Identification of egg protein-derived peptides as xanthine oxidase inhibitors: virtual hydrolysis, molecular docking, and in vitro activity evaluation
The purpose of this study was to screen the xanthine oxidase (XO) inhibitory peptides from egg white proteins through virtual hydrolysis, in vitro activity validation, and molecular docking. The results demonstrated that tripeptide EEK from ovalbumin exhibited potent XO inhibitory activity with an I...
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| Format: | Article |
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Tsinghua University Press
2022-11-01
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| Series: | Food Science and Human Wellness |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2213453022001008 |
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| author | Zhipeng Yu Yaxin Cao Ruotong Kan Huizhuo Ji Wenzhu Zhao Sijia Wu Jingbo Liu David Shiuan |
| author_facet | Zhipeng Yu Yaxin Cao Ruotong Kan Huizhuo Ji Wenzhu Zhao Sijia Wu Jingbo Liu David Shiuan |
| author_sort | Zhipeng Yu |
| collection | DOAJ |
| description | The purpose of this study was to screen the xanthine oxidase (XO) inhibitory peptides from egg white proteins through virtual hydrolysis, in vitro activity validation, and molecular docking. The results demonstrated that tripeptide EEK from ovalbumin exhibited potent XO inhibitory activity with an IC50 value of 141 µmol/L. The molecular docking results showed that tripeptide EEK bound with the active center of XO via 3 carbon hydrogen bond interactions, 2 salt bridges, 5 conventional hydrogen bond interactions, and 4 attractive charge interactions. The residues Glu802, Phe1009, and Arg880 may play key roles in the XO catalytic reaction. Especially, the key intermolecular forces of inhibiting XO activity may be special type of hydrogen bonds including carbon hydrogen bond interactions and attraction charge interactions. The novel tripeptide EEK is potential candidates for controlling hyperuricemia. |
| format | Article |
| id | doaj-art-8eaf4e1f476e4e6595064666eb392022 |
| institution | Kabale University |
| issn | 2213-4530 |
| language | English |
| publishDate | 2022-11-01 |
| publisher | Tsinghua University Press |
| record_format | Article |
| series | Food Science and Human Wellness |
| spelling | doaj-art-8eaf4e1f476e4e6595064666eb3920222025-02-02T23:24:56ZengTsinghua University PressFood Science and Human Wellness2213-45302022-11-0111615911597Identification of egg protein-derived peptides as xanthine oxidase inhibitors: virtual hydrolysis, molecular docking, and in vitro activity evaluationZhipeng Yu0Yaxin Cao1Ruotong Kan2Huizhuo Ji3Wenzhu Zhao4Sijia Wu5Jingbo Liu6David Shiuan7School of Food Science and Engineering, Hainan University, Haikou 570228, ChinaCollege of Food Science and Engineering, Bohai University, Jinzhou 121013, ChinaCollege of Food Science and Engineering, Bohai University, Jinzhou 121013, ChinaCollege of Food Science and Engineering, Bohai University, Jinzhou 121013, ChinaSchool of Food Science and Engineering, Hainan University, Haikou 570228, China; Corresponding author.Lab of Nutrition and Functional Food, Jilin University, Changchun 130062, ChinaLab of Nutrition and Functional Food, Jilin University, Changchun 130062, ChinaInstitute of Drug Discovery Technology, Ningbo University, Ningbo 315211, ChinaThe purpose of this study was to screen the xanthine oxidase (XO) inhibitory peptides from egg white proteins through virtual hydrolysis, in vitro activity validation, and molecular docking. The results demonstrated that tripeptide EEK from ovalbumin exhibited potent XO inhibitory activity with an IC50 value of 141 µmol/L. The molecular docking results showed that tripeptide EEK bound with the active center of XO via 3 carbon hydrogen bond interactions, 2 salt bridges, 5 conventional hydrogen bond interactions, and 4 attractive charge interactions. The residues Glu802, Phe1009, and Arg880 may play key roles in the XO catalytic reaction. Especially, the key intermolecular forces of inhibiting XO activity may be special type of hydrogen bonds including carbon hydrogen bond interactions and attraction charge interactions. The novel tripeptide EEK is potential candidates for controlling hyperuricemia.http://www.sciencedirect.com/science/article/pii/S2213453022001008Egg protein-derived peptidesHyperuricemiaInhibitor mechanismMolecular dockingXanthine oxidase |
| spellingShingle | Zhipeng Yu Yaxin Cao Ruotong Kan Huizhuo Ji Wenzhu Zhao Sijia Wu Jingbo Liu David Shiuan Identification of egg protein-derived peptides as xanthine oxidase inhibitors: virtual hydrolysis, molecular docking, and in vitro activity evaluation Food Science and Human Wellness Egg protein-derived peptides Hyperuricemia Inhibitor mechanism Molecular docking Xanthine oxidase |
| title | Identification of egg protein-derived peptides as xanthine oxidase inhibitors: virtual hydrolysis, molecular docking, and in vitro activity evaluation |
| title_full | Identification of egg protein-derived peptides as xanthine oxidase inhibitors: virtual hydrolysis, molecular docking, and in vitro activity evaluation |
| title_fullStr | Identification of egg protein-derived peptides as xanthine oxidase inhibitors: virtual hydrolysis, molecular docking, and in vitro activity evaluation |
| title_full_unstemmed | Identification of egg protein-derived peptides as xanthine oxidase inhibitors: virtual hydrolysis, molecular docking, and in vitro activity evaluation |
| title_short | Identification of egg protein-derived peptides as xanthine oxidase inhibitors: virtual hydrolysis, molecular docking, and in vitro activity evaluation |
| title_sort | identification of egg protein derived peptides as xanthine oxidase inhibitors virtual hydrolysis molecular docking and in vitro activity evaluation |
| topic | Egg protein-derived peptides Hyperuricemia Inhibitor mechanism Molecular docking Xanthine oxidase |
| url | http://www.sciencedirect.com/science/article/pii/S2213453022001008 |
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