Improved Synthesis of Lysine- and Arginine-Derived Amadori and Heyns Products and in Vitro Measurement of their Angiotensin I-Converting Enzyme Inhibitory Activity

2012 ◽  
Vol 60 (6) ◽  
pp. 1522-1527 ◽  
Author(s):  
Sudhanva M. Srinivas ◽  
Nanishankar V. Harohally
Keyword(s):  
Inhibitory Activity ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Angiotensin I Converting Enzyme

scholarly journals Angiotensin I-converting Enzyme (ACE) Inhibitory Activity and Chemical Composition of Alchemilla Viridiflora Rothm.

2021 ◽  
Author(s):  
Jelena Radović ◽  
Relja Suručić ◽  
Marjan Niketić ◽  
Tatjana Kundakovic-Vasovic
Keyword(s):  
Inhibitory Activity ◽  
Methanol Extract ◽  
Flavonoid Glycosides ◽  
Herbaceous Plant ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Ace Inhibitory Activity ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory

Abstract Alchemilla viridiflora Rothm., Rosaceae is a herbaceous plant widespread in central Greece, Bulgaria, North Macedonia and Serbia with Kosovo. LC-MS analysis leads to the identification of 20 compounds in methanol extract, mainly ellagitannins and flavonoid glycosides. Considering that different plant extracts were traditionally used for treatment of hypertension and that some of the analyzed methanol extract constituents possess beneficial cardiovascular effects, we hypothesized that some of these effects are achieved through inhibition of angiotensin I-converting enzyme (ACE). The dose-dependent activities ACE inhibitory activity of A. viridiflora and miquelianin were observed with an IC50 of 2.51 ± 0.00 µg/ml of A. viridiflora compared to IC50 of 2.59 ± 0.00 µg/mL for miquelianin. Contribution of the single compounds to the tested activity was further analyzed through the in silico experimental approach. Computational docking results showed that tiliroside, ellagic acid pentose and galloyl-HHDP-glucose exhibited even better binding affinity for ACE active site than miquelianin, which ACE activity was confirmed by an in vitro assay.

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 Inhibitory Peptides Obtained afterIn VitroHydrolysis of Pea (Pisum sativumvar. Bajka) Globulins

2014 ◽  
Vol 2014 ◽  
pp. 1-8 ◽  
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.

Sign in / Sign up

Export Citation Format

Share Document