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Novel tyrosinase-inhibitory peptides derived from Locusta migratoria protein hydrolysates: Preparation, identification and molecular docking analysis

Summary

Scientists have discovered that peptides from locusts can effectively inhibit tyrosinase, an enzyme responsible for skin pigmentation. These peptide extracts showed strong ability to prevent melanin production, comparable to existing skin-whitening agents but with much lower toxicity to normal cells. The research identified over 1100 different peptide sequences that could be useful in cosmetic and pharmaceutical products for treating age spots, freckles, and other pigmentation issues.

Background

Tyrosinase plays a pivotal role in melanin biosynthesis and excessive activation leads to skin disorders including freckles, melasma, and age spots. Current tyrosinase inhibitors have limitations in solubility, stability, and safety. Locusts are a rich protein source with potential for bioactive peptide development.

Objective

To investigate defatted locust powder as a source of tyrosinase-inhibitory peptides through enzymatic hydrolysis, identify the peptide sequences, and evaluate their molecular mechanisms and cellular safety profiles.

Results

Peptides below 1 kDa showed the strongest inhibition at 53.00% at 10 mg/mL. LC-MS/MS identified 1108 peptide sequences primarily from vitellogenin proteins. Peptides exhibited mixed-type reversible inhibition and low cytotoxicity in HEK-293 T cells with 37.26% tyrosinase inhibition in B16 melanoma cells at 2 mg/mL.

Conclusion

Locust-derived peptides represent promising natural tyrosinase inhibitors with potent bioactivity and high safety profiles. These findings support potential applications in cosmetics, pigmentation treatments, and food preservation industries.
  • Published in:Food Chemistry X,
  • Study Type:Experimental Research Study,
  • Source: 40823129
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