Abstract
In this study, the sea food Sipunculus nudus L. was hydrolyzed by trypsin, and peptides were isolated and purified from the hydrolysates. As a result, two novel nonapeptides were identified by LC–MS–MS with amino sequences of GFAGDDAPR and GLGGLSPEK. The ACEI activity were determined and the IC50 values of the peptides for ACE inhibition activity were 0.76 mmol/L and 0.91 mmol/L, respectively. The results showed that both peptides had ACE inhibitory activity. Analysis of the Lineweaver–Burk plot demonstrated that these peptides served as non-competitive ACE inhibitors. Molecular docking study showed that these peptides could interact with the active site of ACE mainly through hydrogen bonding and electrostatic force. The amino acid residue that plays a key role in ACE inhibitory activity was its C-terminal Arg. It is therefore suggested that S. nudus may be a useful raw material for the production of antihypertensive peptides which can offer therapeutic and commercial benefits as an ingredient in functional foods.
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Acknowledgements
We very thank our teachers Yingnian Lu and Yi Qi for their guidance on this work. Finally, I am very grateful to my mentor, Professor Hui Luo, for his great support to this research.
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This research was funded by the public service platform of south China Sea for R&D marine biomedicine resources (2017C8A), Zhanjiang Science and Technology Development Special Fund Project 2020A04005.
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XT and YQ performed experiments, HL and QL collected and analyzed data, XT and HL wrote the manuscript. HL and YL designed the experiments and supervised the work.
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Qi, Y., Tang, X., Liu, H. et al. Identification of Novel Nonapeptides from Sipunculus nudus L. and Comparing Its ACEI Activities Mechanism by Molecular Docking. Int J Pept Res Ther 28, 20 (2022). https://doi.org/10.1007/s10989-021-10328-3
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DOI: https://doi.org/10.1007/s10989-021-10328-3