title: Synthesis and molecular modeling of a lisinopril-tryptophan analogue inhibitor of angiotensin I-converting enzyme.
abstract: With a view to developing a more C-domain-selective angiotensin I-converting enzyme (ACE)-inhibitor, a novel analogue of lisinopril has been synthesized which incorporates a bulky P(2)(') tryptophan functionality. This inhibitor demonstrated a significantly increased specificity for the C-domain as compared with lisinopril. Molecular docking revealed hydrophobic and hydrogen-bonding interactions with residues of the C-domain S(2)(') subsite.
authors.affiliation: Institute of Infectious Disease and Molecular Medicine, University of Cape Town, Observatory, South Africa.
authors.forename: Aloysius T
authors.initials: AT
authors.lastname: Nchinda
authors.forename: Kelly
authors.initials: K
authors.lastname: Chibale
authors.forename: Pierre
authors.initials: P
authors.lastname: Redelinghuys
authors.forename: Edward D
authors.initials: ED
authors.lastname: Sturrock
mesh_terms: D000806:Angiotensin-Converting Enzyme Inhibitors / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology*; D001665:Binding Sites; D017706:Lisinopril / Q000737:chemistry*; D008958:Models, Molecular; D015394:Molecular Structure; D007703:Peptidyl-Dipeptidase A / Q000737:chemistry / Q000378:metabolism; D014364:Tryptophan / Q000031:analogs & derivatives / Q000138:chemical synthesis / Q000737:chemistry*
chemical_list: D000806:Angiotensin-Converting Enzyme Inhibitors; D014364:Tryptophan; D017706:Lisinopril; D007703:Peptidyl-Dipeptidase A