Novel peptides with tyrosinase inhibitory activity

Schurink, Marloes; Berkel, Willem J.H. van; Wichers, Harry J.; Boeriu, Carmen G.

doi:10.1016/j.peptides.2006.11.023

Cited by 169 publications

(173 citation statements)

References 34 publications

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“…This difference may have caused their functional divergences in inhibiting tyrosinase, and indicates that the active Glu189 residue is important for tyrosinase binding and/or inhibition. Moreover, it was reported that good tyrosinase-inhibitory peptides preferably contain arginine in combination with valine, alanine, and/or leucine (Schurink et al, 2007); this was obviously observed in our screened tetrapeptides, CRVI, KARC, and RAQC. Molecular models of the active site of tyrosinase of C-and N-terminal tyrosine-containing tetrapeptides revealed that tyrosine residues of tyrosine-containing tetrapeptides were most likely to interact with copper ions as well, regardless of being located at the N or C terminus.…”

Section: Discussionsupporting

confidence: 63%

“…Thus, several studies made efforts to find novel proteins and peptides from natural resources, such as silk (Kato et al, 1998), milk (Nakajima et al, 1996;Chen et al, 2006), honey (Oszmianski, 1990;Ates and Cokmus, 2001), wheat (Okot-Kotber et al, 2001), and the housefly (Daquinag et al, 1995(Daquinag et al, , 1999, for tyrosinase inhibition. On top of that, dipeptides (Girelli et al, 2004), kojic acid tripeptides (Noh et al, 2007), mimosine tetrapeptides (Upadhyay et al, 2011), cyclic peptides (Morita et al, 1994), short-sequence oligopeptides (Abu Ubeid et al, 2009), and octameric peptides (Schurink et al, 2007) were also investigated for their tyrosinase-inhibitory abilities. Herein without precedent, we systematically and comprehensively investigated C-and N-terminal cysteine/tyrosine-containing tetrapeptides for tyrosinase inhibition and found that the CRVI tetrapeptide showed the strongest mushroom tyrosinase-inhibitory potency.…”

Section: Discussionmentioning

confidence: 99%

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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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Section: Discussionsupporting

confidence: 63%

Section: Discussionmentioning

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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“…In the human melanogenesis, tyrosinase plays a key role in catalyzing the hydroxylation of monophenols (tyrosine) to ο-diphenols and their subsequent oxidation to ο-quinones (Husni et al, 2011). Furthermore, tyrosinase was reported to be related to cancer and some neurodegenerative diseases (Schurink et al, 2007). And the tyrosinase inhibitors have been studied for the cosmetics and pharmaceutical applications.…”

Section: Discussionmentioning

confidence: 99%

Potential Biological Activities of Magnoflorine: A Compound from Aristolochia debilis Sieb. et Zucc

Li¹,

Wang²

2014

Korean Journal of Plant Resources

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-Magnoflorine, an important compound in Aristolochia, was usually used as an anxiolytic chemical. In this study, the magnoflorine was isolated from Aristolochia and the biological activities such as antioxidant, α-tyrosinase inhibitory, anti-inflammatory, and anticancer activities were investigated. The magnoflorine showed significant antioxidant activity as a 2,2-diphenyl-2-picryl-hydrazyl (DPPH) free radical scavenger, 50 µg/mL of the magnoflorine scavenged about 70.8% of all the free radicals. And it was good at α-tyrosinase inhibiting, 100 µg/mL of the magnoflorine inhibited 36.5% of the tyrosinase. High dosage of magnoflorine inhibited the inflammation production nitric oxide (NO), and the magnoflorine protected the murine macrophage cells (RAW 264.7) from LPS-induced apoptosis. The cell viability of human colon cancer calls (HT-29) was around 100% when treated with different dose of magnoflorine, it's suggesting that magnoflorine had no anticancer effect.

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“…Tyrosinases are copper-containing enzymes that catalyse the ortho-hydroxylation of monophenols to catechols and their subsequent oxidation to ortho-quinones (Schurink et al, 2007). Tyrosinases are known to play roles in cancer and neurodegenerative diseases such as parkinson's disease (Aramwit et al, 2010;Cavalieri et al, 2002).…”

Section: Anti-proliferative Action Of the Cordycepin Extracted Towardmentioning

confidence: 99%

An Anti-Cancer Cordycepin Produced by Cordyceps militaris Growing on the Dead Larva of Bombyx mori Silkworm

Aramwit¹,

Bang²,

Ratanavaraporn³

et al. 2014

JAS

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In this study, we introduced the dead pupa and larva of Bombyx mori silkworms as nutrition medium for the growing of different fungi including Cordyceps militaris, Isaria tenuipes and Isaria farinose to produce Cordyceps mycelia and anti-cancer cordycepin. The anti-proliferative and anti-migratory activities of cordycepin extracted toward cancer cells were investigated. We found that the dead silk larva which contained high carbohydrate and moisture but low fat content could be a good host for the growth of Cordyceps militaris and Isaria tenuipes to produce Cordyceps. The cordycepin extracted from Cordyceps mycelia of Cordyceps militaris grown on dead silk larva showed the highest anti-proliferative potential toward human non-small cell lung cancer NCI-H460 cells with a half maximal inhibitory concentration (IC 50 ) of 0.7 µM. Furthermore, the viability of human lung adenocarcinoma epithelial A549 cell line remained < 20% while that of human airway epithelial Calu-3 cell line was < 40% after treated with the cordycepin extracted (0.125-2 µM) due to the disruption of cell membrane by cordycepin. We also found that our cordycepin (0.25-2 µM) could inhibit the migration of A549 cells. On the other hand, the cordycepin was not toxic to small airway epithelial cells (SAEC) of non-cancer cells. Therefore, Cordyceps militaris grown on the dead larva of B. mori silkworms was introduced as a promising source for the production of Cordyceps mycelia and anti-cancer cordycepin without toxicity to non-cancer cells.

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Novel peptides with tyrosinase inhibitory activity

Cited by 169 publications

References 34 publications

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

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

Potential Biological Activities of Magnoflorine: A Compound from Aristolochia debilis Sieb. et Zucc

An Anti-Cancer Cordycepin Produced by Cordyceps militaris Growing on the Dead Larva of Bombyx mori Silkworm

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