| A strategy to boost xanthine oxidase and angiotensin converting enzyme inhibitory activities of peptides via molecular docking and module substitution | |
Meng, Pengfei1,2; Wang, Yanxin1,2; Huang, Yumeng1,2; Liu, Tong1,2; Ma, Mingxia1,2; Han, Jiaojiao1,2; Su, Xiurong1,2; Li, Wenjun4 ; Wang, Yanbo3,5; Lu, Chenyang1,2,3
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| Source Publication | FOOD CHEMISTRY
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| ISSN | 0308-8146 |
| 2024-06-01 | |
| Volume | 442Pages:9 |
| Keyword | Peptide Activity boosting strategy Molecular docking Module substitution Xanthine oxidase inhibitory Angiotensin-converting enzyme inhibitory |
| DOI | 10.1016/j.foodchem.2024.138401 |
| Corresponding Author | Li, Wenjun(wjli@yic.ac.cn) ; Lu, Chenyang(luchenyang@nbu.edu.cn) |
| Abstract | Molecular docking and activity evaluation screened the dipeptide module GP with low xanthine oxidase (XOD) inhibitory activity and modules KE and KN with high activity, and identified them as low- and high-contribution modules, respectively. We hypothesized the substitution of low-contribution modules in peptides with high contributions would boost their XOD inhibitory activity. In the XOD inhibitory peptide GPAGPR, substitution of GP with both KE and KN led to enhanced affinity between the peptides and XOD. They also increased XOD inhibitory activity (26.4% and 10.3%) and decreased cellular uric acid concentrations (28.0% and 10.4%). RNA sequencing indicated that these improvements were attributable to the inhibition of uric acid biosynthesis. In addition, module substitution increased the angiotensin-converting enzyme inhibitory activity of GILRP and GAAGGAF by 84.8% and 76.5%. This study revealed that module substitution is a feasible strategy to boost peptide activity, and provided information for the optimization of hydrolysate preparation conditions. |
| Funding Organization | National Natural Science Foundation of China ; China Postdoctoral Science Foundation ; National Key Research and Development Program of China ; Public Welfare Project of Ningbo City ; Chinese Academy of Sciences ; Wong Magna Fund of Ningbo University |
| Indexed By | SCI |
| Language | 英语 |
| WOS Keyword | IN-VITRO ; PROFILE |
| WOS Research Area | Chemistry ; Food Science & Technology ; Nutrition & Dietetics |
| WOS ID | WOS:001164584800001 |
| Citation statistics | |
| Document Type | 期刊论文 |
| Identifier | http://ir.yic.ac.cn/handle/133337/34886 |
| Collection | 中国科学院烟台海岸带研究所 |
| Corresponding Author | Li, Wenjun; Lu, Chenyang |
| Affiliation | 1.Ningbo Univ, State Key Lab Managing Biot & Chem Threats Qual &, Ningbo 315211, Peoples R China 2.Ningbo Univ, Sch Marine Sci, Ningbo 315211, Peoples R China 3.Zhejiang Gongshang Univ, Sch Food Sci & Biotechnol, Food Safety Key Lab Zhejiang Prov, Hangzhou 310018, Peoples R China 4.Chinese Acad Sci, Yantai Inst Coastal Zone Res, Yantai 264003, Peoples R China 5.Beijing Technol & Business Univ, Sch Food & Hlth, Beijing 100048, Peoples R China |
| Recommended Citation GB/T 7714 | Meng, Pengfei,Wang, Yanxin,Huang, Yumeng,et al. A strategy to boost xanthine oxidase and angiotensin converting enzyme inhibitory activities of peptides via molecular docking and module substitution[J]. FOOD CHEMISTRY,2024,442:9. |
| APA | Meng, Pengfei.,Wang, Yanxin.,Huang, Yumeng.,Liu, Tong.,Ma, Mingxia.,...&Lu, Chenyang.(2024).A strategy to boost xanthine oxidase and angiotensin converting enzyme inhibitory activities of peptides via molecular docking and module substitution.FOOD CHEMISTRY,442,9. |
| MLA | Meng, Pengfei,et al."A strategy to boost xanthine oxidase and angiotensin converting enzyme inhibitory activities of peptides via molecular docking and module substitution".FOOD CHEMISTRY 442(2024):9. |
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