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Letters in Drug Design & Discovery

Editor-in-Chief

ISSN (Print): 1570-1808
ISSN (Online): 1875-628X

Docking Study, Synthesis and SAH-Hydrolase Inhibitory Activity of LAdeninylalanine and Related Analogues

Author(s): Nicolas Floquet, Samuel Leroy, Murielle Muzard, Georges Guillerm and Jean-Bernard Behr

Volume 2, Issue 8, 2005

Page: [579 - 583] Pages: 5

DOI: 10.2174/157018005774717262

Price: $65

Abstract

docking simulations were performed on the open and the closed conformations of (S)-adenosyl-Lhomocysteine- hydrolase with a series of L-adeninylalanine analogues. Theoretical Ki values were calculated and compared to experimental Kis, determined after enzymatic assay. These results suggest that the competitive inhibitors evaluated bind reversibly to the open form of SAH-hydrolase and do not induce the conformational transition to the closed conformation.

Keywords: Docking study, SAH-hydrolase, inhibitors, antiviral agents, nucleoside analogues


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