Screening of Oral Potential Angiotensin-Converting Enzyme Inhibitory Peptides from Zizyphus jujuba Proteins Based on Gastrointestinal Digestion In Vivo
文献类型： 外文期刊
作者： Gao, Xinchang 1 ; Zhang, Chaoying 3 ; Wang, Ning 1 ; Lin, Jin-Ming 2 ; Dang, Yali 4 ; Zhao, Yufen 1 ;
作者机构： 1.Ningbo Univ, Inst Drug Discovery Technol, Ningbo 315211, Peoples R China
2.Tsinghua Univ, Dept Chem, Beijing 100084, Peoples R China
3.Chinese Acad Fishery Sci, Beijing 100141, Peoples R China
4.Ningbo Univ, Coll Food & Pharmaceut Sci, Ningbo 315211, Peoples R China
关键词： Zizyphus jujuba; ACE-inhibitory peptides; screening; digestion stability; 3D-QSAR model
期刊名称：INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES （ 影响因子：5.6； 五年影响因子：6.2 ）
ISSN： 1661-6596
年卷期： 2023 年 24 卷 21 期
页码：
收录情况： SCI
摘要： Plant proteins are a good source of active peptides, which can exert physiological effects on the body. Predicting the possible activity of plant proteins and obtaining active peptides with oral potential are challenging. In this study, the potential activity of peptides from Zizyphus jujuba proteins after in silico simulated gastrointestinal digestion was predicted using the BIOPEP-UWM (TM) database. The ACE-inhibitory activity needs to be further investigated. The actual peptides in mouse intestines after the oral administration of Zizyphus jujuba protein were collected and analyzed, 113 Zizyphus jujuba peptides were identified, and 3D-QSAR models of the ACE-inhibitory activity were created and validated using a training set (34 peptides) and a test set (12 peptides). Three peptides, RLPHV, TVKPGL and KALVAP, were screened using the 3D-QSAR model and were found to bind to the active sites of the ACE enzyme, and their IC50 values were determined. Their values were 6.01, 3.81, and 17.06 mu M, respectively. The in vitro digestion stabilities of the RLPHV, TVKPGL, and KALVAP peptides were 82%, 90%, and 78%. This article provides an integrated method for studying bioactive peptides derived from plant proteins.
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