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Design of the first highly potent and selective aminopeptidase N (EC 3.4.11.2) inhibitor
H Chen1, B P Roques, M C Fournié-Zaluski
1Département 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.
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