Predicted Release and Analysis of Novel ACE-I, Renin, and DPP-IV Inhibitory Peptides from Common Oat (Avena sativa) Protein Hydrolysates Using in Silico Analysis

Bleakley, Stephen; Hayes, María; Shea, Nora O'; Gallagher, Eimear; Lafarga, Tomás

doi:10.3390/foods6120108

Cited by 61 publications

(47 citation statements)

References 59 publications

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“…ExPASy PeptideCutter was employed to simulate digestive reactions of col8a1 by pepsin and trypsin, with 214 cleavages sites generated from all possible fragments ( Table S10 ). These data indicate that the combination of various enzymes increases the number of peptides, although not all predicted AHTPs could be produced or some peptides occurred with unknown activities [ 34 , 35 ]. For example, AHTPs of GLP, GPL and LPG are always split by pepsin, while PGF, GDK, PGK and PQY, whose activities have not been proved yet, appeared as potential candidates according to the prediction of AHTpin [ 36 ] ( ).…”

Section: Discussionmentioning

confidence: 99%

“…For example, AHTPs of GLP, GPL and LPG are always split by pepsin, while PGF, GDK, PGK and PQY, whose activities have not been proved yet, appeared as potential candidates according to the prediction of AHTpin [ 36 ] ( ). In fact, many platforms could identify AHTPs in protein hydrolysates in silico, demonstrating the advantages of bioinformatics for instructing us to perform subsequent physiological tests [ 34 , 37 ]. The actual situation, nonetheless, has numerous complex tasks to complete.…”

Section: Discussionmentioning

confidence: 99%

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High Throughput Identification of Antihypertensive Peptides from Fish Proteome Datasets

Zhang

et al. 2018

Marine Drugs

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Antihypertensive peptides (AHTPs) are a group of small peptides with the main role to block key enzymes or receptors in the angiotensin genesis pathway. A great number of AHTPs have been isolated or digested from natural food resources; however, comprehensive studies on comparisons of AHTPs in various species from the perspective of big data are rare. Here, we established a simplified local AHTP database, and performed in situ mapping for high throughput identification of AHTPs with high antihypertensive activity from high-quality whole proteome datasets of 18 fish species. In the 35 identified AHTPs with reported high activity, we observed that Gly-Leu-Pro, Leu-Pro-Gly, and Val-Ser-Val are the major components of fish proteins, and AHTP hit numbers in various species demonstrated a similar distributing pattern. Interestingly, Atlantic salmon (Salmo salar) is in possession of far more abundant AHTPs compared with other fish species. In addition, collagen subunit protein is the largest group with more matching AHTPs. Further exploration of two collagen subunits (col4a5 and col8a1) in more fish species suggested that the hit pattern of these conserved proteins among teleost is almost the same, and their phylogeny is consistent with the evolution of these fish species. In summary, our present study provides basic information for the relationship of AHTPs with fish proteins, which sheds light on rapid discovery of marine drugs or food additives from fish protein hydrolysates to alleviate hypertension.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

High Throughput Identification of Antihypertensive Peptides from Fish Proteome Datasets

Zhang

et al. 2018

Marine Drugs

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“…Peptide Ranker is a database which predicts the probability (between 0 and 1) of a peptide to be bioactive. (Bleakley, Hayes, O' Shea, Gallagher, & Lafarga, 2017). The closer the predicted probability is to 1, the higher the confidence in the biological activity of the peptide.…”

Section: Bioactive Prediction Of Tri-peptidesmentioning

confidence: 99%

Novel ACE inhibitors derived from soybean proteins using in silico and in vitro studies

