Hydroxyphenyl thiosemicarbazones as inhibitors of mushroom tyrosinase and antibrowning agents

Carcelli, Mauro; Rogolino, Dominga; Bartoli, Jennifer; Pala, Nicolino; Compari, Carlotta; Ronda, Nicoletta; Bacciottini, Franco; Incerti, Matteo; Fisicaro, E.

doi:10.1016/j.foodchem.2019.125310

Cited by 35 publications

(14 citation statements)

References 37 publications

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“…The results are presented as a Lineweaver-Burk plot of 1/v0 versus 1/[S] to determine the binding mechanism. 10-methoxy-leonurine (1) and leonurine (2) made a family line induced by Equation (3). As shown in Figure 2C,D, inhibitors 1 and 2 had different −1/Km and 1/Vmax values ( Figure 2C,D, Table 1), suggesting that these compounds are competitive inhibitors.…”

Section: Enzyme Kineticsmentioning

confidence: 88%

“…Tyrosinase (EC 1.14.18.1), found in bacteria, fungi, plants, and mammals [1], is a copper-containing metalloenzyme with various catalytic functions, such as hydroxylation of monophenols and oxidation of diphenols, which are important for the production of melanin pigment [2]. Excessive accumulation of melanin is responsible not only for pigment disorders in human skin but also enzymatic browning of fresh-cut fruits and vegetables [3]. It is also important for cuticle formation in insects [4].…”

Section: Introductionmentioning

confidence: 99%

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The Guanidine Pseudoalkaloids 10-Methoxy-Leonurine and Leonurine Act as Competitive Inhibitors of Tyrosinase

Kim

Leem

Lee³

2020

Biomolecules

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Tyrosinase plays a key role in the production of melanin. A variety of industrial fields have shown interest in the development of tyrosinase inhibitors from plants. In this study, compounds 1–5 derived from Leonurus japonicas were evaluated to determine their ability to inhibit tyrosinase. Of these, 10-methoxy-leonurine (1) and leonurine (2) exhibited IC50 values of 7.4 ± 0.4 and 12.4 ± 0.8 μM, respectively, and acted as competitive inhibitors of tyrosinase, with Ki values in the micromolar range. In silico modeling revealed a guanidine group located in the inner cavity and a benzene ring docked within the active site of these compounds. These guanidine pseudoalkaloids show potential not only as tyrosinase inhibitors but also as lead compounds in new scaffolds for the development of novel inhibitors.

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Section: Enzyme Kineticsmentioning

confidence: 88%

Section: Introductionmentioning

confidence: 99%

The Guanidine Pseudoalkaloids 10-Methoxy-Leonurine and Leonurine Act as Competitive Inhibitors of Tyrosinase

Kim

Leem

Lee³

2020

Biomolecules

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“…The ethyl acetate leaf extract was reported as the most potent lipase inhibitor, with 102.80 ± 7.25 mg OE/g. Tyrosinase is the prime enzyme involved the o-hydroxylation of monophenols and oxidation of o-diphenols to o-quinones resulting in the biosynthesis of melanin (brown or black pigment) [48]. Melanin has multifaceted roles; apart from giving colour to the skin, it also acts as a skin photo-protector and convert harmful UV light into harmless heat.…”

Section: Enzymatic Inhibitory Effectsmentioning

confidence: 99%

Assessment of the Pharmacological Properties and Phytochemical Profile of Bruguiera gymnorhiza (L.) Lam Using In Vitro Studies, In Silico Docking, and Multivariate Analysis

