Identification and action mechanism of low-molecular-weight peptides derived from Atlantic salmon (Salmo salar L.) skin inhibiting angiotensin I–converting enzyme

Liu, Wenying; Feng, Xingjun; Cheng, Qingli; Zhao, Xiaohan; Li, Guoming; Gu, Rong

doi:10.1016/j.lwt.2021.111911

Cited by 18 publications

(9 citation statements)

References 51 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The MWs of the 10 ACEi peptides (TP1-TP10) were determined as 411. 35 5), which agreed well with their theoretical MWs (Table 1).…”

Section: Peptide Sequence and Mw Determinationsupporting

confidence: 85%

“…Those fish byproducts result in burdensome disposal problems, and unreasonable treatment will give rise to serious environmental pollution (24-26). For making full use of these fish byproducts, many ACEi peptides were prepared from different processing byproducts, such as tuna bone (27, 28), skate (Okamejei kenojei) skin (29), mackerel skin (30), Nile tilapia skin (31) and skeleton (32), sea cucumber (Stichopus japonicus) gonad (33), smooth-hound (Mustelus mustelus) viscera (34), Atlantic salmon skin (35), Alaska pollack skins (36), and rainbow trout (Oncorhynchus mykiss) viscera (37). Those sea-food derived ACEi peptides exhibit high potential application value in terms of diet and clinical therapeutics on anti-hypertension (5,38,39).…”

mentioning

confidence: 99%

See 1 more Smart Citation

Novel angiotensin-converting enzyme inhibitory peptides from tuna byproducts—milts: Preparation, characterization, molecular docking study, and antioxidant function on H2O2-damaged human umbilical vein endothelial cells

et al. 2022

View full text Add to dashboard Cite

To prepare peptides with high angiotensin-converting enzyme (ACE) inhibitory (ACEi) activity, Alcalase was screened from five proteases and employed to prepare protein hydrolysate (TMH) of skipjack tuna (Katsuwonus pelamis) milts. Subsequently, 10 novel ACEi peptides were isolated from the high-ACEi activity TMH and identified as Tyr-Asp-Asp (YDD), Thr-Arg-Glu (TRE), Arg-Asp-Tyr (RDY), Thr-Glu-Arg-Met (TERM), Asp-Arg-Arg-Tyr-Gly (DRRYG), Ile-Cys-Tyr (ICY), Leu-Ser-Phe-Arg (LSFR), Gly-Val-Arg-Phe (GVRF), Lys-Leu-Tyr-Ala-Leu-Phe (KLYALF), and Ile-Tyr-Ser-Pro (IYSP) with molecular weights of 411.35, 404.41, 452.45, 535.60, 665.69, 397.48, 521.61, 477.55, 753.91, and 478.53 Da, respectively. Among them, the IC50 values of ICY, LSFR, and IYSP on ACE were 0.48, 0.59, and 0.76 mg/mL, respectively. The significant ACEi activity of ICY, LSFR, and IYSP with affinities of −7.0, −8.5, and −8.3 kcal/mol mainly attributed to effectively combining with the ACEi active sites through hydrogen bonding, electrostatic force, and hydrophobic interaction. Moreover, ICY, LSFR, and IYSP could positively influence the production of nitric oxide (NO) and endothelin-1 (ET-1) secretion in human umbilical vein endothelial cells (HUVECs) and weaken the adverse impact of norepinephrine (NE) on the production of NO and ET-1. In addition, ICY, LSFR, and IYSP could provide significant protection to HUVECs against H2O2 damage by increasing antioxidase levels to decrease the contents of reactive oxide species and malondialdehyde. Therefore, the ACEi peptides of ICY, LSFR, and IYSP are beneficial functional molecules for healthy foods against hypertension and cardiovascular diseases.

show abstract

“…The MWs of the 10 ACEi peptides (TP1-TP10) were determined as 411. 35 5), which agreed well with their theoretical MWs (Table 1).…”

Section: Peptide Sequence and Mw Determinationsupporting

confidence: 85%

mentioning

confidence: 99%

Novel angiotensin-converting enzyme inhibitory peptides from tuna byproducts—milts: Preparation, characterization, molecular docking study, and antioxidant function on H2O2-damaged human umbilical vein endothelial cells

et al. 2022

View full text Add to dashboard Cite

show abstract

“…Furthermore, according to Ishak and Sarbon (2018), the molecular weight of bioactive peptides from fish waste with ACEi activity and antioxidant properties were reported to be <1.2 kDa, <1 kDa and an average of 640-25,719 Da, respectively. The highest fish gelatin ACEi peptide activity was found in the study of Byun and Kim (2001), with GPL peptides (glycine, proline, leucine), while the lowest ACEi activity was in GPR peptides (glycine, proline, arginine) with 3201 M activity and a molecular weight of 328 (Liu et al 2021). The molecular weight, composition and position of the amino acids formed determine the activity of ACEi (Sitanggang et al, 2021).…”

