Angiotensin I-converting enzyme inhibitory peptides in oat (Avena sativa L.) proteins-derived digests – In silico and in vitro study

2016 ◽  
Vol 33 ◽  
pp. S173 ◽  
Author(s):  
Małgorzata Darewicz ◽  
Justyna Borawska ◽  
Monika Pliszka ◽  
Gerd E. Vegarud ◽  
Anna Iwaniak ◽  
...  
Keyword(s):  
Avena Sativa ◽  
In Silico ◽  
In Vitro Study ◽  
Vitro Study ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Inhibitory Peptides ◽  
Angiotensin I Converting Enzyme ◽  
L Proteins

Hybrid in Silico/in Vitro Approach for the Identification of Angiotensin I Converting Enzyme Inhibitory Peptides from Parma Dry-Cured Ham

2015 ◽  
Vol 63 (28) ◽  
pp. 6366-6375 ◽  
Author(s):  
Luca Dellafiora ◽  
Sara Paolella ◽  
Chiara Dall’Asta ◽  
Arnaldo Dossena ◽  
Pietro Cozzini ◽  
...  
Keyword(s):  
In Silico ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Inhibitory Peptides ◽  
Angiotensin I Converting Enzyme ◽  
Dry Cured Ham

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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