Isolation, identification, and preparation of tyrosinase inhibitory peptides from Pinctada martensii meat

Meng, Jinhao; Liu, Jiaojiao; Lu, Jing; Jiang, Pingyingzi; Bai, Yunxia; Liu, Xiaoling; Li, Shubo

doi:10.1007/s10529-023-03437-0

Cited by 2 publications

(1 citation statement)

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“…Owing to extreme environmental conditions, marine organisms can produce biologically active peptides with structures and properties that differ from those of terrestrial organisms. For example, Meng et al [10] used Bacillus licheniformis protease to hydrolyze the pearl oyster Pinctada martensii. Subsequent isolation, purification, molecular docking, and bioactivity studies revealed that peptide W3 exhibited significant TYR inhibitory activity and could be used as a TYR inhibitor.…”

Section: Introductionmentioning

confidence: 99%

Anti-Melanogenic Effects of Takifugu flavidus Muscle Hydrolysate in B16F10 Melanoma Cells and Zebrafish

Hu,

Chen,

et al. 2024

Marine Drugs

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Abnormal melanogenesis can lead to hyperpigmentation. Tyrosinase (TYR), a key rate-limiting enzyme in melanin production, is an important therapeutic target for these disorders. We investigated the TYR inhibitory activity of hydrolysates extracted from the muscle tissue of Takifugu flavidus (TFMH). We used computer-aided virtual screening to identify a novel peptide that potently inhibited melanin synthesis, simulated its binding mode to TYR, and evaluated functional efficacy in vitro and in vivo. TFMH inhibited the diphenolase activities of mTYR, reducing TYR substrate binding activity and effectively inhibiting melanin synthesis. TFMH indirectly reduced cAMP response element-binding protein phosphorylation in vitro by downregulating melanocortin 1 receptor expression, thereby inhibiting expression of the microphthalmia-associated transcription factor, further decreasing TYR, tyrosinase related protein 1, and dopachrome tautomerase expression and ultimately impeding melanin synthesis. In zebrafish, TFMH significantly reduced black spot formation. TFMH (200 μg/mL) decreased zebrafish TYR activity by 43% and melanin content by 52%. Molecular dynamics simulations over 100 ns revealed that the FGFRSP (T-6) peptide stably binds mushroom TYR via hydrogen bonds and ionic interactions. T-6 (400 μmol/L) reduced melanin content in B16F10 melanoma cells by 71% and TYR activity by 79%. In zebrafish, T-6 (200 μmol/L) inhibited melanin production by 64%. TFMH and T-6 exhibit good potential for the development of natural skin-whitening cosmetic products.

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Section: Introductionmentioning

confidence: 99%