Design of the first highly potent and selective aminopeptidase N (EC 3.4.11.2) inhibitor.
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.
Chen
H
H
Département de Pharmacochimie Moléculaire et Structurale INSERM U266 - CNRS UMR 8600 UFR des Sciences Pharmaceutiques et Biologiques, Paris, France.
Roques
B P
BP
Fournié-Zaluski
M C
MC
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
D004791:Enzyme Inhibitors; D018826:CD13 Antigens