scholarly journals ACE inhibitory peptides in standard and fermented deer velvet: an in silico and in vitro investigation

2019 ◽  
Vol 19 (1) ◽  
Author(s):  
Stephen R. Haines ◽  
Mark J. McCann ◽  
Anita J. Grosvenor ◽  
Ancy Thomas ◽  
Alasdair Noble ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
In Silico ◽  
Bioactive Peptides ◽  
Gastrointestinal Digestion ◽  
Ace Inhibitory Activity ◽  
In Vitro Investigation ◽  
Vitro Analysis ◽  
Ace Inhibitory ◽  
In Vitro Analysis

Abstract Background The use of deer velvet antler (DVA) as a potent traditional medicine ingredient goes back for over 2000 years in Asia. Increasingly, though, DVA is being included as a high protein functional food ingredient in convenient, ready to consume products in Korea and China. As such, it is a potential source of endogenous bioactive peptides and of ‘cryptides’, i.e. bioactive peptides enzymatically released by endogenous proteases, by processing and/or by gastrointestinal digestion. Fermentation is an example of a processing step known to release bioactive peptides from food proteins. In this study, we aimed to identify in silico bioactive peptides and cryptides in DVA, before and after fermentation, and subsequently to validate the major predicted bioactivity by in vitro analysis. Methods Peptides that were either free or located within proteins were identified in the DVA samples by liquid chromatography-tandem mass spectrometry (LC-MS/MS) followed by database searching. Bioactive peptides and cryptides were identified in silico by sequence matching against a database of known bioactive peptides. Angiotensin-converting enzyme (ACE) inhibitory activity was measured by a colorimetric method. Results Three free bioactive peptides (LVVYPW, LVVYPWTQ and VVYPWTQ) were solely found in fermented DVA, the latter two of which are known ACE inhibitors. However matches to multiple ACE inhibitor cryptides were obtained within protein and peptide sequences of both unfermented and fermented DVA. In vitro analysis showed that the ACE inhibitory activity of DVA was more pronounced in the fermented sample, but both unfermented and fermented DVA had similar activity following release of cryptides by simulated gastrointestinal digestion. Conclusions DVA contains multiple ACE inhibitory peptide sequences that may be released by fermentation or following oral consumption, and which may provide a health benefit through positive effects on the cardiovascular system. The study illustrates the power of in silico combined with in vitro methods for analysis of the effects of processing on bioactive peptides in complex functional ingredients like DVA.

scholarly journals Simulated Gastrointestinal Digestion of Cocoa: Detection of Resistant Peptides and In Silico/In Vitro Prediction of Their Ace Inhibitory Activity

Nutrients ◽  
2019 ◽  
Vol 11 (5) ◽  
pp. 985 ◽  
Author(s):  
Angela Marseglia ◽  
Luca Dellafiora ◽  
Barbara Prandi ◽  
Veronica Lolli ◽  
Stefano Sforza ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
In Silico ◽  
Internal Standard ◽  
Gastrointestinal Digestion ◽  
Ace Inhibitory Activity ◽  
Cocoa Beans ◽  
Vitro Assay ◽  
Simulated Gastrointestinal Digestion ◽  
Ace Inhibitory

In this study we investigated the oligopeptide pattern in fermented cocoa beans and derived products after simulated gastrointestinal digestion. Peptides in digested cocoa samples were identified based on the mass fragmentation and on the software analysis of vicilin and 21 KDa cocoa seed protein sequences, the most abundant cocoa proteins. Quantification was carried out by liquid chromatography/electrospray ionisation mass spectrometry (LC/ESI-MS) using an internal standard. Sixty five peptides were identified in the digested samples, including three pyroglutamyl derivatives. The in vitro angiotensin-converting enzyme (ACE)-inhibitory activity of cocoa digests were tested, demonstrating a high inhibition activity, especially for digestates of cocoa beans. The peptides identified were screened for their potential ACE inhibitory activity through an in silico approach, and about 20 di-, three- and tetra-peptides actually present in our samples were predicted as active. Two of the potentially active peptides were chemically synthesized and then assessed for their inhibitory activity by using the ACE in vitro assay. These peptides demonstrated an ACE inhibitory activity, however, that was too weak to explain alone the high activity of cocoa digestates, suggesting a synergic effect of all cocoa peptides. As a whole, results showed that an average chocolate portion (30 g) ensures an amount of peptides after digestion that, assuming complete absorption, could reach almost a complete inhibition of ACE.

Angiotensin I Converting Enzyme–Inhibitory Activity of Bovine, Ovine, and Caprine κ-Casein Macropeptides and Their Tryptic Hydrolysates

2003 ◽  
Vol 66 (9) ◽  
pp. 1686-1692 ◽  
Author(s):  
M. A. MANSO ◽  
R. LÓPEZ-FANDIÑO
Keyword(s):  
Inhibitory Activity ◽  
Converting Enzyme ◽  
Gastrointestinal Digestion ◽  
Ace Inhibitory Activity ◽  
Angiotensin I Converting Enzyme ◽  
Gastrointestinal Conditions ◽  
Tryptic Hydrolysate ◽  
Inhibitory Activities ◽  
Ace Inhibitory

This work evaluated the angiotensin-converting enzyme (ACE)–inhibitory activities of bovine, ovine, and caprine κ-casein macropeptides (CMPs) and their tryptic hydrolysates. The results obtained indicate that bovine, ovine, and caprine CMPs exhibited moderate in vitro ACE-inhibitory activities that increased considerably after digestion under simulated gastrointestinal conditions. Active peptides could also be produced from CMPs via proteolysis with trypsin, with tryptic hydrolysates exhibiting a more extensive ACE-inhibitory activity than intact CMPs during simulated gastrointestinal digestion. Two active fractions were chromatographically separated from the tryptic hydrolysate of the bovine CMP, but their complexity hampered the assignment of the ACE-inhibitory activity to specific peptide sequences. Evidence for the release of the strong ACE-inhibitory tripeptide IPP was found upon simulation of the gastrointestinal digestion of peptides released by trypsin from the CMP sequence. These findings might help to promote further exploitation of cheese whey in the preparation of nutraceuticals for inclusion in the composition of functional food products with high added values.

