title: Synthesis and properties of the first all-aza analogue of a biologically active peptide.
abstract: 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.
authors.affiliation: E. Merck Darmstadt, Medicinal Chemistry Cardiovascular Department, Germany.
authors.forename: J
authors.initials: J
authors.lastname: Gante
authors.forename: M
authors.initials: M
authors.lastname: Krug
authors.forename: G
authors.initials: G
authors.lastname: Lauterbach
authors.forename: R
authors.initials: R
authors.lastname: Weitzel
authors.forename: W
authors.initials: W
authors.lastname: Hiller
mesh_terms: 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
chemical_list: D001372:Aza Compounds; D004791:Enzyme Inhibitors; D010455:Peptides; D000092502:Renin Inhibitors