Section: Bioactive Characteristics Of Fish Gelatin Peptides As Aceimentioning

confidence: 92%

“…The Papain enzyme is more commonly combined with other enzymes. In this regard, there are three studies involving the use of Papain, applied at 60 o C and pH 7(Gu et al, 2011;Ngo et al, 2011;Liu et al, 2021) Halim et al (2016). mentioned that hydrolysis conditions using Alcalase on various fish substrates were found at pH 7.5-10 and 45-60 o C. Neutrase worked properly at…”

mentioning

confidence: 99%

Enzymatic hydrolysis of marine fish gelatin for producing ACE inhibitor peptides: meta-analysis

Ahmad¹,

Sukarno²,

Budijanto³

et al. 2022

AUDJG - Food Technology

View full text Add to dashboard Cite

Bioactive peptides showing Angiotensin-I-Converting Enzyme inhibitory (ACEi) activity can control blood pressure. They can be produced from various protein sources, including fish gelatin. This article provides a systematic review and meta-analysis on gelatin extraction, conditions of enzymatic hydrolysis, characteristics of ACEi peptides, and effect of hydrolysis procedure on ACEi peptides. Fish gelatin preparation uses various solutions such as acids, bases and distilled water. Enzymatic hydrolysis is carried out with an E/S ratio of 0.2 – 7% and temperature of 28.9 oC (using bromelain) and 60.6 oC (using Alcalase). Level of pH in hydrolysis also varied greatly, from 2 (using Pepsin) to 10 (using Purafect enzyme). The molecular weight of fish gelatin ACEi peptides ranged from 186-829 Da and the sequence of peptides was dominated by hydrophobic and aliphatic amino acids. Based on a meta-analysis, hydrolysis using enzyme combination resulted in more satisfying product than a single enzyme, represented with a combined effect size value of 0.593.

show abstract

“…Therefore, we presume that the R V in the peptide sequence has been found to enhance the ACE inhibitory activity of the peptide (Liu et al, 2021). The dipeptides VR and IR have been reported to exhibit inhibitory activity against ACE (Ko et al, 2017;Liu et al, 2021). Molecular docking studies have revealed that the three dipeptides (VR, IR, and RI) can interact with multiple amino acid residues at the ACE active site by forming hydrogen bonds.…”

Section: Ace Inhibitory Activity Of Dipeptidesmentioning

confidence: 99%

Oyster‐derived dipeptides RI, IR, and VR promote testosterone synthesis by reducing oxidative stress in TM3 cells

Yan,

Li,

Wei

et al. 2023

Food Science & Nutrition

View full text Add to dashboard Cite

Short peptides have gained widespread utilization as functional constituents in the development of functional foods due to their remarkable biological activity. Previous investigations have established the positive influence of oysters on testosterone biosynthesis, although the underlying mechanism remains elusive. This study aims to assess the impact of three dipeptides derived from oysters on the oxidative stress state of TM3 cells induced by AAPH while concurrently examining alterations in cellular testosterone biosynthesis capacity. The investigation encompasses an analysis of reactive oxygen species (ROS) content, antioxidant enzyme activity, apoptotic status, and expression levels of crucial enzymes involved in the testosterone synthesis pathway within TM3 cells, thus evaluating the physiological activity of the three dipeptides. Additionally, molecular docking was employed to investigate the inhibitory activity of the three dipeptides against ACE. The outcomes of this study imply that the oxidative stress state of cells impedes the synthesis of testosterone by inhibiting the expression of essential proteins in the testosterone synthesis pathway. These three dipeptides derived from oysters ameliorate cellular oxidative stress by directly scavenging excess ROS or reducing ROS production rather than enhancing cellular antioxidant capacity through modulation of antioxidant enzyme activity. These findings introduce a novel avenue for developing and utilizing antioxidant peptides derived from food sources.

show abstract

Identification and action mechanism of low-molecular-weight peptides derived from Atlantic salmon (Salmo salar L.) skin inhibiting angiotensin I–converting enzyme

Cited by 18 publications

References 51 publications

Novel angiotensin-converting enzyme inhibitory peptides from tuna byproducts—milts: Preparation, characterization, molecular docking study, and antioxidant function on H2O2-damaged human umbilical vein endothelial cells

Novel angiotensin-converting enzyme inhibitory peptides from tuna byproducts—milts: Preparation, characterization, molecular docking study, and antioxidant function on H2O2-damaged human umbilical vein endothelial cells

Enzymatic hydrolysis of marine fish gelatin for producing ACE inhibitor peptides: meta-analysis

Oyster‐derived dipeptides RI, IR, and VR promote testosterone synthesis by reducing oxidative stress in TM3 cells

Contact Info

Product

Resources

About