Inhibitory mechanism of scutellarein on tyrosinase by kinetics, spectroscopy and molecular simulation

Chen, Qinfei; Shang, Chao; Han, Mengqi; Chen, Chan; Tang, Weikang; Liu, Wenbin

doi:10.1016/j.saa.2023.122644

Cited by 13 publications

(5 citation statements)

References 40 publications

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“…The enzyme concentration ([E]) was plotted against the initial reaction rate ([V]) at different YYP concentrations, and the results manifested a set of straight lines passing through the origin, and all the lines showed a good linear relationship. As the concentration of YYP increased, the slope of the straight line gradually decreased, indicating that the addition of YYP did not change the amount of enzyme, but decreased the ability to decompose the substrate by reducing the activity of the enzyme, so the inhibition of YYP on the enzyme was reversible, and the results of the present experiments were more consistent with those of previous research [50,51].…”

Section: Synthetic Peptide Activity Validationsupporting

confidence: 91%

“…Methoxy-substituted tyramine derivatives acted as hybrid inhibitors with stronger binding between the enzyme and the compounds, indicating that the enzyme prefers a competitive approach (K I < K IS ) [54]. Summarized in Table 10, based on the slope ratio and intercept ratio of the Lineweaver-Burk curve (with and without the presence of samples), the K I and K IS can be obtained [51]. K I and K IS gradually increased with increasing concentration of YYP, and 1/K IS > 1/K I , indicating that the affinity of YYP for tyrosinase was greater than that of the complex of L-tyr and tyrosinase.…”

Section: Discussionmentioning

confidence: 99%

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Optimization of a Novel Tyrosinase Inhibitory Peptide from Atrina pectinata Mantle and Its Molecular Inhibitory Mechanism

Wang,

Lin,

Shen

et al. 2023

Foods

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In order to realize the multi-level utilization of marine shellfish resources and to develop the potential biological activity of processing by-products of Atrina pectinata, gelatin was extracted from the mantle and the potential whitening effect of its enzymatic peptides was explored. Taking tyrosinase inhibitory activity as the evaluation index, the enzyme hydrolysate process was optimized by response-surface methodology, and the optimal enzyme hydrolysate conditions were as follows: pH 5.82, 238 min enzyme hydrolysate time, and temperature of 54.5 °C. Under these conditions, the tyrosinase inhibition activity of Atrina pectinata mantle gelatin peptide (APGP) was 88.6% (IC50 of 3.268 ± 0.048 mg/mL). The peptides obtained from the identification were separated by ultrafiltration and LC–MS/MS, and then four new peptides were screened by molecular docking, among which the peptide Tyr-Tyr-Pro (YYP) had the strongest inhibitory effect on tyrosinase with an IC50 value of 1.764 ± 0.025 mM. The molecular-docking results indicated that hydrogen bonding is the main driving force for the interaction of the peptide YYP with tyrosinase. From the Lineweaver–Burk analysis, it could be concluded that YYP is inhibitory to tyrosinase and exhibits a mixed mechanism of inhibition. These results suggest that YYP could be widely used as a tyrosinase inhibitor in whitening foods and pharmaceuticals.

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Section: Synthetic Peptide Activity Validationsupporting

confidence: 91%

Section: Discussionmentioning

confidence: 99%

Optimization of a Novel Tyrosinase Inhibitory Peptide from Atrina pectinata Mantle and Its Molecular Inhibitory Mechanism

Wang,

Lin,

Shen

et al. 2023

Foods

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“…Tyrosinase, also called polyphenol oxidase, is a multipurpose oxidase that contributes to food browning through enzymatic activity and melanin biosynthesis in melanocytes. With a molecular weight of 120 kDa, this metalloenzyme contains two divalent copper ions (CuA and CuB) in its catalytically active pocket (Chen et al, 2023). Since it is the only enzyme that limits the rate at which melanin can be produced, TYR is crucial to melanin synthesis (Chen et al, 2023).…”

Section: Introductionmentioning

confidence: 99%

“…With a molecular weight of 120 kDa, this metalloenzyme contains two divalent copper ions (CuA and CuB) in its catalytically active pocket (Chen et al, 2023). Since it is the only enzyme that limits the rate at which melanin can be produced, TYR is crucial to melanin synthesis (Chen et al, 2023). TYR deploys its monophenolase activity to change L-4-hydroxyphenylalanine (L-tyrosine) into L-3,4dihydroxyphenylalanine (L-DOPA), which is then transformed into L-dopaquinone by its diphenolase activity in cells (Shen et al, 2023).…”

