Screening and mechanisms of novel angiotensin-I-converting enzyme inhibitory peptides from rabbit meat proteins: A combined in silico and in vitro study

•Seven novel ACE inhibitory peptides were screened from rabbit meat proteins.•Two novel peptides (EACF and CDF) exhibited strong ACE inhibitory activities.•EACF was a competitive ACE inhibitor with IC50 value of 41.06 ± 0.82 µM.•CDF was a non-competitive ACE inhibitor with IC50 value of 192.17 ± 2.4...

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Bibliographic Details
Published in:Food chemistry 2022-02, Vol.370, p.131070-131070, Article 131070
Main Authors: Chen, Junbo, Yu, Xiaodong, Chen, Qianzi, Wu, Qiyun, He, Qiyi
Format: Article
Language:English
Subjects:
Angiotensin-I-converting enzyme
In silico
Inhibitory mechanism
Peptides
Rabbit meat proteins
Screening
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Summary:•Seven novel ACE inhibitory peptides were screened from rabbit meat proteins.•Two novel peptides (EACF and CDF) exhibited strong ACE inhibitory activities.•EACF was a competitive ACE inhibitor with IC50 value of 41.06 ± 0.82 µM.•CDF was a non-competitive ACE inhibitor with IC50 value of 192.17 ± 2.46 µM.•Virtual screening is a promising method for the discovery of bioactive peptides. Bioactive peptides derived from food proteins have various physiological roles and have attracted increasing attention in recent years. In this study, two novel ACE inhibitory peptides (EACF and CDF), screened from rabbit meat proteins using in silico methods, exhibited strong inhibitory effects in vitro. EACF and CDF were competitive and non-competitive inhibitors with half-maximal inhibitory concentrations of 41.06 ± 0.82 µM and 192.17 ± 2.46 µM, respectively. Molecular docking experiments revealed that EACF established eight H-bond interactions in the S1 and S2 pockets, and a metal-acceptor interaction with Zn 701. CDF shared four H-bond interactions in the S1 pocket of ACE. The results suggested that rabbit meat proteins could be a suitable material for the preparation of ACE inhibitory peptides, and that virtual screening is an effective, accurate and promising method for the discovery of novel active peptides.
ISSN:0308-8146
1873-7072
DOI:10.1016/j.foodchem.2021.131070