ArticleBiomolecules2025
The Inhibitory Effect of Peptide Hydrolysate of Type I Collagen Derived from Pig Skin on Melanogenesis in B16F10 Melanoma Cells.
Article in Biomolecules, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed.
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Collagen peptides, as a natural source of peptides, possess multiple advantages such as anti-aging, anti-inflammatory properties, tissue repair, and the ability to inhibit melanin production. In this study, type I collagen extracted from pig skin was hydrolyzed with 1% and 3% hydrochloric acid, yielding collagen peptides CPH1 and CPH3. The melanin content and tyrosinase activity in B16F10 cells were compared via direct and paracrine action when CPH1 and CPH3 were used to interfere with melanogenesis. It was found that CPH3 significantly inhibited melanogenesis in B16F10 through the paracrine action involving HaCaT keratinocytes. The intracellular melanin content was measured at 65.23 ± 1.30%, and the mRNA levels of tyrosinase and microphthalmia transcription factor in cells were 55.77 ± 6.09% and 50.70 ± 8.18% of the negative control, respectively. Furthermore, pigment deposition assays in zebrafish showed that, at a concentration of 1.0 mg/mL, CPH3 significantly inhibited melanogenesis compared to the negative control. Finally, tyrosinase inhibitory peptides were identified from CPH3 through peptide segment sequence identification and molecular dynamics simulation. The peptides of Nona-AGPPGFPGA, Octa-APGPVGPA, and Octa-GLPGPPGP have a double effect on the inhibition of tyrosinase and melanin content in B16F10 cells.
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