Hai-Biao Gong, Ye Yue, Si Tan, Qi Wang, Xiao-Yuan Gu, Chang‐Yu Yan, Yufei Wang, Yi‐Ning Chen, Shisheng Chen, Jianwen Ye, Wan‐Yang Sun, Weixi Li, Kun Li, Jing‐Hao Wang, Hiroshi Kurihara, Yi‐Fang Li, Rong‐Rong He
Despite the known benefits of tea ( Camellia sinensis ), the functional potential of tea-derived proteins remains largely unexplored. To investigate this, tea proteins were extracted and enzymatically hydrolyzed with alkaline protease to obtain tea protein hydrolysates (TPH). Characterized by ultra performance liquid chromatography tandem mass spectrometry (UPLC-MS/MS), TPH were screened via integrated in silico and molecular docking for dual-action peptides targeting tyrosinase inhibition and antioxidant activity. Two peptides, EGFG and FGDPHG, were identified and validated as potential tyrosinase inhibitors and antioxidants, exhibiting strong free radical scavenging and iron-chelating capabilities in cell-free systems. In B16-F10 melanoma cells, both peptides significantly reduced α-melanocyte-stimulating hormone (α-MSH)-induced melanogenesis and protected against hydrogen peroxide (H 2 O 2 )-induced oxidative stress. Their whitening efficacy was further confirmed in a zebrafish model. These findings establish EGFG and FGDPHG as novel, dual-action whitening peptides, highlighting their potential as functional ingredients in cosmetics and nutraceuticals.