文献类型：期刊文献

英文题名：In Silico Identification and Molecular Mechanism of Novel Tyrosinase Inhibitory Peptides Derived from Nacre of Pinctada martensii

作者：Li, Fei[1];Lin, Haisheng[1,2,3];Qin, Xiaoming[1,2,3];Gao, Jialong[1,2,3];Chen, Zhongqin[1,2,3];Cao, Wenhong[1,2,3];Zheng, Huina[1,2,3];Xie, Shaohe[4]

机构：[1]Guangdong Ocean Univ, Coll Food Sci & Technol, Natl Res & Dev Branch Ctr Shellfish Proc Zhanjian, Guangdong Prov Engn Technol Res Ctr Seafood,Guang, Zhanjiang 524088, Peoples R China;[2]Guangdong Ocean Univ, Shenzhen Inst, Shenzhen 518108, Peoples R China;[3]Dalian Polytech Univ, Collaborat Innovat Ctr Seafood Deep Proc, Dalian 116034, Peoples R China;[4]Guangdong Shaohe Pearl Co Ltd, Shantou 515041, Peoples R China

年份：2024

卷号：22

期号：8

外文期刊名：MARINE DRUGS

收录：SCI-EXPANDED(收录号：WOS:001306730300001)、、WOS

基金：This work was supported by the earmarked fund for China Agriculture Research System (CARS-49), Doctoral Startup Project of Guangdong Ocean University (R17082), the Guangdong Province Modern Agricultural Industry Technology System Innovation Team Construction Project (Grant No. 2023KJ146), the Innovative Team Program of High Education of Guangdong Province (2021KCXTD021).

语种：英文

外文关键词：Pinctada martensii; molecular docking; melanogenesis; antioxidant

外文摘要：Pearl and nacre powders have been valuable traditional Chinese medicines with whitening properties for thousands of years. We utilized a high-temperature and high-pressure method along with compound enzyme digestion to prepare the enzymatic hydrolysates of nacre powder of Pinctada martensii (NP-PMH). The peptides were identified using LC-MS/MS and screened through molecular docking and molecular dynamics simulations. The interactions between peptides and tyrosinase were elucidated through enzyme kinetics, circular dichroism spectropolarimetry, and isothermal titration calorimetry. Additionally, their inhibitory effects on B16F10 cells were explored. The results showed that a tyrosinase-inhibitory peptide (Ala-His-Tyr-Tyr-Asp, AHYYD) was identified, which inhibited tyrosinase with an IC50 value of 2.012 +/- 0.088 mM. The results of the in vitro interactions showed that AHYYD exhibited a mixed-type inhibition of tyrosinase and also led to a more compact enzyme structure. The binding reactions of AHYYD with tyrosinase were spontaneous, leading to the formation of a new set of binding sites on the tyrosinase. The B16F10 cell-whitening assay revealed that AHYYD could reduce the melanin content of the cells by directly inhibiting the activity of intracellular tyrosinase. Additionally, it indirectly affects melanin production by acting as an antioxidant. These results suggest that AHYYD could be widely used as a tyrosinase inhibitor in whitening foods and pharmaceuticals.