Effect of simulated gastrointestinal digestion on the antihypertensive properties of synthetic β-lactoglobulin peptide sequences

2007 ◽  
Vol 74 (3) ◽  
pp. 336-339 ◽  
Author(s):  
Blanca Hernández-Ledesma ◽  
Marta Miguel ◽  
Lourdes Amigo ◽  
Maria Amaya Aleixandre ◽  
Isidra Recio
Keyword(s):  
Inhibitory Activity ◽  
Ace Inhibition ◽  
Antihypertensive Activity ◽  
Gastrointestinal Digestion ◽  
Ace Inhibitory Activity ◽  
Simulated Gastrointestinal Digestion ◽  
The Impact ◽  
Β Lactoglobulin ◽  
Ace Inhibitory

In this study, the antihypertensive activity in spontaneously hypertensive rats of two peptides isolated from β-lactoglobulin hydrolysates with thermolysin was evaluated. These peptides, with sequences LLF [β-lg f(103–105)] and LQKW [β-lg f(58–61)], showed potent in vitro ACE-inhibitory activity. Two hours after administration, both sequences caused a clear and significant decrease in the blood pressure of these rats. The impact of a simulated gastrointestinal digestion on ACE-inhibitory and antihypertensive activities of these peptides was also studied. The results showed that both fragments were susceptible to proteolytic degradation after incubation with pepsin and Corolase PP®. In addition, their in vitro ACE-inhibitory activity decreased after the simulated digestion. It is likely that fragment LQK was the active end product of the gastrointestinal digestion of peptide LQKW. The fragment LL, observed after digestion of peptide LLF, probably exert its antihypertensive effect through a mechanism of action different than ACE-inhibition.

scholarly journals In Silico Analysis and In Vitro Characterization of the Bioactive Profile of Three Novel Peptides Identified from 19 kDa α-Zein Sequences of Maize

Molecules ◽  
2020 ◽  
Vol 25 (22) ◽  
pp. 5405
Author(s):  
Jorge L. Díaz-Gómez ◽  
Ines Neundorf ◽  
Laura-Margarita López-Castillo ◽  
Fabiola Castorena-Torres ◽  
Sergio O. Serna-Saldívar ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
In Silico ◽  
Structural Model ◽  
Solid Phase ◽  
Antioxidant Activities ◽  
Ace Inhibitory Activity ◽  
Helical Structures ◽  
In Vitro Characterization ◽  
Ace Inhibitory

In this study, we characterized three novel peptides derived from the 19 kDa α-zein, and determined their bioactive profile in vitro and developed a structural model in silico. The peptides, 19ZP1, 19ZP2 and 19ZP3, formed α-helical structures and had positive and negative electrostatic potential surfaces (range of −1 to +1). According to the in silico algorithms, the peptides displayed low probabilities for cytotoxicity (≤0.05%), cell penetration (10–33%) and antioxidant activities (9–12.5%). Instead, they displayed a 40% probability for angiotensin-converting enzyme (ACE) inhibitory activity. For in vitro characterization, peptides were synthesized by solid phase synthesis and tested accordingly. We assumed α-helical structures for 19ZP1 and 19ZP2 under hydrophobic conditions. The peptides displayed antioxidant activity and ACE-inhibitory activity, with 19ZP1 being the most active. Our results highlight that the 19 kDa α-zein sequences could be explored as a source of bioactive peptides, and indicate that in silico approaches are useful to predict peptide bioactivities, but more structural analysis is necessary to obtain more accurate data.

scholarly journals Effect of in Vitro Gastrointestinal Digestion on Bioactivity of Poultry Protein Hydrolysate

2016 ◽  
Vol 4 (Special-Issue-October) ◽  
pp. 77-86 ◽  
Author(s):  
Torkova Anna ◽  
Kononikhin Alexey ◽  
Bugrova Anna ◽  
Khotchenkov Vyacheslav ◽  
Tsentalovich Mikhail ◽  
...  
Keyword(s):  
Antioxidant Activity ◽  
Inhibitory Activity ◽  
Protein Hydrolysate ◽  
Gastrointestinal Digestion ◽  
Ace Inhibitory Activity ◽  
Food Ingredient ◽  
Inhibitory Peptides ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory

In vitro simulated gastrointestinal digestion (GID) was performed to evaluate changes in bioactive properties of Poultry protein hydrolysate HCP Premium P150 (PPH) showing strong antioxidant (448.2±37.0 µM TE/g of protein) and moderate Angiotensin-I converting enzyme inhibitory activity (IC50 0.617±0.022 mg/ml). Antioxidant and ACE-inhibitory activity were measured with use of ORAC assay and FRET-substrate methods, correspondingly. Gastric digestion (GD) increased ACE inhibitory activity 2.23 times and didn’t change antioxidant activity of PPH significantly. The subsequent intestinal digestion increased antioxidant activity 1.29 times and didn’t change ACE-inhibitory activity significantly. New potent ACE-inhibitory peptides: APGAPGPVG (IC50 16.2±3.8 µM), PDLVF (IC50 84.9±6.3 µM) and antioxidant dipeptide WG (2.29±0.04 µM TE/µM) were identified in the digested PPH. The digested PPH proved to be a rich source of antioxidant and ACE inhibiting molecules and could be a potential new food ingredient used for prevention or treatment of socially significant diseases.

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