Design of the first highly potent and selective aminopeptidase N (EC 3.4.11.2) inhibitor

Bioorg Med Chem Lett. 1999 Jun 7;9(11):1511-6. doi: 10.1016/S0960-894X(99)00219-X.

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.

MeSH terms

  • Animals
  • CD13 Antigens / antagonists & inhibitors*
  • Drug Design
  • Enzyme Inhibitors / chemical synthesis*
  • Enzyme Inhibitors / pharmacokinetics
  • Kidney / enzymology
  • Kinetics
  • Swine

Substances

  • Enzyme Inhibitors
  • CD13 Antigens