Angiotensin I-converting enzyme (ACE) inhibition and nitric oxide (NO)-mediated antihypertensive effect of octaphlorethol A isolated from Ishige sinicola: In vitro molecular mechanism and in vivo SHR model

2015 ◽  
Vol 18 ◽  
pp. 289-299 ◽  
Author(s):  
Seok-Chun Ko ◽  
Won-Kyo Jung ◽  
Sung-Myung Kang ◽  
Seung-Hong Lee ◽  
Min Cheol Kang ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Molecular Mechanism ◽  
Antihypertensive Effect ◽  
Ace Inhibition ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Angiotensin I Converting Enzyme

scholarly journals Bioavailability of angiotensin I converting enzyme inhibitory peptides

2004 ◽  
Vol 92 (3) ◽  
pp. 357-366 ◽  
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.

scholarly journals Aronia melanocarpa ElliotReduces the Activity of Angiotensin I-Converting Enzyme—In VitroandEx VivoStudies

2014 ◽  
Vol 2014 ◽  
pp. 1-7 ◽  
Author(s):  
Joanna Sikora ◽  
Marlena Broncel ◽  
Elżbieta Mikiciuk-Olasik
Keyword(s):  
Ace Inhibition ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Hypotensive Action ◽  
Aronia Melanocarpa ◽  
Clinical Observations ◽  
Angiotensin I Converting Enzyme ◽  
Ace Activity ◽  
Positive Correlations

Purpose. The aim of the study was to analyze the effects of two-month supplementation with chokeberry preparation on the activity of angiotensin I-converting enzyme (ACE) in patients with metabolic syndrome (MS). During thein vitrostage of the study, we determined the concentration of chokeberry extract, which inhibited the activity of ACE by 50% (IC50).Methods. The participants (n=70) were divided into three groups: I—patients with MS who received chokeberry extract supplements, II—healthy controls, and III—patients with MS treated with ACE inhibitors.Results. After one and two months of the experiment, a decrease in ACE activity corresponded to 25% and 30%, respectively. We documented significant positive correlations between the ACE activity and the systolic (r=0.459,P=0.048) and diastolic blood pressure, (r=0.603,P=0.005) and CRP. The IC50of chokeberry extract and captopril amounted to155.4±12.1 μg/mL and0.52±0.18 μg/mL, respectively.Conclusions. Ourin vitrostudy revealed that chokeberry extract is a relatively weak ACE inhibitor. However, the results of clinical observations suggest that the favorable hypotensive action of chokeberry polyphenols may be an outcome of both ACE inhibition and other pleotropic effects, for example, antioxidative effect.

scholarly journals Camel Hemorphins Exhibit a More Potent Angiotensin-I Converting Enzyme Inhibitory Activity than Other Mammalian Hemorphins: An In Silico and In Vitro Study

Biomolecules ◽  
2020 ◽  
Vol 10 (3) ◽  
pp. 486 ◽  
Author(s):  
Amanat Ali ◽  
Seham Abdullah Rashed Alzeyoudi ◽  
Shamma Abdulla Almutawa ◽  
Alya Nasir Alnajjar ◽  
Yusra Al Dhaheri ◽  
...  
Keyword(s):  
Binding Affinity ◽  
Active Site ◽  
Inhibitory Activity ◽  
In Vitro Study ◽  
Ace Inhibition ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Angiotensin I Converting Enzyme ◽  
Dynamics Simulations

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.

scholarly journals Angiotensin I-Converting Enzyme (ACE) Inhibitory Activity of Peptides Isolated from Carabao Mango (Mangifera indica) Flesh

KIMIKA ◽  
2021 ◽  
Vol 32 (1) ◽  
pp. 1-18
Author(s):  
Trisha Rojas ◽  
Jherome Co ◽  
Mia Clare Marie Bercansil ◽  
Lory Jane Dela Cruz ◽  
Lawrence Yves Uy ◽  
...  
Keyword(s):  
Mangifera Indica ◽  
Ace Inhibition ◽  
The Philippines ◽  
Antihypertensive Activity ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Inhibitory Peptide ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory

Hypertension has been reported as the second major cause of morbidity in the Philippines. One of the mechanisms to control blood pressure is through the inhibition of the angiotensin I-converting enzyme (ACE). This study specifically focused on the determination of ACE inhibitory activities of peptides from ‘Carabao’ mango flesh of three shell colors (SC1, SC3, SC5). The bioactive peptides were obtained upon a series of extraction, purification, and enzymatic hydrolysis steps. Among the undigested and digested crude and purified samples, the highest in vitro ACE inhibition was exhibited by the three-hour digest of SC3 (83.28 ± 0.83%). The most prominent peak from the fractionation of the mixture of peptides in SC3 digest was evaluated for ACE inhibition, and the decrease in activity inferred the synergistic effect of the peptides in exhibiting the inhibitory function. This selected bioactive peptide was revealed to have alanine and phenylalanine as the components, which can possibly be AF – an ACE inhibitory peptide determined from in silico analyses. Meanwhile, assessment of the in vivo antihypertensive activity showed no significant results due to insufficiently administered doses of the samples. Overall, the measured activity of the ACE inhibitory peptides inferred the potential of mango as a functional food in dealing with hypertension.  

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