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Bioorg Med Chem Lett. 1999 Jun 7;9(11):1511-6.

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

Author information

1
Département de Pharmacochimie Moléculaire et Structurale INSERM U266 - CNRS UMR 8600 UFR des Sciences Pharmaceutiques et Biologiques, Paris, France.

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.

PMID:
10386926
[Indexed for MEDLINE]

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