phosphoramidon and omapatrilat

phosphoramidon has been researched along with omapatrilat* in 2 studies

Reviews

1 review(s) available for phosphoramidon and omapatrilat

Article	Year
[The new class of drugs-- metalloprotease inhibitors -- in the treatment of heart failure]. Klinicheskaia meditsina, 2004, Volume: 82, Issue:5 Topics: Glycopeptides; Heart Failure; Hemodynamics; Humans; Indans; Metalloproteases; Propionates; Protease Inhibitors; Pyridines; Thiazepines; Thiorphan	2004

Other Studies

1 other study(ies) available for phosphoramidon and omapatrilat

Article	Year
Molecular Basis for Omapatrilat and Sampatrilat Binding to Neprilysin-Implications for Dual Inhibitor Design with Angiotensin-Converting Enzyme. Journal of medicinal chemistry, 2020, 05-28, Volume: 63, Issue:10 Neprilysin (NEP) and angiotensin-converting enzyme (ACE) are two key zinc-dependent metallopeptidases in the natriuretic peptide and kinin systems and renin-angiotensin-aldosterone system, respectively. They play an important role in blood pressure regulation and reducing the risk of heart failure. Vasopeptidase inhibitors omapatrilat and sampatrilat possess dual activity against these enzymes by blocking the ACE-dependent conversion of angiotensin I to the potent vasoconstrictor angiotensin II while simultaneously halting the NEP-dependent degradation of vasodilator atrial natriuretic peptide. Here, we report crystal structures of omapatrilat, sampatrilat, and sampatrilat-ASP (a sampatrilat analogue) in complex with NEP at 1.75, 2.65, and 2.6 Å, respectively. A detailed analysis of these structures and the corresponding structures of ACE with these inhibitors has provided the molecular basis of dual inhibitor recognition involving the catalytic site in both enzymes. This new information will be very useful in the design of safer and more selective vasopeptidase inhibitors of NEP and ACE for effective treatment in hypertension and heart failure. Topics: Angiotensin-Converting Enzyme Inhibitors; Antihypertensive Agents; Crystallography, X-Ray; Drug Design; Mesylates; Neprilysin; Peptidyl-Dipeptidase A; Protein Binding; Protein Structure, Secondary; Pyridines; Thiazepines; Tyrosine	2020

Article

Year

Molecular Basis for Omapatrilat and Sampatrilat Binding to Neprilysin-Implications for Dual Inhibitor Design with Angiotensin-Converting Enzyme.

Journal of medicinal chemistry, 2020, 05-28, Volume: 63, Issue:10

Neprilysin (NEP) and angiotensin-converting enzyme (ACE) are two key zinc-dependent metallopeptidases in the natriuretic peptide and kinin systems and renin-angiotensin-aldosterone system, respectively. They play an important role in blood pressure regulation and reducing the risk of heart failure. Vasopeptidase inhibitors omapatrilat and sampatrilat possess dual activity against these enzymes by blocking the ACE-dependent conversion of angiotensin I to the potent vasoconstrictor angiotensin II while simultaneously halting the NEP-dependent degradation of vasodilator atrial natriuretic peptide. Here, we report crystal structures of omapatrilat, sampatrilat, and sampatrilat-ASP (a sampatrilat analogue) in complex with NEP at 1.75, 2.65, and 2.6 Å, respectively. A detailed analysis of these structures and the corresponding structures of ACE with these inhibitors has provided the molecular basis of dual inhibitor recognition involving the catalytic site in both enzymes. This new information will be very useful in the design of safer and more selective vasopeptidase inhibitors of NEP and ACE for effective treatment in hypertension and heart failure.

Topics: Angiotensin-Converting Enzyme Inhibitors; Antihypertensive Agents; Crystallography, X-Ray; Drug Design; Mesylates; Neprilysin; Peptidyl-Dipeptidase A; Protein Binding; Protein Structure, Secondary; Pyridines; Thiazepines; Tyrosine

2020