Identification of a novel ACE-inhibitory peptide from casein and evaluation of the inhibitory mechanisms

Tu, Maolin; Wang, Cong; Chen, Cheng; Zhang, Ruyi; Liu, Hanxiong; Lu, Weihong; Jiang, Lianzhou; Du, Ming

doi:10.1016/j.foodchem.2018.02.107

Cited by 167 publications

(105 citation statements)

References 34 publications

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“…Moreover, the content of hydrophobic amino acid residues was 50.00% ( Table 2). These structural features all significantly contributed to its relatively high ACE-inhibitory activity (72.24 µM), which was higher (p < 0.05) than that of the peptides identified from horrens protein (GSAGY, IC 50 : 706 µM) and casein (NMAINPSKENLCSTFCK, IC 50 : 129.07 µM) [38,40]. Furthermore, the Arg at the N-terminal of RWDISQPY contributed substantially to the high activity [41].…”

Section: Inhibition Kinetics Of Synthetic Peptidesmentioning

confidence: 95%

Efficacy of a Novel ACE-Inhibitory Peptide from Sargassum maclurei in Hypertension and Reduction of Intracellular Endothelin-1

2020

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Sargassum maclurei is a potential protein resource because of its high protein content and relatively balanced amino acid composition. To promote its usage in food, medical, or other industries, S. maclurei protein was hydrolyzed by pepsin and papain to obtain bioactive peptides. The S. maclurei protein hydrolysates (SMPHs) were purified using gel chromatography and reversed-phase high performance liquid chromatography (RP-HPLC), and 12 major fractions were obtained. The fraction D11 with the highest angiotensin I-converting enzyme (ACE) inhibition (61.59%, at 1 mg/mL) was subjected to liquid chromatography-mass spectrometry (LC-MS/MS) analysis, and about 17 peptides were identified, of which the RWDISQPY (1063.5 Da) was chosen to be synthesized based on in silico analysis. The RWDISQPY demonstrated high ACE inhibition ability (IC 50 : 72.24 µM) with competitive inhibition mode, and could effectively (p < 0.05) lower the systolic blood pressure and diastolic pressure of spontaneously hypertensive rats at the concentration of 150 mg/kg body weight. The results of the molecular docking simulation demonstrated that RWDISQPY could bind with the active sites S1 and S2 of ACE via short hydrogen bonds. Moreover, RWDISQPY showed acceptable endothelin-1 suppressing capacity (26.21% at 1.5 mg/mL). These results indicate that S. maclurei could be developed into functional foods such as antihypertensive products.

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Section: Inhibition Kinetics Of Synthetic Peptidesmentioning

confidence: 95%

Efficacy of a Novel ACE-Inhibitory Peptide from Sargassum maclurei in Hypertension and Reduction of Intracellular Endothelin-1

2020

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“…In recent years, it has been demonstrated that ACE appears to prefer substrates or competitive inhibitors that contain hydrophobic amino acid residues, particularly Val, Leu, and/or aromatic residues (Trp, Tyr, or Phe) in the C-terminal tripeptide [25,29]. Moreover, accumulating studies suggest that the positive charge of Arg (guanidine group) at N-terminus contributes substantially to the inhibitory activity against ACE [32,33]. Regarding the antioxidant activity of peptides, it was more related to size, amino acid constituents and sequence, structure, and hydrophobicity [27].…”

Section: Characterization Of Pooled Peptide Fraction By Mass Spectrommentioning

confidence: 99%

Isolation of Novel ACE-Inhibitory and Antioxidant Peptides from Quinoa Bran Albumin Assisted with an In Silico Approach: Characterization, In Vivo Antihypertension, and Molecular Docking

