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A strategy to boost xanthine oxidase and angiotensin converting enzyme inhibitory activities of peptides via molecular docking and module substitution

文献类型：期刊论文

作者Meng, Pengfei2,3; Wang, Yanxin2,3; Huang, Yumeng2,3; Liu, Tong2,3; Ma, Mingxia2,3; Han, Jiaojiao2,3; Su, Xiurong2,3; Li, Wenjun5; Wang, Yanbo1,4; Lu, Chenyang1,2,3
刊名FOOD CHEMISTRY
出版日期2024-06-01
卷号442页码:9
关键词Peptide Activity boosting strategy Molecular docking Module substitution Xanthine oxidase inhibitory Angiotensin-converting enzyme inhibitory
ISSN号0308-8146
DOI10.1016/j.foodchem.2024.138401
通讯作者Li, Wenjun(wjli@yic.ac.cn) ; Lu, Chenyang(luchenyang@nbu.edu.cn)
英文摘要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.
WOS关键词IN-VITRO ; PROFILE
WOS研究方向Chemistry ; Food Science & Technology ; Nutrition & Dietetics
语种英语
WOS记录号WOS:001164584800001
资助机构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
源URL[http://ir.yic.ac.cn/handle/133337/36300]  
专题海岸带生物学与生物资源利用重点实验室
烟台海岸带研究所_海岸带生物学与生物资源利用所重点实验室
通讯作者Li, Wenjun; Lu, Chenyang
作者单位1.Zhejiang Gongshang Univ, Sch Food Sci & Biotechnol, Food Safety Key Lab Zhejiang Prov, Hangzhou 310018, Peoples R China
2.Ningbo Univ, Sch Marine Sci, Ningbo 315211, Peoples R China
3.Ningbo Univ, State Key Lab Managing Biot & Chem Threats Qual &, Ningbo 315211, Peoples R China
4.Beijing Technol & Business Univ, Sch Food & Hlth, Beijing 100048, Peoples R China
5.Chinese Acad Sci, Yantai Inst Coastal Zone Res, Yantai 264003, Peoples R China
推荐引用方式
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.

入库方式： OAI收割

来源：烟台海岸带研究所

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