Identification and molecular mechanism of novel tyrosinase inhibitory peptides from collagen

Xue, Wenrui; Li, Xuan; Zhao, Wenzhu; Yu, Zhipeng

doi:10.1111/1750-3841.16160

Cited by 16 publications

(8 citation statements)

References 40 publications

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“…In this study, a dihydrochalcone moiety was chosen as the synthetic backbone, with the goal of designing superior novel tyrosinase inhibitors. As reported previously, 45,46,50,51 resorcinol is the key pharmacophore of TYR inhibitors, and compounds containing this group have good TYR inhibitory activity. To obtain more effective tyrosinase inhibitors with better permeability, we designed and synthesized a series of novel dihydrochalcone hybrids by introducing the resorcinol structure into the skeleton of dihydrochalcone (Figure 3) to explore the SAR of TYR inhibitors and identify a novel candidate agent for the potential treatment of skin hyperpigmentation.…”

Section: ■ Introductionsupporting

confidence: 63%

“…TYR inhibitors such as hydroquinone ( 4 ), arbutin ( 5 ), azelaic acid ( 6 ), l -ascorbic acid ( 7 ), ellagic acid ( 8 ), and kojic acid ( 9 ) have been used clinically and have been shown to reduce skin pigmentation and cure skin disorders (Figure ). They have been mainly used in cosmetics, with some side effects such as low skin permeation, instability, high cytotoxicity, and carcinogenicity. − Due to these factors, their applications are limited. Therefore, it is essential to develop more effective new agents with low toxicity and high skin permeability for the treatment of skin hyperpigmentation.…”

Section: Introductionmentioning

confidence: 99%

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Design, Synthesis, and Biological Evaluation of Novel Hybrids Containing Dihydrochalcone as Tyrosinase Inhibitors to Treat Skin Hyperpigmentation

Xue

et al. 2023

J. Med. Chem.

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Excessive melanin deposition may lead to a series of skin disorders. The production of melanin is carried out by melanocytes, in which the enzyme tyrosinase performs a key role. In this work, we identified a series of novel tyrosinase inhibitor hybrids with a dihydrochalcone skeleton and resorcinol structure, which can inhibit tyrosinase activity and reduce the melanin content in the skin. Compound 11c possessed the most potent activity against tyrosinase, showing IC 50 values at nanomolar concentration ranges, along with significant antioxidant activity and low cytotoxicity. Furthermore, in vitro permeation tests, supported by HPLC analysis and 3D OrbiSIMS imaging visualization, revealed the excellent permeation of 11c. More importantly, compound 11c reduced the melanin content on UV-induced skin pigmentation in a guinea pig model in vivo. These results suggest that compound 11c may serve as a promising potent tyrosinase inhibitor for the development of a potential therapy to treat skin hyperpigmentation.

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Section: ■ Introductionsupporting

confidence: 63%

Section: Introductionmentioning

confidence: 99%

Design, Synthesis, and Biological Evaluation of Novel Hybrids Containing Dihydrochalcone as Tyrosinase Inhibitors to Treat Skin Hyperpigmentation

Xue

et al. 2023

J. Med. Chem.

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“…Xue et al . (2022) reported that collagen derived peptides DGL and GAR containing residue Gly have potent tyrosinase inhibitory activity. And Gly as a hydrophobic residue, has also been found contributed to the tyrosinase inhibitory activity of protein materials (Song et al ., 2022).…”

Section: Resultsmentioning

confidence: 99%

“…In addition, all peptides DGGR, DGD, NAGE, LVGE and GSEG International Journal of Food Science and Technology 2022 contained residue Gly. Xue et al (2022) reported that collagen derived peptides DGL and GAR containing residue Gly have potent tyrosinase inhibitory activity. And Gly as a hydrophobic residue, has also been found contributed to the tyrosinase inhibitory activity of protein materials (Song et al, 2022).…”

Section: Inhibitory Effects Of Peptide On Tyrosinasementioning

confidence: 99%

Colla corii asini–derived peptides as tyrosinase inhibitors: identification, inhibitory activity and molecular mechanism