et al. 2019

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Albumin is the major fraction of quinoa protein that is characterized as having high nutritional value. However, until now, scant information is available on the bioactivity of quinoa albumin or its hydrolysates. To promote its usage, we extracted albumin in this study from quinoa bran assisted with cellulase and hemicellulose, and hydrolyzed it by alcalase and trypsin to produce bioactive peptides. The hydrolysates (QBAH) were purified by gel filtration and reversed-phase high-performance liquid chromatography (RP-HPLC), followed by identification using liquid chromatography-mass spectrometry (LC-MS/MS). Furthermore, based on in silico analysis, one angiotensin-I converting enzyme (ACE)-inhibitory and antioxidant peptide, RGQVIYVL (946.6 Da), and two antioxidant peptides, ASPKPSSA (743.8 Da), and QFLLAGR (803.5 Da), from QBAH were synthesized. RGQVIYVL showed a high ACE-inhibitory activity (IC 50 = 38.16 µM) with competitive mode of inhibition, and showed significant antihypertensive effect in spontaneously hypertensive rats at a concentration of 100-150 mg/kg body weight (bw). Molecular docking simulation showed that it could interact with the active ACE site via hydrogen bonds with high binding power. Moreover, RGQVIYVL, ASPKPSSA, and QFLLAGR all demonstrated high ·OH scavenging activity (IC 50 = 61.69-117.46 µM), ABTS + scavenging activity (58.29-74.28%) and Fe 2+ chelating ability (32.54-82.48% at 0.5 mg/mL). They could also retain activity after gastrointestinal enzyme digestion. These results indicate that quinoa albumin is a potential source of bioactive peptides possessing antioxidant and ACE-inhibitory activities.

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“…The amino acid composition analysis results of GP, GPH-P, and GPH-T are shown in Leu, Gly residues, and C-terminal peptides with Arg, Tyr, Phe, and Pro residues have significant antihypertensive effects (Block et al, 2017;Girgih, He, & Aluko, 2014;Tu, Wang, et al, 2018). According to the proportion of these kinds of amino acids in GPH-P and GPH-T, GP hydrolyzed with appropriate enzymes could…”

Section: Amino Acids Compositional Analysis Of Gp Gph-p and Gph-tmentioning

confidence: 99%

Antioxidant and antihypertensive effects of garlic protein and its hydrolysates and the related mechanism

Gao

Xue

et al. 2019

J Food Biochem

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Garlic protein (GP) was enzymatically hydrolyzed using pepsin and trypsin followed by the evaluation of antioxidant and angiotensin-converting enzyme (ACE) inhibitory activities of GP and its hydrolysates. The antihypertensive effects of GP and its hydrolysates were determined in vivo. The results showed that GP and its hydrolysates namely GPH-P (pepsin) and GPH-T (trypsin) possessed appreciable antioxidant and ACE inhibitory activities. The ACE inhibitory activity of GP, GPH-T, and GPH-P was in consistent with their antioxidant activities. GP and its hydrolysates offered significant protective effects against H 2 O 2 -induced oxidative damage (p < .05). In addition, the administration of GP, GPH-T, and GPH-P reduced the blood pressure in hypertensive rats. The mechanism might be to reduce blood pressure by inhibiting the activity of ACE, reducing the formation of ACEII, and protecting the activity of bradykinin. This study suggested that GP might be utilized as a promising functional food as antioxidant and antihypertensive agents. Practical applicationsGarlic (Allium sativum L.) is one of the oldest cultivated plants that belongs to the Liliaceae family and it has been used in cooking and medicinal applications. Large quantities of garlic residuals were produced with the development of the garlic essential oil industry. These residuals are highly rich in proteins and they can be used for the preparation of protein hydrolysates. Generally, hydrolysates are considered as a promising food supplement due to the enrichment of amino acids present in it.In this study, garlic proteins (GPs) and its hydrolysates retain effective antioxidant effects. They were found to reduce the blood pressure and prevent oxidative stress induced by H 2 O 2 . The information from this study could be used to develop a new nutritional supplement from GP and its hydrolysates to treat hypertension as well as prevent oxidative damage. K E Y W O R D SACE inhibitory activity, antioxidant, L02 cells, oxidative damage

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Identification of a novel ACE-inhibitory peptide from casein and evaluation of the inhibitory mechanisms

Cited by 167 publications

References 34 publications

Efficacy of a Novel ACE-Inhibitory Peptide from Sargassum maclurei in Hypertension and Reduction of Intracellular Endothelin-1

Efficacy of a Novel ACE-Inhibitory Peptide from Sargassum maclurei in Hypertension and Reduction of Intracellular Endothelin-1

Isolation of Novel ACE-Inhibitory and Antioxidant Peptides from Quinoa Bran Albumin Assisted with an In Silico Approach: Characterization, In Vivo Antihypertension, and Molecular Docking

Antioxidant and antihypertensive effects of garlic protein and its hydrolysates and the related mechanism

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