Studies on the structural feature of S'1 subsite of neprilysin (EC.3.4.24.11): Stereochemical requirement for the enzyme-inhibitor docking process

Autor:	Jean-Charles Schwartz, Lucette Duhamel, Jeanne-Marie Lecomte, Denis Danvy, Claude Gros, Jean-Christophe Plaquevent, Thierry Monteil, Nadine Noel, Pierre Duhamel
Rok vydání:	1996
Předmět:	biology Stereochemistry Aryl Organic Chemistry Clinical Biochemistry Pharmaceutical Science Thiorphan Biochemistry chemistry.chemical_compound chemistry Enzyme inhibitor Docking (molecular) Drug Discovery biology.protein Molecular Medicine Molecular Biology Neprilysin
Zdroj:	Bioorganic & Medicinal Chemistry Letters. 6:2437-2440
ISSN:	0960-894X
DOI:	10.1016/0960-894x(96)00448-9
Popis:	The preferred conformation of thiorphan during the inhibitor-neprilysin docking process was investigated. A series of achiral inhibitors were tested. This study led to the design of a potent inhibitor, in which the ethylenic bond bears the aryl residue of P′1.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::1eedce172988cf0b4854c502db0a4ab7 https://doi.org/10.1016/0960-894x(96)00448-9 Zobrazit plný text záznamu Full Text from ScienceDirect