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 designe...

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Detalles Bibliográficos
Autores principales: Huixiong Chen, Roques, Bernard P., Fournié-Zaluski, Marie-Claude
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Published by Elsevier Ltd. 1999
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7172755/
https://www.ncbi.nlm.nih.gov/pubmed/10386926
http://dx.doi.org/10.1016/S0960-894X(99)00219-X
Descripción
Sumario: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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