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Seventeen novel angiotensin converting enzyme (ACE) inhibitory peptides from the protein hydrolysate of : isolation, identification, molecular docking study, and protective function on HUVECs
In the study, seventeen angiotensin converting enzyme (ACE) inhibitory peptides were isolated from the protein hydrolysate of blue mussel (
Mytilus edulis
) and identified as MFR, MFV, FV, KP, QP, QVK, IK, YKV, IRK, MLKV, NFRPQ, YEGDP, WF, GPE, SWISS, SVEWK, and FKWH, respectively. Among them, IK, YEGDP, WF, and SWISS showed the strongest ACE inhibitory activity with IC
50
values of 0.77 ± 0.020, 0.19 ± 0.010, 0.40 ± 0.015, and 0.32 ± 0.017 mg mL
−1
, respectively. Molecular docking study indicated that IK, YEGDP, WF, and SWISS exhibited better inhibitory activity attributed to its effective interaction with the active site of ACE by hydrogen bonding, electrostatic force and hydrophobic interaction. Furthermore, IK, YEGDP and WF perform an important protective function on human umbilical vein endothelial cells (HUVECs) by increasing nitric oxide (NO) content, decreasing endothelin-1 (ET-1) secretion, and antagonizing the adverse impact of norepinephrine on the secretion of NO and ET-1. In addition, YEGDP and WF could provide protection to HUVECs against H
2
O
2
damage by increasing superoxide dismutase (SOD), glutathione peroxidase (GSH-Px) and NO levels to decrease the contents of reactive oxygen species (ROS) and malondialdehyde. Therefore, seventeen ACE inhibitory peptides, especially YEGDP and WF, might be used as natural ingredients for the development of products with antihypertensive functions.
This study suggested that bioactive peptides from blue mussel could serve as a therapeutic alternative in the treatment of hypertension because of their ACE inhibitory activity and protective effects on oxidative damaged HUVECs.
Sprache
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Identifikatoren
ISSN: 2042-6496
eISSN: 2042-650X
DOI: 10.1039/d2fo00275b
Titel-ID: cdi_rsc_primary_d2fo00275b
Format
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