Probing the importance of spacial and conformational domains in captopril analogs for angiotensin converting enzyme activity.
A new synthesis of 4,5-methano-L-prolines and the enzymatic activity of the corresponding N-(3-mercapto-2-R-methyl-propionyl) analogs as inhibitors of angiotensin converting enzyme are described.
Hanessian
S
S
Department of Chemistry, Université de Montréal, Québec, Canada.
Reinhold
U
U
Saulnier
M
M
Claridge
S
S
D000806:Angiotensin-Converting Enzyme Inhibitors / Q000737:chemistry* / Q000494:pharmacology; D000818:Animals; D002216:Captopril / Q000031:analogs & derivatives* / Q000737:chemistry / Q000494:pharmacology; D015195:Drug Design; D007202:Indicators and Reagents; D007536:Isomerism; D008168:Lung / Q000201:enzymology; D008958:Models, Molecular; D008968:Molecular Conformation; D007703:Peptidyl-Dipeptidase A / Q000302:isolation & purification / Q000378:metabolism; D011392:Proline / Q000031:analogs & derivatives* / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology; D011817:Rabbits; D017257:Ramipril / Q000031:analogs & derivatives / Q000737:chemistry / Q000494:pharmacology; D013329:Structure-Activity Relationship
D000806:Angiotensin-Converting Enzyme Inhibitors; D007202:Indicators and Reagents; C052549:ramiprilat; D011392:Proline; D002216:Captopril; D007703:Peptidyl-Dipeptidase A; D017257:Ramipril