文献类型：期刊文献

英文题名：In Vitro In Silico Screening Strategy and Mechanism of Novel Tyrosinase Inhibitory Peptides from Nacre of Hyriopsis cumingii

作者：Lin, Haisheng[1,2,3];Li, Fei[1];Kang, Jiaao[1];Xie, Shaohe[4];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];Song, Wenkui[1,2,3]

机构：[1]Coll Food Sci & Technol, Guangdong Prov Key Lab Aquat Prod Proc & Safety, Guangdong Prov Engn Technol Res Ctr Seafood, Guangdong Prov Engn Lab Marine Biol Prod,Key Lab, 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：9

外文期刊名：MARINE DRUGS

收录：SCI-EXPANDED(收录号：WOS:001326464000001)、、WOS

基金：This work was supported by the earmarked fund for the China Agriculture Research System funded by X.Q. (CARS-49), the Doctoral Startup Project of Guangdong Ocean University funded by W.S. and H.L. (R20076 and R17082, respectively), the Guangdong Province Modern Agricultural Industry Technology System Innovation Team Construction Project funded by H.Z. (Grant No. 2023KJ146), Undergraduate innovation team of Guangdong Ocean University funded by J.K. (CXTD2021004) and Innovation and entrepreneurship training program for college students of Guangdong Ocean University funded by J.K.(S202310566017). .

语种：英文

外文关键词：Hyriopsis cumingii; molecular docking; melanogenesis; antioxidant

外文摘要：For thousands of years, pearl and nacre powders have been important traditional Chinese medicines known for their skin whitening effects. To prepare the enzymatic hydrolysates of Hyriopsis cumingii nacre powder (NP-HCH), complex enzymatic hydrolysis by pineapple protease and of neutral protease was carried out after the powder was pre-treated with a high-temperature and high-pressure method. The peptides were identified using LC-MS/MS and picked out through molecular docking and molecular dynamics simulations. Subsequently, the tyrosinase inhibitory and antioxidant properties of novel tyrosinase inhibitory peptides were investigated in vitro. In addition, the enzymatic activity of tyrosinase in B16F10 cells as well as melanin content and antioxidant enzyme levels were also examined. The results showed that a tyosinase inhibitory peptide (Tyr-Pro-Asn-Pro-Tyr, YPNPY) with an efficient IC50 value of 0.545 +/- 0.028 mM was identified. The in vitro interaction results showed that YPNPY is a reversible competitive inhibitor of tyrosinase, suggesting that it binds to the free enzyme. The B16F10 cell whitening test revealed that YPNPY can reduce the melanin content of B16F10 cells by directly inhibiting the activity of intracellular tyrosinase. Additionally, it indirectly affects melanin production by acting as an antioxidant. These results suggest that YPNPY could be widely used as a tyrosinase inhibitor in whitening foods and drugs.