In vitro study on digestion of peptides in Emmental cheese: Analytical evaluation and influence on angiotensin I converting enzyme inhibitory peptides

Angiotensin-I converting enzyme (ACE) is a zinc metallopeptidase that has an important role in regulating the renin-angiotensin-aldosterone system (RAAS). It is also an important drug target for the management of cardiovascular diseases. Hemorphins are endogenous peptides that are produced by proteolytic cleavage of beta hemoglobin. A number of studies have reported various therapeutic activities of hemorphins. Previous reports have shown antihypertensive action of hemorphins via the inhibition of ACE. The sequence of hemorphins is highly conserved among mammals, except in camels, which harbors a unique Q>R variation in the peptide. Here, we studied the ACE inhibitory activity of camel hemorphins (LVVYPWTRRF and YPWTRRF) and non-camel hemorphins (LVVYPWTQRF and YPWTQRF). Computational methods were used to determine the most likely binding pose and binding affinity of both camel and non-camel hemorphins within the active site of ACE. Molecular dynamics simulations showed that the peptides interacted with critical residues in the active site of ACE. Notably, camel hemorphins showed higher binding affinity and sustained interactions with all three subsites of the ACE active site. An in vitro ACE inhibition assay showed that the IC50 of camel hemorphins were significantly lower than the IC50 of non-camel hemorphins.

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In vitro-in silico screening strategy and mechanism of angiotensin I-converting enzyme inhibitory peptides from α-lactalbumin

LWT ◽

10.1016/j.lwt.2021.112984 ◽

2021 ◽

pp. 112984

Author(s):

Dewei Xie ◽

Lei Du ◽

Haisheng Lin ◽

Erzheng Su ◽

Yaling Shen ◽

...

Keyword(s):

In Silico ◽

Screening Strategy ◽

Converting Enzyme ◽

Angiotensin I ◽

In Silico Screening ◽

Inhibitory Peptides ◽

Angiotensin I Converting Enzyme

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Bioavailability of angiotensin I converting enzyme inhibitory peptides

British Journal Of Nutrition ◽

10.1079/bjn20041189 ◽

2004 ◽

Vol 92 (3) ◽

pp. 357-366 ◽

Cited By ~ 343

Author(s):

Vanessa Vermeirssen ◽

John Van Camp ◽

Willy Verstraete

Keyword(s):

Blood Pressure ◽

Antihypertensive Effect ◽

Converting Enzyme ◽

Angiotensin I ◽

Inhibitory Peptides ◽

Angiotensin I Converting Enzyme ◽

Ace Inhibitory Peptides ◽

Ace Inhibitory

Hypertension or high blood pressure is a significant health problem worldwide. Bioactive peptides that inhibit angiotensin I converting enzyme (ACE) in the cardiovascular system can contribute to the prevention and treatment of hypertension. These ACE inhibitory peptides are derived from many food proteins, especially milk proteins. An ACE inhibitory activity in vitro does not always imply an antihypertensive effect in vivo. Even if it does, it is very difficult to establish a direct relationship between in vitro and in vivo activity. This is mainly due to the bioavailability of the ACE inhibitory peptides after oral administration and the fact that peptides may influence blood pressure by mechanisms other than ACE inhibition. To exert an antihypertensive effect after oral ingestion, ACE inhibitory peptides have to reach the cardiovascular system in an active form. Therefore, they need to remain active during digestion by human proteases and be transported through the intestinal wall into the blood. The bioavailability of some ACE inhibitory peptides has been studied. It is also known that (hydroxy)proline-containing peptides are generally resistant to degradation by digestive enzymes. Peptides can be absorbed intact through the intestine by paracellular and transcellular routes, but the potency of the bioactivity after absorption is inversely correlated to chain length. In addition, some strategies are proposed to increase the bioavailability of ACE inhibitory peptides. Further research into the bioavailability of ACE inhibitory peptides will lead to the development of more effective ACE inhibitory peptides and foods.

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Angiotensin I Converting Enzyme Inhibitory Peptides Obtained afterIn VitroHydrolysis of Pea (Pisum sativumvar. Bajka) Globulins

BioMed Research International ◽

10.1155/2014/438459 ◽

2014 ◽

Vol 2014 ◽

pp. 1-8 ◽

Cited By ~ 28

Author(s):

Anna Jakubczyk ◽

Barbara Baraniak

Keyword(s):

Inhibitory Activity ◽

Deae Cellulose ◽

Degree Of Hydrolysis ◽

Converting Enzyme ◽

Angiotensin I ◽

Inhibitory Peptides ◽

Angiotensin I Converting Enzyme ◽

Ace Inhibitory Peptides ◽

Ace Inhibitory

Pea seeds represent a valuable source of active compounds that may positively influence health. In this study, the pea globulins were digestedin vitrounder gastrointestinal condition and potentially bioaccessible angiotensin I converting enzyme (ACE) inhibitory peptides were identified. The degree of hydrolysis after pepsin, 14.42%, and pancreatin, 30.65%, were noted. The peptides with the highest ACE inhibitory properties were separated using ion exchange chromatography on DEAE-cellulose. Thirteen peptides fractions were obtained but only four showed potential antihypertensive properties. The highest inhibitory activity was determined for the fraction F8 (IC50 = 0.0014 mg/mL). This fraction was separated on Sephadex G10 and two peptide fractions were obtained. The peptides fraction (B) with the highest ACE inhibitory activity (IC50 = 0.073 mg/mL) was identified by ESI-MS/MS. The sequences of ACE inhibitory peptides were GGSGNY, DLKLP, GSSDNR, MRDLK, and HNTPSR. Based on Lineweaver-Burk plots for the fraction B, the kinetic parameters asKm,Vmax, andKiand mode of inhibition were determined. This fraction belongs to uncompetitive inhibitor of ACE activity. The seeds of pea are the source of precursor protein, which releases the ACE inhibitory peptides as a result of enzymatic hydrolysis.

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