Mechanism and efficacy of a Zingiber cassumunar-derived peptide in tyrosinase inhibition and melanin suppression in B16F10 cells and zebrafish embryos

Abstract

This study investigates the bioactive potential of the peptide DGIFVLNY (DY-8), derived from the rhizomes of Zingiber cassumunar, a medically important plant with extensive traditional medicinal functions and bioactivities, for its potential application in bio-based cosmetic and personal care products. The findings based on molecular docking reveal the ability of this peptide to bind to the active tyrosinase site, with inhibitory effects. To investigate this inhibitory process further, the peptides were synthesized for testing. The findings presented the inhibition of tyrosinase with an IC50 value of 0.18 ± 0.01 μg/mL for the mono-phenolase activity, rising to 0.81 ± 0.06 μg/mL for the di-phenolase activity. Construction of a Lineweaver-Burk plot revealed competitive type inhibition. The peptide was employed at various concentrations in the range of 0–100 μM in order to treat B16F10 cells. The outcome revealed the absence of significant cytotoxicity. The peptide was shown to significantly inhibit tyrosinase activity and by extension reduce the production of melanin. Further examination of the inhibition of melanin synthesis was carried out via qRT-PCR (quantitative reverse transcription polymerase chain reaction) involving MITF (microphthalmia-associated transcription factor), TYR (tyrosinase), TRP-1 (tyrosinase-related protein-1), and TRP-2 (tyrosinase-related protein-2). The in vivo efficacy of DY-8 was further validated in zebrafish embryos, where a significant reduction in pigmentation was observed. These findings highlight DY-8 as a promising, sustainable, and natural bio-based ingredient for the cosmetic and personal care industries, emphasizing the industrial potential of Zingiber cassumunar in developing functional skincare products.