Zhao

Xue

et al. 2019

J Food Biochem

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The widespread application of soybean‐derived peptides is currently limited due to the challenges in the identification of peptides. In the present work, in silico and in vitro analysis were applied to identify ACE inhibitory tri‐peptides from soybean protein. The soybean protein was cleaved by PeptideCutter. Then, unknown tri‐peptides were selected to solubility estimation and ADME prediction. Subsequently, Discovery Studio was applied to evaluate the interaction mechanism between ACE and tri‐peptides. Finally, in vitro activity of theoretical ACE inhibitory tri‐peptides was verified by RP‐HPLC method. As a result, DMG was selected as a potent ACE inhibitory peptide. Cell experiment showed that DMG had no cytotoxic effects on HEK‐293 cells. And molecular docking results indicated that DMG contacted well with ACE’s active sites (Gln281, His353, Ala354, Glu384, Lys511, His513, and Tyr520). Furthermore, DMG could exert potent activity against ACE, with IC50 value of 3.95 ± 0.11 mM. Practical applications Present research showed soybean is a potential protein resource to obtain ACE inhibitory peptides. Simultaneously, virtual screening method is a feasible way to substitute for classical method in emerging nutritional fields. What's more, present study provides a theoretical basis for industrial research on foodstuff for ACE inhibitory peptides without side effects.

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“…In another recent work and using oat proteins, in silico analysis was used to identify six potential renin‐inhibitory peptides: IFFFL, FFG, WCY, PFL, FLLA, and WWK (Bleakley, Hayes, O’Shea, Gallagher, & Lafarga, ). However, in vitro evaluation showed very poor renin inhibition with a highest value of ~18% for IFFFL followed by 10% for WWK and lower values for FLLA, PFL and WCY while FFG had no measurable effect at 1 mg/mL peptide concentration (Figure ).…”

Section: Seed Protein Hydrolysatesmentioning

confidence: 99%

Food protein-derived renin-inhibitory peptides:in vitroandin vivoproperties

Aluko

2018

J Food Biochem

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Renin catalyzes the rate-determining step in the renin-angiotensin-aldosterone system that regulates mammalian blood pressure by converting angiotensinogen to angiotensin I (Ang I). Excessive plasma levels of Ang I is a causative factor in hypertension development. Therefore, inhibition of renin activity can lower blood pressure and provide relief from clinical symptoms associated with hypertension. Synthetic compounds are currently the most used group of renin inhibitors; however, only aliskiren is approved as a drug for hypertension treatment. But some negative side effects are associated with aliskiren therapy, which have necessitated the search for alternative natural compounds such as food protein-derived renin-inhibitory peptides with blood pressure-reducing effects. This paper is a concise review of the currently known sources and methods of production of renin-inhibitory peptides including their potential in vitro and in vivo extent of renin inhibition. Practical applicationsHypertension is a major human chronic disease that leads to severe cardiovascular impairment and ultimately death if not managed properly. Current therapeutic approach to hypertension management involves the use of drugs that inhibit excessive activities of renin and angiotensin converting enzyme (ACE), the two main enzymes that control mammalian blood pressure. Since renin catalyzes a single reaction that is the rate-determining step in the renin-angiotensin system, inhibition of this enzyme activity could be a highly effective strategy for controlling blood pressure without severe negative side effects. However, therapeutic control of renin activity remains difficult with only one approved drug. Some food protein-derived peptides have been found to inhibit renin activity inhibition, which could offer a drug-free treatment for hypertension. Therefore, this review provides a summary of recent developments in the advances and efficacy testing of renin-inhibitory peptides. K E Y W O R D Sbioactive peptides, blood pressure, food proteins, protein hydrolyzates, renin, renin-angiotensin system, spontaneously hypertensive rats How to cite this article: Aluko RE. Food protein-derived renin-inhibitory peptides: in vitro and in vivo properties.

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Predicted Release and Analysis of Novel ACE-I, Renin, and DPP-IV Inhibitory Peptides from Common Oat (Avena sativa) Protein Hydrolysates Using in Silico Analysis

Cited by 61 publications

References 59 publications

High Throughput Identification of Antihypertensive Peptides from Fish Proteome Datasets

High Throughput Identification of Antihypertensive Peptides from Fish Proteome Datasets

Novel ACE inhibitors derived from soybean proteins using in silico and in vitro studies

Food protein-derived renin-inhibitory peptides:in vitroandin vivoproperties

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