[Synthesis of angiotensin converting enzyme inhibitors containing residues of substituted quinolines and a study of their biological activity].
Inhibitors of the angiotensin-converting enzyme were synthesized by substituting N-and C-terminal amino acid residues of tripeptide Bz-Phe-Ala-Pro by the residues of 8-methoxy-5-sulphoquinoline and carboxy-1,2,3,4-tetrahydroquinoline, respectively, and their in vivo and in vitro biological activity was determined. The enzyme's S2' site proved to be non specific to the position of the carboxylic group in the C-terminal heterocyclic part of the inhibitor molecule. Introducing a modified quinoline residue into the N-terminal part of the inhibitor does not increase its specific interaction with the hydrophobic pocket of the angiotensin-converting enzyme.
Filatova
M P
MP
Krit
N A
NA
Uskova
N N
NN
Maksimova
E M
EM
Gracheva
I N
IN
Reĭssmann
Z
Z
D000806:Angiotensin-Converting Enzyme Inhibitors / Q000138:chemical synthesis* / Q000378:metabolism / Q000494:pharmacology; D000818:Animals; D001665:Binding Sites; D002216:Captopril / Q000494:pharmacology; D004656:Enalapril / Q000494:pharmacology; D007703:Peptidyl-Dipeptidase A / Q000378:metabolism; D011804:Quinolines / Q000737:chemistry*; D051381:Rats
D000806:Angiotensin-Converting Enzyme Inhibitors; D011804:Quinolines; D004656:Enalapril; D002216:Captopril; D007703:Peptidyl-Dipeptidase A
Sintez ingibitorov angiotenzinprevrashchaiushchego fermenta, soderzhashch ostatki zameshchennykh khinolinov, i issledovanie ikh biologicheskoĭ aktivnosti.