STUDIES ON THE STRUCTURAL FEATURE OF S'1 SUBSITE OF NEPRILYSIN (EC.3.4.24.11) - STEREOCHEMICAL REQUIREMENT FOR THE ENZYME-INHIBITOR DOCKINGPROCESS

Authors
DANVY D MONTEIL T PLAQUEVENT JC DUHAMEL L DUHAMEL P GROS C NOEL N SCHWARTZ JC LECOMTE JM
Citation
D. Danvy et al., STUDIES ON THE STRUCTURAL FEATURE OF S'1 SUBSITE OF NEPRILYSIN (EC.3.4.24.11) - STEREOCHEMICAL REQUIREMENT FOR THE ENZYME-INHIBITOR DOCKINGPROCESS, Bioorganic & medicinal chemistry letters, 6(20), 1996, pp. 2437-2440
Citations number
16
Categorie Soggetti
Chemistry Inorganic & Nuclear","Chemistry Medicinal
Journal title
Bioorganic & medicinal chemistry letters → ACNP
ISSN journal
0960894X
Volume
6
Issue
20
Year of publication
1996
Pages
2437 - 2440
Database
ISI
SICI code
0960-894X(1996)6:20<2437:SOTSFO>2.0.ZU;2-2
Abstract
The preferred conformation of thiorphan during the inhibitor-neprilysi n docking process was investigated. A series of achiral inhibitors wer e tested. This study led to the design of a potent inhibitor, in which the ethylenic bond bears the aryl residue of P'1. Copyright (C) 1996 Elsevier Science Ltd.