analytical techniques in different assays performed using in vitro model as well as their advantages and limitations. This article also provides an insight on recent finding and re‐examination of some protocols as well as their effectiveness and reliability in the evaluation of depigmenting compounds. Evidence and support from related patents are also incorporated in this present article to give an overview on current patented technology, latest trends, and intellectual values of some depigmenting compounds and protocols, which are rarely highlighted in the literatures.

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The C‐terminally shortened analogs of a hexapeptide derived from Lingzhi hydrolysate with enhanced tyrosinase‐inhibitory activity

Krobthong

Yingchutrakul

Samutrtai

et al. 2021

Archiv der Pharmazie

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Ganoderma lucidum or Lingzhi (Chinese) is a medicinal fungus widely used in traditional medicine as a health supplement. This study was conducted to identify an approach to enhance the anti-tyrosinase activity of a peptide from G. lucidum by chemical modification of its C-terminus. The original peptide was obtained from protease-digested Lingzhi proteins, followed by ultrafiltration (molecular weight cut-off 3 kDa) and C18 solid-phase extraction. The hexapeptide (NH 2 -VLTCGF-COOH) possessing the anti-tyrosinase activity was identified by liquid chromatography-tandem mass spectrometry (LC-MS/MS). This hexapeptide was subjected to shortening to enhance the anti-tyrosinase activity. Both the original peptide and the shortened peptides were synthesized by solid-phase peptide synthesis. The purity and mass of the synthetic peptide and the modified peptide were evaluated by high-performance liquid chromatography and LC-MS, respectively. Comparison of the tyrosinase activities showed that the modified peptide demonstrated more than 23.27 ± 1.07% activity, which was better than that of the hexapeptide. The structure-related biological activity was explained by molecular docking, wherein the VLT-tyrosinase complex showed two interaction forces: Asn260 and Gly281 through H-bonding and Glu256 through electrostatic interaction. This information could help toward gaining further understanding of the correlation between the anti-tyrosinase activity and the molecular structure of the modified hexapeptide and support its potential use as a safe cosmetic ingredient with tyrosinase-suppressing ability.

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A convenient screening method to differentiate phenolic skin whitening tyrosinase inhibitors from leukoderma-inducing phenols

Cited by 36 publications

References 42 publications

Conjugation with Dihydrolipoic Acid Imparts Caffeic Acid Ester Potent Inhibitory Effect on Dopa Oxidase Activity of Human Tyrosinase

Conjugation with Dihydrolipoic Acid Imparts Caffeic Acid Ester Potent Inhibitory Effect on Dopa Oxidase Activity of Human Tyrosinase

Discovery of new depigmenting compounds and their efficacy to treat hyperpigmentation: Evidence from in vitro study

The C‐terminally shortened analogs of a hexapeptide derived from Lingzhi hydrolysate with enhanced tyrosinase‐inhibitory activity

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