et al. 2020

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Bruguiera gymnorhiza (L.) Lam. is claimed to effectively manage a number of ailments including diabetes and associated complications. Nonetheless, no attempt has been made to delineate its pharmacological propensities and phytochemical profile. This study was designed to appraise the antioxidant and enzymatic inhibitory properties relevant to the management of diabetes mellitus, obesity, and neurodegenerative and skin disorders. A combination of colorimetric assays and ultra-high-performance liquid chromatography/electrospray ionization tandem mass spectrometry (UHPLC-ESI-MS/MS) were applied for the phytochemical screening of leaf, root, twig, and fruit extracts (methanol and ethyl acetate). In vitro antioxidant evaluations were via radical scavenging abilities (DPPH, ABTS), reducing potential (FRAP, CUPRAC), chelating power, and total antioxidant capacity (phosphomolybdenum). Seven key metabolic enzymes (α-amylase, α-glucosidase, tyrosinase, elastase, lipase, AChE, and BChE) were targeted to determine the inhibitory effects. Multivariate and in silico docking analysis were performed on collected data. Methanolic fruit extract yielded the highest total phenolic, tannin, and triterpenoid contents (174.18 ± 4.27 mg GAE/g, 176.24 ± 3.10 mg CE/g, 63.11 ± 3.27 mg OAE/g, respectively); significantly depressed tyrosinase, elastase, and α-amylase activities (155.35 ± 0.29 mg KAE/g, 4.56 ± 0.10 mg CAE/g, 1.00 ± 0.05 mmol ACAE/g, accordingly); and harboured the most potent antioxidant capacities with DPPH, CUPRAC, FRAP (492.62 ± 5.31, 961.46 ± 11.18, 552.49 ± 8.71 mg TE/g, respectively), and phosphomolybdenum (4.17 ± 0.31 mmol TE/g) assays. Multivariate analysis suggested that the type of solvents used influenced the biological activities more compared to plant parts. Docking analysis showed that azelaic acid binds with tyrosinase by Van der Waals and conventional hydrogen bonds. We anticipate that the present study may establish baseline data on this halophyte that could open new avenues for the development of biomedicine.

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“…Proteins have UV absorption due to the presence of Tryptophan (Trp) and Tyrosine (Tyr) residues 47,48 . When a small molecule binds to the TY protein, the absorption spectrum of TY may shift, resulting in a new complex formation due to conformational changes.…”

Section: Resultsmentioning

confidence: 99%

Spectroscopic studies and molecular docking on the interaction of delphinidin‐3‐O‐galactoside with tyrosinase

Chen

Shi

Liu

et al. 2021

Biotech and App Biochem

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The inhibitory effects of delphinidin-3-O-galactoside (DG) on the activities of tyrosinase (EC 1.14.18.1) (TY) from the edible Agaricus bisporus mushroom were investigated by enzyme kinetics, multispectroscopic methods, and molecular docking. As a result, DG showed strong inhibition on TY with the IC 50 of 34.14 × 10 -6 mol L -1 . The inhibition mode of DG against TY was mixed type with α values of 5.09. The binding constant K a and related thermodynamic parameters at the three different temperatures showed that the fluorescence quenching of TY by DG was static quenching. Synchronous fluorescence, three-dimensional fluorescence, ultraviolet-visible spectroscopy, and circular dichroism spectroscopies confirmed that the conformation or microenvironment of the TY protein were changed after binding with DG. Molecular docking revealed that DG had strong binding affinity to TY through hydrogen bonding and van der Waals force, and the results were consistent with the fluorescence data. Our findings suggested that DG may be potential TY inhibitor.

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Hydroxyphenyl thiosemicarbazones as inhibitors of mushroom tyrosinase and antibrowning agents

Cited by 35 publications

References 37 publications

The Guanidine Pseudoalkaloids 10-Methoxy-Leonurine and Leonurine Act as Competitive Inhibitors of Tyrosinase

The Guanidine Pseudoalkaloids 10-Methoxy-Leonurine and Leonurine Act as Competitive Inhibitors of Tyrosinase

Assessment of the Pharmacological Properties and Phytochemical Profile of Bruguiera gymnorhiza (L.) Lam Using In Vitro Studies, In Silico Docking, and Multivariate Analysis

Spectroscopic studies and molecular docking on the interaction of delphinidin‐3‐O‐galactoside with tyrosinase

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