title: Design of the first highly potent and selective aminopeptidase N (EC 3.4.11.2) inhibitor.
abstract: A series of phosphinic compounds mimicking the transition state of substrates hydrolysed by aminopeptidase N (EC 3.4.11.2) were synthesized. These new compounds have potent inhibitory activities with Ki values in the nanomolar range. These derivatives behave as the most potent APN inhibitors designed to date.
authors.affiliation: Département de Pharmacochimie Moléculaire et Structurale INSERM U266 - CNRS UMR 8600 UFR des Sciences Pharmaceutiques et Biologiques, Paris, France.
authors.forename: H
authors.initials: H
authors.lastname: Chen
authors.forename: B P
authors.initials: BP
authors.lastname: Roques
authors.forename: M C
authors.initials: MC
authors.lastname: Fournié-Zaluski
mesh_terms: D000818:Animals; D018826:CD13 Antigens / Q000037:antagonists & inhibitors*; D015195:Drug Design; D004791:Enzyme Inhibitors / Q000138:chemical synthesis* / Q000493:pharmacokinetics; D007668:Kidney / Q000201:enzymology; D007700:Kinetics; D013552:Swine
chemical_list: D004791:Enzyme Inhibitors; D018826:CD13 Antigens