Zhao

2022

Int J of Food Sci Tech

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The aim of the present study was to investigate the effect of peptides derived from Colla corii asini on tyrosinase. The sequences of Colla corii asini-derived peptides were identified using mass spectrometry. To characterise the potential peptides with tyrosinase inhibitory activity and clarify their molecular mechanism, both in silico digestion and molecular docking were used. In addition, the tyrosinase inhibitory activities of potential peptides in vitro were also validated. The results showed that Colla corii asini consisted of 472 peptides, and most peptides derived from collagen. Peptides DGGR, DGD, NAGE, LVGE and GSEG were released from the digestion of Colla corii asini-derived peptides and possessed potent inhibitory activity against tyrosinase with IC 50 values of 0.92, 0.50, 0.77, 0.66 and 0.69 mg mL À1 , respectively. The molecular interaction results showed that hydrogen bond and van der Waals interactions are important forces in the interaction of peptides with tyrosinase. Surface forces containing aromatic interaction, hydrogen bond, hydrophilicity and solvent-accessible surface contributed to the interaction between tyrosinase and peptides.

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“…It is more effective than arbutin (a known tyrosinase inhibitor with an IC 50 value of 5.73 ± 0.01 mmol L −1 ) and Asp-Gly-Leu (a novel tyrosinase inhibitory peptide from donkey collagen, with an IC 50 value of 0.47 ± 0.01 mmol L −1 ). [20][21][22] In summary, the Spirulina tyrosinase inhibitory peptide DER can be used as a natural tyrosinase inhibitory peptide, which has activity against tyrosinase.…”

Section: Molecular Docking Of Peptides With Tyrosinasementioning

confidence: 99%

Identification and molecular docking of tyrosinase inhibitory peptides from allophycocyanin in Spirulina platensis

Yu,

Lv,

Zhou

et al. 2024

J Sci Food Agric

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BackgroundTyrosinase, a copper‐containing metalloenzyme with catalytic activity, is widely found in mammals. It is the key rate‐limiting enzyme that catalyzes melanin synthesis. For humans, tyrosinase is beneficial to the darkening of eyes and hair. However, excessive deposition of melanin in the skin can lead to dull skin color and lead to pigmentation. Therefore, many skin‐whitening compounds have been developed to decrease tyrosinase activity. This study aimed to identify a new tyrosinase inhibitory peptide through enzymatic hydrolysis, in vitro activity verification, molecular docking, and molecular dynamics simulation.ResultsA tri‐peptide Asp‐Glu‐Arg (DER) was identified, with a ‘‐CDOCKER_Energy’ value of 121.26 Kcal/mol. DER has effective tyrosinase inhibitory activity. Research shows that its half inhibitory concentration value is 1.04 ± 0.01 mmol L−1. In addition, DER binds to tyrosinase residues His85, His244, His259, and Asn260, which are key residues that drive the interaction between the peptide and tyrosinase. Finally, through Molecular Dynamics (MD) simulation, the conformational changes and structural stability of the complexes were further explored to verify and supplement the results of molecular docking.ConclusionThis experiment shows that DER can effectively inhibit tyrosinase activity. His244, His259, His260, and Asn260 are the critical residues that drive the interaction between the peptide and tyrosinase, and hydrogen bonding is an important force.DER from Spirulina has the potential to develop functional products with tyrosinase inhibition.This article is protected by copyright. All rights reserved.

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Identification and molecular mechanism of novel tyrosinase inhibitory peptides from collagen

Cited by 16 publications

References 40 publications

Design, Synthesis, and Biological Evaluation of Novel Hybrids Containing Dihydrochalcone as Tyrosinase Inhibitors to Treat Skin Hyperpigmentation

Design, Synthesis, and Biological Evaluation of Novel Hybrids Containing Dihydrochalcone as Tyrosinase Inhibitors to Treat Skin Hyperpigmentation

Colla corii asini–derived peptides as tyrosinase inhibitors: identification, inhibitory activity and molecular mechanism

Identification and molecular docking of tyrosinase inhibitory peptides from allophycocyanin in Spirulina platensis

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