Synthesis and properties of the first all-aza analogue of a biologically active peptide.
The synthesis of the first all-aza-amino acid analogue (2) of a peptidic renin inhibitor is described. The X-ray structural analysis and molecular modelling investigations of this novel compound reveal interesting conformational features which have a significant impact on its biological activity. In addition, insight into conformational features of azapeptides in general in comparison with the corresponding purely peptidic compounds is given.
Gante
J
J
E. Merck Darmstadt, Medicinal Chemistry Cardiovascular Department, Germany.
Krug
M
M
Lauterbach
G
G
Weitzel
R
R
Hiller
W
W
D001372:Aza Compounds / Q000138:chemical synthesis* / Q000737:chemistry* / Q000494:pharmacology; D018360:Crystallography, X-Ray; D004791:Enzyme Inhibitors / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology; D006801:Humans; D066298:In Vitro Techniques; D008958:Models, Molecular; D015394:Molecular Structure; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry* / Q000494:pharmacology; D011487:Protein Conformation; D000092502:Renin Inhibitors
D001372:Aza Compounds; D004791:Enzyme Inhibitors; D010455:Peptides; D000092502:Renin Inhibitors