In Vitro In Silico Screening Strategy and Mechanism of Novel Tyrosinase Inhibitory Peptides from Nacre of <i>Hyriopsis cumingii</i>
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 <i>Hyriopsis cumingii</i> nacre powder (NP-HCH), complex enzymatic hydrolysis by pineapple protease and of ne...
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2024-09-01
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| author | Haisheng Lin Fei Li Jiaao Kang Shaohe Xie Xiaoming Qin Jialong Gao Zhongqin Chen Wenhong Cao Huina Zheng Wenkui Song |
| author_facet | Haisheng Lin Fei Li Jiaao Kang Shaohe Xie Xiaoming Qin Jialong Gao Zhongqin Chen Wenhong Cao Huina Zheng Wenkui Song |
| author_sort | Haisheng Lin |
| collection | DOAJ |
| description | 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 <i>Hyriopsis cumingii</i> 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 IC<sub>50</sub> 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. |
| format | Article |
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| issn | 1660-3397 |
| language | English |
| publishDate | 2024-09-01 |
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| series | Marine Drugs |
| spelling | doaj-art-86250f015e2a4a1e91535d78b73f41ef2025-08-20T01:55:38ZengMDPI AGMarine Drugs1660-33972024-09-0122942010.3390/md22090420In Vitro In Silico Screening Strategy and Mechanism of Novel Tyrosinase Inhibitory Peptides from Nacre of <i>Hyriopsis cumingii</i>Haisheng Lin0Fei Li1Jiaao Kang2Shaohe Xie3Xiaoming Qin4Jialong Gao5Zhongqin Chen6Wenhong Cao7Huina Zheng8Wenkui Song9Guangdong Provincial Key Laboratory of Aquatic Products Processing and Safety, National Research and Development Branch Center for Shellfish Processing (Zhanjiang), Guangdong Provincial Engineering Technology Research Center of Seafood, Guangdong Province Engineering Laboratory for Marine Biological Products, College of Food Science and Technology, Guangdong Ocean University, Zhanjiang 524088, ChinaGuangdong Provincial Key Laboratory of Aquatic Products Processing and Safety, National Research and Development Branch Center for Shellfish Processing (Zhanjiang), Guangdong Provincial Engineering Technology Research Center of Seafood, Guangdong Province Engineering Laboratory for Marine Biological Products, College of Food Science and Technology, Guangdong Ocean University, Zhanjiang 524088, ChinaGuangdong Provincial Key Laboratory of Aquatic Products Processing and Safety, National Research and Development Branch Center for Shellfish Processing (Zhanjiang), Guangdong Provincial Engineering Technology Research Center of Seafood, Guangdong Province Engineering Laboratory for Marine Biological Products, College of Food Science and Technology, Guangdong Ocean University, Zhanjiang 524088, ChinaGuangdong Shaohe Pearl Co., Ltd., Shantou 515041, ChinaGuangdong Provincial Key Laboratory of Aquatic Products Processing and Safety, National Research and Development Branch Center for Shellfish Processing (Zhanjiang), Guangdong Provincial Engineering Technology Research Center of Seafood, Guangdong Province Engineering Laboratory for Marine Biological Products, College of Food Science and Technology, Guangdong Ocean University, Zhanjiang 524088, ChinaGuangdong Provincial Key Laboratory of Aquatic Products Processing and Safety, National Research and Development Branch Center for Shellfish Processing (Zhanjiang), Guangdong Provincial Engineering Technology Research Center of Seafood, Guangdong Province Engineering Laboratory for Marine Biological Products, College of Food Science and Technology, Guangdong Ocean University, Zhanjiang 524088, ChinaGuangdong Provincial Key Laboratory of Aquatic Products Processing and Safety, National Research and Development Branch Center for Shellfish Processing (Zhanjiang), Guangdong Provincial Engineering Technology Research Center of Seafood, Guangdong Province Engineering Laboratory for Marine Biological Products, College of Food Science and Technology, Guangdong Ocean University, Zhanjiang 524088, ChinaGuangdong Provincial Key Laboratory of Aquatic Products Processing and Safety, National Research and Development Branch Center for Shellfish Processing (Zhanjiang), Guangdong Provincial Engineering Technology Research Center of Seafood, Guangdong Province Engineering Laboratory for Marine Biological Products, College of Food Science and Technology, Guangdong Ocean University, Zhanjiang 524088, ChinaGuangdong Provincial Key Laboratory of Aquatic Products Processing and Safety, National Research and Development Branch Center for Shellfish Processing (Zhanjiang), Guangdong Provincial Engineering Technology Research Center of Seafood, Guangdong Province Engineering Laboratory for Marine Biological Products, College of Food Science and Technology, Guangdong Ocean University, Zhanjiang 524088, ChinaGuangdong Provincial Key Laboratory of Aquatic Products Processing and Safety, National Research and Development Branch Center for Shellfish Processing (Zhanjiang), Guangdong Provincial Engineering Technology Research Center of Seafood, Guangdong Province Engineering Laboratory for Marine Biological Products, College of Food Science and Technology, Guangdong Ocean University, Zhanjiang 524088, ChinaFor 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 <i>Hyriopsis cumingii</i> 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 IC<sub>50</sub> 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.https://www.mdpi.com/1660-3397/22/9/420<i>Hyriopsis cumingii</i>molecular dockingB16F10 cellsmelanogenesisantioxidant |
| spellingShingle | Haisheng Lin Fei Li Jiaao Kang Shaohe Xie Xiaoming Qin Jialong Gao Zhongqin Chen Wenhong Cao Huina Zheng Wenkui Song In Vitro In Silico Screening Strategy and Mechanism of Novel Tyrosinase Inhibitory Peptides from Nacre of <i>Hyriopsis cumingii</i> Marine Drugs <i>Hyriopsis cumingii</i> molecular docking B16F10 cells melanogenesis antioxidant |
| title | In Vitro In Silico Screening Strategy and Mechanism of Novel Tyrosinase Inhibitory Peptides from Nacre of <i>Hyriopsis cumingii</i> |
| title_full | In Vitro In Silico Screening Strategy and Mechanism of Novel Tyrosinase Inhibitory Peptides from Nacre of <i>Hyriopsis cumingii</i> |
| title_fullStr | In Vitro In Silico Screening Strategy and Mechanism of Novel Tyrosinase Inhibitory Peptides from Nacre of <i>Hyriopsis cumingii</i> |
| title_full_unstemmed | In Vitro In Silico Screening Strategy and Mechanism of Novel Tyrosinase Inhibitory Peptides from Nacre of <i>Hyriopsis cumingii</i> |
| title_short | In Vitro In Silico Screening Strategy and Mechanism of Novel Tyrosinase Inhibitory Peptides from Nacre of <i>Hyriopsis cumingii</i> |
| title_sort | in vitro in silico screening strategy and mechanism of novel tyrosinase inhibitory peptides from nacre of i hyriopsis cumingii i |
| topic | <i>Hyriopsis cumingii</i> molecular docking B16F10 cells melanogenesis antioxidant |
| url | https://www.mdpi.com/1660-3397/22/9/420 |
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