Synthesis and biological evaluation of novel 4-hydroxybenzaldehyde derivatives as tyrosinase inhibitors

Yi, Wei; Cao, Rihui; Peng, Wenlie; Wen, Huan; Yan, Qin; Zhou, Binhua P.; Ma, Lin; Song, Huacan

doi:10.1016/j.ejmech.2009.11.007

Cited by 91 publications

(46 citation statements)

References 22 publications

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“…We hypothesized that the aldehyde (CHO) functional group of arabinose participates in blocking catalysis and inducing unfolding by binding to tyrosinase. Previous findings show the importance of aldehyde groups in tyrosinase inhibition [27][28][29] in terms of molecular position, number, and specific interactions with the enzyme; these findings further support our hypothesis. Experimentally, arabinose exerted a mixed-type of inhibition on tyrosinase.…”

Section: Introductionsupporting

confidence: 90%

Kinetic, structural and molecular docking studies on the inhibition of tyrosinase induced by arabinose

Park

et al. 2012

International Journal of Biological Macromolecules

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Section: Introductionsupporting

confidence: 90%

Kinetic, structural and molecular docking studies on the inhibition of tyrosinase induced by arabinose

Park

et al. 2012

International Journal of Biological Macromolecules

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“…Previous reports confirmed that tyrosinase was one of the main causes of most fruits and vegetables quality loss during post harvest handling and processing, leading to faster degradation and shorter shelf life (Yi et al, 2010). Tyrosinase has also been linked to Parkinson's and other neurodegenerative diseases (Zhu et al, 2011).…”

Section: Introductionmentioning

confidence: 95%

“…The spectrophotometric assay for tyrosinase was performed according to the method reported by our groups with some slight modifications (Liu et al, 2008;Yi et al, 2010). Briefly, all the synthesised compounds were screened for the diphenolase inhibitory activity of tyrosinase using L-DOPA as substrate.…”

Section: Tyrosinase Assaymentioning

confidence: 99%

Biological evaluation of coumarin derivatives as mushroom tyrosinase inhibitors

Liu¹,

Wu²,

Lingjuan³

et al. 2012

Food Chemistry

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“…Arbutin, a structural analog of hydroquinone, can be metabolized into hydroquinone (Blaut et al, 2006), increasing the possibility of getting cancer. Thus, much research has identified tyrosinase inhibitors synthesized in the laboratory (Kubo et al, 2000;Shiino et al, 2001;Jun et al, 2007;Jirawattanapong et al, 2009;Delogu et al, 2010;Yi et al, 2010;Cha et al, 2011;Tajima et al, 2011;Song et al, 2012;Hamidian, 2013;Hamidian et al, 2013;Zhu et al, 2013) and extracted from plants (Piao et al, 2009;Sung et al, 2009;Chang et al, 2011;Liang et al, 2012;Zheng et al, 2012;Sarkhail et al, 2013). Some attention has been drawn to applying peptide sequences for tyrosinase inhibition; however, most of them are fragments isolated from known proteins and peptide-derived compounds.…”

Section: Introductionmentioning

confidence: 99%

Phage Display–Mediated Discovery of Novel Tyrosinase-Targeting Tetrapeptide Inhibitors Reveals the Significance of N-Terminal Preference of Cysteine Residues and Their Functional Sulfur Atom

et al. 2014

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Tyrosinase, a key copper-containing enzyme involved in melanin biosynthesis, is closely associated with hyperpigmentation disorders, cancer, and neurodegenerative diseases, and as such, it is an essential target in medicine and cosmetics. Known tyrosinase inhibitors possess adverse side effects, and there are no safety regulations; therefore, it is necessary to develop new inhibitors with fewer side effects and less toxicity. Peptides are exquisitely specific to their in vivo targets, with high potencies and relatively few off-target side effects. Thus, we systematically and comprehensively investigated the tyrosinase-inhibitory abilities of N-and C-terminal cysteine/tyrosine-containing tetrapeptides by constructing a phage-display random tetrapeptide library and conducting computational molecular docking studies on novel tyrosinase tetrapeptide inhibitors. We found that N-terminal cysteine-containing tetrapeptides exhibited the most potent tyrosinase-inhibitory abilities. The positional preference of cysteine residues at the N terminus in the tetrapeptides significantly contributed to their tyrosinase-inhibitory function. The sulfur atom in cysteine moieties of N-and C-terminal cysteine-containing tetrapeptides coordinated with copper ions, which then tightly blocked substrate-binding sites. N-and C-terminal tyrosinecontaining tetrapeptides functioned as competitive inhibitors against mushroom tyrosinase by using the phenol ring of tyrosine to stack with the imidazole ring of His263, thus competing for the substrate-binding site. The N-terminal cysteine-containing tetrapeptide CRVI exhibited the strongest tyrosinase-inhibitory potency (with an IC 50 of 2.7 6 0.5 mM), which was superior to those of the known tyrosinase inhibitors (arbutin and kojic acid) and outperformed kojic acid-tripeptides, mimosine-FFY, and shortsequence oligopeptides at inhibiting mushroom tyrosinase.

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Synthesis and biological evaluation of novel 4-hydroxybenzaldehyde derivatives as tyrosinase inhibitors

Cited by 91 publications

References 22 publications

Kinetic, structural and molecular docking studies on the inhibition of tyrosinase induced by arabinose

Kinetic, structural and molecular docking studies on the inhibition of tyrosinase induced by arabinose

Biological evaluation of coumarin derivatives as mushroom tyrosinase inhibitors

Phage Display–Mediated Discovery of Novel Tyrosinase-Targeting Tetrapeptide Inhibitors Reveals the Significance of N-Terminal Preference of Cysteine Residues and Their Functional Sulfur Atom

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