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Cited by 15melanin and skin pigmentationBioactive natural compoundsMelanoma and MAPK Pathways

Brassinin Abundant in Brassicaceae Suppresses Melanogenesis through Dual Mechanisms of Tyrosinase Inhibition

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Lee, Min-Kyeong, Ryu, Heeyeon, Jeong, Hyeon Hak, Lee, Bonggi·2022·Foods
DOI 10.3390/foods12010121PMC PMC9818315
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Abstract

Brassinin is a phytoalexin abundant in plants, especially in cabbage, and has been reported to act as an anti-cancer and anti-inflammatory agent. However, limited studies are available to elucidate the functionalities of brassinin. Here, we tested the effects of brassinin on melanogenesis using cell-free and cell-based biochemical analysis and docking simulation. Cell-free experiments exhibited that brassinin has antioxidant and anti-tyrosinase activities. When applied to B16F10 cells stimulated with a melanogenesis inducer α-MSH, brassinin pretreatment significantly reduced melanin accumulation and cellular tyrosinase activity. Docking simulation indicates that the docking score of brassinin to the binding pocket of tyrosinase is better than that of kojic acid or arbutin, anti-melanogenic positive controls, indicating that brassinin inhibits melanogenesis at least partially by binding to and inactivating tyrosinase. In addition, qPCR results showed that brassinin reduced tyrosinase mRNA levels. Together, these results suggest that brassinin exerts anti-melanogenesis effects by inhibiting both the activity and mRNA expression levels of tyrosinase. Therefore, our study showed that brassinin has the potential to be used in pharmaceutical or cosmetic products for depigmentation.

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  • Even if melanin precursors are synthesized normally, inhibitors can target enzymes involved in the oxidative polymerization step, such as LAC or tyrosinase, to prevent the final formation of melanin.

    “Even if melanin precursors are synthesized normally, inhibitors can target enzymes involved in the oxidative polymerization step, such as LAC or tyrosinase, to prevent the final formation of melanin [94,95].”

    From Fungal Melanin in Plant Pathogens: Complex Biosynthesis Pathways and Diverse Biological Functions (2025) · cites this paper as [95]

    The Introduction (page unavailable) says tyrosinase oxidizes L-DOPA and that tyrosinase inhibitors can suppress pigmentation; the Discussion (page unavailable) reports that brassinin suppresses tyrosinase activity. But the Introduction places tyrosinase at the initial step of melanogenesis, not a final oxidative-polymerization step after precursors have formed. The paper does not address LAC. (LLM, conf=0.88)

    Experimental — accuracy not yet measured

  • This prevents the oxidative polymerization of DHN into melanin, thereby attenuating pathogen virulence.

    “This prevents the oxidative polymerization of DHN into melanin, thereby attenuating pathogen virulence.”

    From Fungal Melanin in Plant Pathogens: Complex Biosynthesis Pathways and Diverse Biological Functions (2025) · cites this paper as [95]

    The Introduction describes tyrosinase-mediated conversion of L-tyrosine and L-DOPA in melanogenesis, while the Discussion reports that brassinin suppresses melanogenesis in B16F10 cells (pages not provided). Searches for DHN polymerization and pathogen virulence found no passage addressing either point, so this copy cannot verify the attributed claim. (LLM, conf=0.76)

    Experimental — accuracy not yet measured

  • Certain inhibitors bind to the copper ion active center of LAC, decreasing its oxidizing capacity.

    “For example, certain inhibitors bind to the copper ion active center of LAC, decreasing its oxidizing capacity.”

    From Fungal Melanin in Plant Pathogens: Complex Biosynthesis Pathways and Diverse Biological Functions (2025) · cites this paper as [95]

    The Introduction describes tyrosinase as a copper-containing oxidase, and the Discussion suggests brassinin may bind its active site and reduce its activity. Neither section identifies LAC or says inhibitors bind LAC’s copper-ion center. Searches for LAC, laccase, and copper-center binding found no passage addressing that mechanism. (LLM, conf=0.76)

    Experimental — accuracy not yet measured

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Cited by

Sorted by citations

Authors
Lee, M.-K., Ryu, H., Jeong, H. H., & Lee, B.
Affiliations
Pukyong National University (KR)
Corresponding author
Lee, Bonggi
ORCID
Venue
Foods
Publisher
MDPI AG
Published
2022-12-26
Volume
12
Issue
1
Pages
121
ISSN
2304-8158 (ISSN-L)
DOI
10.3390/foods12010121
PMC
PMC9818315
OpenAlex
W4313260155
Cited by
15
References
0
Citations by year
2026: 4 · 2025: 3 · 2024: 6 · 2023: 2
FWCI
1.47
Type
journal article
Language
en
Open access
Licence
Locations
  • Foods (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
Funders
Pukyong National University (2022, 202205990001)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › melanin and skin pigmentation
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bioactive natural compounds
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Melanoma and MAPK Pathways
Keywords
brassinin, phytoalexins, melanogenesis, tyrosinase inhibition, anti-melanogenic activity, B16F10 melanoma cells, alpha-melanocyte-stimulating hormone, antioxidant activity, depigmentation, Brassicaceae, kojic acid, arbutin, molecular docking

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