Tyrosinase inhibition by isophthalic acid: Kinetics and computational simulation

Si, Yue-Xiu; Yin, Sheng; Park, Daeui; Chung, Hae Young; Li, Yan; Lu, Ziwen; Zhou, Hai‐Meng; Yang, Jun‐Mo; Qian, Guo‐Ying; Park, Yong‐Doo

doi:10.1016/j.ijbiomac.2011.02.015

Cited by 71 publications

(27 citation statements)

References 32 publications

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“…Our analysis is distinct compared to previous simulation studies [32,33,40] in three respects: (1) the crystal 3D structure of tyrosinase from A. bisporus was directly used in the present study rather than simulating its 3D structure via modeling programs; (2) our data more clearly showed the docking sites and copper chelating evidence compared to previous results; and (3) we used kojic acid as the control compound to compare the docking effectiveness. Kojic acid is the most well known inhibitor of tyrosinase [41][42][43][44].…”

Section: Discussionmentioning

confidence: 87%

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Effect of hesperetin on tyrosinase: Inhibition kinetics integrated computational simulation study

Wang

Park

et al. 2012

International Journal of Biological Macromolecules

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Section: Discussionmentioning

confidence: 87%

“…A spectrophotometric tyrosinase assay was performed as previously described [32,33]. To begin the assay, a 10 L sample of enzyme solution was added to 1 mL of reaction mix.…”

Section: Tyrosinase Assaymentioning

confidence: 99%

Effect of hesperetin on tyrosinase: Inhibition kinetics integrated computational simulation study

Wang

Park

et al. 2012

International Journal of Biological Macromolecules

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“…A spectrophotometric tyrosinase assay was performed as previously described. [16][17][18] To begin the assay, a 10 mL sample of the enzyme solution was added to 1 mL of the reaction mixture. Tyrosinase activity (v) was recorded as the change in absorbance per min at 475 nm as determined using a Shimadzu UV-1800 spectrophotometer (Shimadzu, Kyoto).…”

Section: Methodsmentioning

confidence: 99%

Effects of Isorhamnetin on Tyrosinase: Inhibition Kinetics and Computational Simulation

Wang

Park

et al. 2012

Bioscience, Biotechnology, and Biochemistry

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“…Compound (a) showed the strongest inhibitory effect due to the introduction of an electron donor methoxy group with high hydrophobicity at the para-position stabilizing the Schiff base and the ortho hydroxyl group forming a quasi substrate complex (K IS ) was gained from a plot of the vertical intercepts versus the inhibitor concentrations, which are linearly fitted, showing that compound (a) has a single inhibition site or a single class of inhibition site on tyrosinase (Si et al, 2011), as shown in the inset. The inhibition constants are summarized in Table 1 for comparison.…”

Section: Methodsmentioning

confidence: 99%

“…There are many tyrosinase inhibitors, such as hydroquinone (Garcia and Fulton Jr, 1996), ascorbic acid (Kameyama et al, 1996), arbutin (Nakajima et al, 1998), kojic acid (Mishima et al, 1994), aromatic aldehydes (Jimenez et al, 2001;, aromatic acids (Chen et al, 2005;Si et al, 2011), aromatic alcohol (Liu et al, 2007;Zhu et al, 2011), and tropolone (Valero et al, 1991). It has been suggested that the addition of a methoxy group at the meta or para position of salicylaldehyde shows different inhibition strength.…”

Section: Introductionmentioning

confidence: 99%

Tyrosinase Inhibitory Effects and Antioxidant Properties of Paeonol and Its Analogues

Zhu

Cao

2013

FSTR

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With the aim to find out structural features for the tyrosinase inhibitory activity, the inhibitory effects of seven paeonol analogues on the diphenolase of mushroom tyrosinase, the interaction between the inhibitors and the copper ions, and the antioxidant activity by DPPH radical were investigated. These paeonol analogues had suggested remarkable inhibition toward tyrosinase. Among them, paeonol (a) exhibited the strongest inhibition activity (IC 50 =0.21 mM) as well as showed potent scavenging activity on the DPPH radical. The inhibition kinetics revealed that paeonol (a) was a mixed-type inhibitor, 2′-hydroxy acetophenone (c), 4′-hydroxy acetophenone (d), and 2,4′-dihydroxy acetophenone (e) were competitive inhibitors, while acetophenone (b), 2′-methoxyacetophenone (f), and 4′-methoxy acetophenone (g) behaved as noncompetitive inhibitors. The maximum absorbing wavelengths of compounds (c), (d), and (e) showed different significant blue shifts, which could explain that they exhibited competitive inhibition by forming a chelate with the copper ions at the catalytic domain of the tyrosinase.Keywords: paeonol, acetophenone, tyrosinase inhibitor, DPPH radical, copper ions chelation *To whom correspondence should be addressed. E-mail: yuyanying@ncu.edu.cn IntroductionTyrosinase (EC 1.14.18.1), known as polyphenol oxidase, is a multifunctional copper-containing metalloenzyme widely distributed in nature. It mainly catalyzes the o-hydroxylation of monophenols to the corresponding catechols, and the oxidation of monophenols to the corresponding o-quinones (Yoon et al., 2009). Consequently, a series of high reactive quinones are produced to initiate the pigmentation and excessive activation of tyrosinase can cause various dermatological disorders, such as Parkinson and other degenerative diseases (Asanuma et al., 2003).One of the reactions catalyzed by the tyrosinase is the oxidation of L-dopa to L-dopaquinone by utilising molecular oxygen. In addition, reactive oxygen species (ROS) and free radical-mediated reactions are associated with various diseases, such as diabetes mellitus, cancer, ageing, skin disorders, and neurodegenerative diseases (Pham-Huy et al., 2008). If the inhibitors we have designed can weaken the tyrosinase activity as well as scavenge ROS effectively, the production of melanin and the damage of ROS to our human beings will be decreased to a great extent. Hence, tyrosinase inhibitors have become increasingly important in cosmetic (Guevara and Pandya, 2001) and medicinal (Kanost et al., 2004) industry, the food industry (Lunadei et al., 2011) and agriculture (Guerrero and Rosell, 2005) to prevent hyperpigmentation.In recent years, a large number of naturally occurring and synthetic tyrosinase inhibitors have been reported. There are many tyrosinase inhibitors, such as hydroquinone (Garcia and Fulton Jr, 1996), ascorbic acid (Kameyama et al., 1996), arbutin (Nakajima et al., 1998), kojic acid (Mishima et al., 1994, aromatic aldehydes (Jimenez et al., 2001;, aromatic acids (Chen et al., 2005;Si et a...

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Tyrosinase inhibition by isophthalic acid: Kinetics and computational simulation

Cited by 71 publications

References 32 publications

Effect of hesperetin on tyrosinase: Inhibition kinetics integrated computational simulation study

Effect of hesperetin on tyrosinase: Inhibition kinetics integrated computational simulation study

Effects of Isorhamnetin on Tyrosinase: Inhibition Kinetics and Computational Simulation

Tyrosinase Inhibitory Effects and Antioxidant Properties of Paeonol and Its Analogues

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