Thiol-based angiotensin-converting enzyme 2 inhibitors: P(1) modifications for the exploration of the S(1) subsite

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Screening of a metalloprotease library led to the identification of a thiol-based dual ACE/NEP inhibitor as a potent ACE2 inhibitor. Modifications of the P(1) benzyl moiety led to improvements in ACE2 potency as well as to increased selectivity versus ACE and NEP.

Detalles Bibliográficos
Autores principales: Deaton, David N., Gao, Enoch N., Graham, Kevin P., Gross, Jeffrey W., Miller, Aaron B., Strelow, John M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier Ltd. Published by Elsevier Ltd. 2008
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7126659/
https://www.ncbi.nlm.nih.gov/pubmed/18078750
http://dx.doi.org/10.1016/j.bmcl.2007.11.048
Descripción
Sumario:Screening of a metalloprotease library led to the identification of a thiol-based dual ACE/NEP inhibitor as a potent ACE2 inhibitor. Modifications of the P(1) benzyl moiety led to improvements in ACE2 potency as well as to increased selectivity versus ACE and NEP.

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