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

doi:10.1016/j.foodchem.2024.138401

	A strategy to boost xanthine oxidase and angiotensin converting enzyme inhibitory activities of peptides via molecular docking and module substitution
	Meng, Pengfei 1,2; Wang, Yanxin 1,2; Huang, Yumeng 1,2; Liu, Tong 1,2; Ma, Mingxia 1,2; Han, Jiaojiao 1,2; Su, Xiurong 1,2; Li, Wenjun4 ; Wang, Yanbo 3,5; Lu, Chenyang 1,2,3
发表期刊	FOOD CHEMISTRY
ISSN	0308-8146
	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
DOI	10.1016/j.foodchem.2024.138401
通讯作者	Li, Wenjun([email protected]) ; Lu, Chenyang([email protected])
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.
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
收录类别	SCI
语种	英语
关键词[WOS]	IN-VITRO ; PROFILE
研究领域[WOS]	Chemistry ; Food Science & Technology ; Nutrition & Dietetics
WOS记录号	WOS:001164584800001
引用统计	被引频次：4[WOS] [WOS记录] [WOS相关记录]
文献类型	期刊论文
条目标识符	http://ir.yic.ac.cn/handle/133337/36301
专题	海岸带生物学与生物资源利用重点实验室海岸带生物学与生物资源利用重点实验室_海岸带生物学与生物资源保护实验室
通讯作者	Li, Wenjun; Lu, Chenyang
作者单位	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
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.