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Open AccessArticle

Identification and Molecular Docking Study of a Novel Angiotensin-I Converting Enzyme Inhibitory Peptide Derived from Enzymatic Hydrolysates of Cyclina sinensis

1
Zhejiang Provincial Engineering Technology Research Center of Marine Biomedical Products, School of Food and Pharmacy, Zhejiang Ocean University, Zhoushan 316022, China
2
Laboratory of Aquatic Products Processing and Quality Safety, Marine Fisheries Research Institute of Zhejiang, Zhoushan 316021, China
*
Authors to whom correspondence should be addressed.
Mar. Drugs 2018, 16(11), 411; https://doi.org/10.3390/md16110411
Received: 10 October 2018 / Revised: 24 October 2018 / Accepted: 25 October 2018 / Published: 27 October 2018
(This article belongs to the Special Issue The Pharmacological Potential of Marine-Derived Peptides and Proteins)
Marine-derived angiotensin-I converting enzyme (ACE) inhibitory peptides have shown potent ACE inhibitory activity with no side effects. In this study, we reported the discovery of a novel ACE-inhibitory peptide derived from trypsin hydrolysates of Cyclina sinensis (CSH). CSH was separated into four different molecular weight (MW) fractions by ultrafiltration. Fraction CSH-I showed the strongest ACE inhibitory activity. A peptide was purified by fast protein liquid chromatography (FPLC) and reversed-phase high-performance liquid chromatography (RP-HPLC) and its sequence was determined to be Trp-Pro-Met-Gly-Phe (WPMGF, 636.75 Da). The Lineweaver-Burk plot showed that WPMGF was a competitive inhibitor of ACE. WPMGF showed a significant degree of stability at varying temperatures, pH, and simulated gastrointestinal environment conditions. We investigated the interaction between this pentapeptide and ACE by means of a flexible molecular docking tool. The results revealed that effective interaction between WPMGF and ACE occurred mainly through hydrogen bonding, hydrophobic interactions, and coordination bonds between WPMGF and Zn(II). In conclusion, our study indicates that a purified extract derived from Cyclina sinensis or the WPMGF peptide could potentially be incorporated in antihypertensive functional foods or dietary supplements. View Full-Text
Keywords: cyclina sinensis; hypertension; ACE inhibitory peptides; inhibitory pattern; molecular docking cyclina sinensis; hypertension; ACE inhibitory peptides; inhibitory pattern; molecular docking
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Yu, F.; Zhang, Z.; Luo, L.; Zhu, J.; Huang, F.; Yang, Z.; Tang, Y.; Ding, G. Identification and Molecular Docking Study of a Novel Angiotensin-I Converting Enzyme Inhibitory Peptide Derived from Enzymatic Hydrolysates of Cyclina sinensis. Mar. Drugs 2018, 16, 411.

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