Chocolate desserts with ricotta hydrolysates: In vitro study of inhibitory activity against angiotensin‐converting enzyme and cholinesterase

2020 ◽  
Vol 85 (10) ◽  
pp. 3003-3011
Author(s):  
Joanna Kobus‐Cisowska ◽  
Oskar Szczepaniak ◽  
Daria Szymanowska ◽  
Monika Przeor ◽  
Maciej Jarzębski ◽  
...  
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Inhibitory Activity ◽  
In Vitro Study ◽  
Vitro Study ◽  
Converting Enzyme

scholarly journals Inhibitory Activities of Polyphenolic Extracts of Bangladeshi Vegetables against α-Amylase, α-Glucosidase, Pancreatic Lipase, Renin, and Angiotensin-Converting Enzyme

Foods ◽  
2020 ◽  
Vol 9 (7) ◽  
pp. 844
Author(s):  
Razia Sultana ◽  
Adeola M. Alashi ◽  
Khaleda Islam ◽  
Md Saifullah ◽  
C. Emdad Haque ◽  
...  
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Pancreatic Lipase ◽  
Lipase Activity ◽  
Inhibitory Activity ◽  
The Other ◽  
Converting Enzyme ◽  
Inhibitory Activities ◽  
Ash Gourd ◽  
Better Than

The aim of the study was to determine the in vitro enzyme inhibition activities of aqueous polyphenolic extracts of nine popular Bangladeshi vegetables, namely ash gourd, bitter gourd, brinjal, Indian spinach, kangkong, okra, ridge gourd, snake gourd, and stem amaranth. Polyphenolic glycosides were the major compounds present in the extracts. Inhibition of α-amylase (up to 100% at 1 mg/mL) was stronger than α-glucosidase inhibition (up to 70.78% at 10 mg/mL). The Indian spinach extract was the strongest inhibitor of pancreatic lipase activity (IC50 = 276.77 µg/mL), which was significantly better than that of orlistat (381.16 µg/mL), a drug. Ash gourd (76.51%), brinjal (72.48%), and snake gourd (66.82%) extracts were the most effective inhibitors of angiotensin-converting enzyme (ACE), an enzyme whose excessive activities have been associated with hypertension. Brinjal also had a significantly higher renin-inhibitory activity than the other vegetable extracts. We conclude that the vegetable extracts may have the ability to reduce enzyme activities that have been associated with hyperglycemia, hyperlipidemia, and hypertension.

scholarly journals In vitro study on α-amylase inhibitory activity of an Indian medicinal plant, Phyllanthus amarus

2010 ◽  
Vol 42 (5) ◽  
pp. 280 ◽  
Author(s):  
A Mitra ◽  
IniyanG Tamil ◽  
B Dineshkumar ◽  
M Nandhakumar ◽  
M Senthilkumar
Keyword(s):  
Medicinal Plant ◽  
Inhibitory Activity ◽  
In Vitro Study ◽  
Vitro Study ◽  
Phyllanthus Amarus ◽  
Indian Medicinal Plant

Inhibitory activity of thymol on native and mature Gardnerella vaginalis biofilms: in vitro study

2011 ◽  
Vol 60 (11) ◽  
pp. 675-681 ◽  
Author(s):  
Pier Braga ◽  
Monica Sasso ◽  
Maria Culici ◽  
Alessandra Spallino
Keyword(s):  
Inhibitory Activity ◽  
In Vitro Study ◽  
Vitro Study ◽  
Gardnerella Vaginalis

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.

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