Seventeen novel angiotensin converting enzyme (ACE) inhibitory peptides from the protein hydrolysate of Mytilus edulis: isolation, identification, molecular docking study, and protective function on HUVECs. Issue 14 (30th June 2022)
- Record Type:
- Journal Article
- Title:
- Seventeen novel angiotensin converting enzyme (ACE) inhibitory peptides from the protein hydrolysate of Mytilus edulis: isolation, identification, molecular docking study, and protective function on HUVECs. Issue 14 (30th June 2022)
- Main Title:
- Seventeen novel angiotensin converting enzyme (ACE) inhibitory peptides from the protein hydrolysate of Mytilus edulis: isolation, identification, molecular docking study, and protective function on HUVECs
- Authors:
- Suo, Shi-Kun
Zhao, Yu-Qin
Wang, Yu-Mei
Pan, Xiao-Yang
Chi, Chang-Feng
Wang, Bin - Abstract:
- Abstract : 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. Abstract : 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 IC50 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 H2 O2 damage by increasing superoxide dismutase (SOD), glutathione peroxidase (GSH-Px) and NO levels to decrease the contents of reactive oxygen species (ROS) and malondialdehyde.Abstract : 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. Abstract : 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 IC50 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 H2 O2 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. … (more)
- Is Part Of:
- Food & function. Volume 13:Issue 14(2022)
- Journal:
- Food & function
- Issue:
- Volume 13:Issue 14(2022)
- Issue Display:
- Volume 13, Issue 14 (2022)
- Year:
- 2022
- Volume:
- 13
- Issue:
- 14
- Issue Sort Value:
- 2022-0013-0014-0000
- Page Start:
- 7831
- Page End:
- 7846
- Publication Date:
- 2022-06-30
- Subjects:
- Food -- Analysis -- Periodicals
Food -- Composition -- Periodicals
Nutrition -- Periodicals
664.07 - Journal URLs:
- http://pubs.rsc.org/en/Journals/JournalIssues/FO ↗
http://pubs.rsc.org/en/journals/journal/fo ↗
http://www.rsc.org/ ↗ - DOI:
- 10.1039/d2fo00275b ↗
- Languages:
- English
- ISSNs:
- 2042-6496
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3977.038457
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 22967.xml