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
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author Huixiong Chen
Roques, Bernard P.
Fournié-Zaluski, Marie-Claude
author_facet Huixiong Chen
Roques, Bernard P.
Fournié-Zaluski, Marie-Claude
author_sort Huixiong Chen
collection PubMed
description 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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spelling pubmed-71727552020-04-22 Design of the first highly potent and selective aminopeptidase N (EC 3.4.11.2) inhibitor Huixiong Chen Roques, Bernard P. Fournié-Zaluski, Marie-Claude Bioorg Med Chem Lett Article 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. Published by Elsevier Ltd. 1999-06-07 1999-08-05 /pmc/articles/PMC7172755/ /pubmed/10386926 http://dx.doi.org/10.1016/S0960-894X(99)00219-X Text en Copyright © 1999 Published by Elsevier Ltd. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.
spellingShingle Article
Huixiong Chen
Roques, Bernard P.
Fournié-Zaluski, Marie-Claude
Design of the first highly potent and selective aminopeptidase N (EC 3.4.11.2) inhibitor
title Design of the first highly potent and selective aminopeptidase N (EC 3.4.11.2) inhibitor
title_full Design of the first highly potent and selective aminopeptidase N (EC 3.4.11.2) inhibitor
title_fullStr Design of the first highly potent and selective aminopeptidase N (EC 3.4.11.2) inhibitor
title_full_unstemmed Design of the first highly potent and selective aminopeptidase N (EC 3.4.11.2) inhibitor
title_short Design of the first highly potent and selective aminopeptidase N (EC 3.4.11.2) inhibitor
title_sort design of the first highly potent and selective aminopeptidase n (ec 3.4.11.2) inhibitor
topic Article
url 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
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