Section: Introductionmentioning

confidence: 99%

“…Excessive melanin production can result in significant esthetic issues such as hyperpigmentation, dermatosis, and melanoma (Lee et al, 2023;Shen et al, 2023). As a result, TYR inhibitors have a wide range of applications in pharmaceutical, food, cosmetic and agricultural products (Yu, Fan, & Ding, 2022;Chen et al, 2023). Kojic acid and arbutin are well-known TYR inhibitors that reduce enzymatic reactions causing foods browning and skin hyperpigmentation.…”

Section: Introductionmentioning

confidence: 99%

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Inhibitive Mechanism of Loquat Flower Isolate on Tyrosinase Activity and Melanin Synthesis in Mouse Melanoma B16 Cells

Chen,

Tao,

Wang

et al. 2024

Preprint

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Melanin is extensively distributed in organisms and believed to be synthetized by tyrosinase (TYR), leading to aberrant coloring and skin conditions when over-produced. Loquat (Eriobotrya japonica (Thunb.) Lindl.) flowers contain large amounts of bioactive substances currently few studied on their suppressive capabilities to melanin synthesis. Its isolate product (LFP) was obtained by ethanol solution extraction and resin purification, of which the inhibitory mechanism on TYR activity was elaborated by enzyme kinetics and multi-spectroscopy determinations and the impact on related proteins’ expression in mouse melanoma B16 cells was analyzed with Western blotting. HPLC-MS analysis indicated that LFP was identified into 137 compounds, with 12 including flavonoids (quercetin, isorhamnoin, p-coumaric acid, etc.), cinnamic acid and its derivatives as well as benzene and its derivatives owning TYR inhibitory activities. LFP inhibited TYR activity in a concentration-dependent manner with its IC50 value being 2.8 mg/mL and an anti-competitive mechanism involved altering the enzyme's conformation. LFP reduced the expression of TYR, TRP1, and TRP2 in melanoma B16 cells, hence inhibiting the synthesis of melanin. Considered collectively, LFP would be a viable option for treating hyperpigmentation caused by tyrosinase, providing a theoretical basis for the value-added utilization of loquat flower resource in beauty and aging related functional products.

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Review on the pharmacological effects and pharmacokinetics of scutellarein

Lai,

2024

Archiv der Pharmazie

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Scutellarein is a flavonoid from Scutellaria baicalensis Georgi that has been shown to have a variety of pharmacological activities. This review aims to summarize the pharmacological and pharmacokinetic studies on scutellarein and provide useful information for relevant scholars. Pharmacological studies indicate that scutellarein possesses a diverse range of pharmacological properties, including but not limited to anti‐inflammatory, antioxidant, antiviral, neuroprotective, hypoglycemic, hypolipidemic, anticancer, and cardiovascular protective effects. Further investigation reveals that the pharmacological effects of scutellarein are driven by multiple mechanisms. These mechanisms encompass the scavenging of free radicals, inhibition of the activation of inflammatory signaling pathways and expression of inflammatory mediators, inhibition of the activity of crucial viral proteins, suppression of gluconeogenesis, amelioration of insulin resistance, improvement of cerebral ischemia‐reperfusion injury, induction of apoptosis in cancer cells, and prevention of myocardial hypertrophy, among others. In summary, these pharmacological studies suggest that scutellarein holds promise for the treatment of various diseases. It is imperative to conduct clinical studies to further elucidate the therapeutic effects of scutellarein. However, it is worth noting that studies on the pharmacokinetics reveal an inhibitory effect of scutellarein on uridine 5′‐diphosphate glucuronide transferases and cytochrome P450 enzymes, potentially posing safety risks.

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Inhibitory mechanism of scutellarein on tyrosinase by kinetics, spectroscopy and molecular simulation

Cited by 13 publications

References 40 publications

Optimization of a Novel Tyrosinase Inhibitory Peptide from Atrina pectinata Mantle and Its Molecular Inhibitory Mechanism

Optimization of a Novel Tyrosinase Inhibitory Peptide from Atrina pectinata Mantle and Its Molecular Inhibitory Mechanism

Inhibitive Mechanism of Loquat Flower Isolate on Tyrosinase Activity and Melanin Synthesis in Mouse Melanoma B16 Cells

Review on the pharmacological effects and pharmacokinetics of scutellarein

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