In vitro and ex vivo studies on angiotensin-i converting enzyme (Ace) inhibitory activity of short synthetic peptides
No Thumbnail Available
Date
2021-01-01
External link to pdf file
https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85105752032&origin=inward
Journal Title
Journal ISSN
Volume Title
Publisher
Abstract
In our days the interest in the studies of new angiotensin-converting-enzyme (ACE) inhibitors as modulators of the renin-angiotensin-system (RAS) is growing, not only because of their importance as drugs for arterial hypertension treatment, but also for their therapeutic potential during COVID-19 infection. This study presents data for the design and synthesis of short peptides by SPPS strategy and investigates in vitro and ex vivo their potential as ACE inhibitors in the light of structural changes. The obtained results give insight into the structure-activity relationship of peptide sequences and show differences regarding the effects of peptides in two experimental procedures (inhibitory potency on purified ACE activity and AT-I induced rat ileum contractions). Three of the newly synthesized peptides with terminal proline, LAP, LKP and VAP, showed relatively high inhibitory activities.