Screening,<i>in Vitro</i> Activity and Molecular Mechanism of ACE Inhibitory Tirpeptides from <i>Larimichthys crocea</i> Protein

JI Huizhuo; CHEN Jiayu; LI Xin; MA Ruping; YU Zhipeng; ZHAO Wenzhu; LI Jianrong

doi:10.13386/j.issn1002-0306.2020060287

Volume 42 Issue 6

Mar. 2021

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Science and Technology of Food Industry > 2021 > 42(6): 125-129,143. > DOI: 10.13386/j.issn1002-0306.2020060287

JI Huizhuo, CHEN Jiayu, LI Xin, MA Ruping, YU Zhipeng, ZHAO Wenzhu, LI Jianrong. Screening,in Vitro Activity and Molecular Mechanism of ACE Inhibitory Tirpeptides from Larimichthys crocea Protein[J]. Science and Technology of Food Industry, 2021, 42(6): 125-129,143. DOI: 10.13386/j.issn1002-0306.2020060287

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Screening,in Vitro Activity and Molecular Mechanism of ACE Inhibitory Tirpeptides from Larimichthys crocea Protein

College of Food Science and Engineering, Bohai University, National & Local Joint Engineering Research Center of Storage, Processing and Safety Control Technology for Fresh Agricultural and Aquatic Products, Jinzhou 121013, China

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Received Date: June 23, 2020
Available Online: March 15, 2021

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Abstract

Abstract

The moesin of Larimichthys crocea was in silico digested by gastrointestinal proteases(pepsin and trypsin) of online databases ExPASy PeptideCutter, and the potential bioactive, solubility, absorption, distribution, metabolism, excretion and toxicity of screened tripeptides were predicted and validated in this study. Furthermore, the interaction mechanism of tripeptides and angiotensin-I converting enzyme(ACE) was elucidated by molecular docking and the CDOCKER-Energy was calculated. The ACE inhibitory activity of potential tripeptides in vitro was determined by RP-HPLC and the interaction site of tripeptides in ACE was also clarified. In this paper, four ACE inhibitory tripeptides CMK, GWR, WAK and WQK were successfully identified from the moesin of Larimichthys crocea, with IC₅₀ values of 0.19, 2.40, 0.40, and 1.10 mmol/L respectively. The results of molecular interaction between tripeptides and ACE suggested that tripeptides CMK, GWR, WAK and WQK interacted with key residues Ala354, Glu384 in S₁ pocket of ACE and key residue His353 in S₂ pocket of ACE. Meanwhile, hydrogen bond may attribute to the molecular interaction of tripeptide and the active pocket of ACE. The current study indicated that tripeptides from Larimichthys crocea moesin could be used to develop functional food to prevent hypertension in the future.
- Larimichthys crocea moesin,
- virtual screening,
- ACE inhibitory peptides,
- molecular mechanism

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