Ketomethyldipeptides I. A new class of angiotensin converting enzyme inhibitors

The design rationale for a new series of angiotensin-converting enzyme (ACE) inhibitors which incorporate a ketone substituent into a peptide backbone is described. Molecular regions which were expected to mimic the binding of an N-acyl tripeptide substrate at secondary binding sites S 1 and S 1′ we...

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Veröffentlicht in:	Biochemical and biophysical research communications 1984-10, Vol.124 (1), p.141-147
Hauptverfasser:	Natarajan, S., Gordon, E.M., Sabo, E.F., Godfrey, J.D., Weller, H.N., Pluščec, Jelka, Rom, M.B., Cushman, D.W.
Format:	Artikel
Sprache:	eng
Schlagworte:	Angiotensin-Converting Enzyme Inhibitors Biological and medical sciences Dipeptides - chemical synthesis Dipeptides - pharmacology General pharmacology ketomethyldipeptides Medical sciences peptidyl dipeptidase A Pharmacology. Drug treatments Physicochemical properties. Structure-activity relationships Protein Binding Stereoisomerism Structure-Activity Relationship
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