208720-79-0

Upstream product

• 187226-97-7 (3R,4R,5S)-4-Acetylamino-5-azido-3-methoxymethoxy-cyclohex-1-enecarboxylic acid methyl ester 
• 187226-93-3 (1R,5R,6R)-5-Methoxymethoxy-7-aza-bicyclo[4.1.0]hept-3-ene-3-carboxylic acid methyl ester 
• 145013-05-4 tert-butyl N-({[(tert-butoxy)carbonyl]amino}methanethioyl)carbamate 
• 208720-71-2 methyl (3R,4R,5S)-4-acetamido-5-amino-3-(pentan-3-yloxy)cyclohex-1-ene-1-carboxylate 
• 187226-95-5 (3R,4R,5S)-4-Amino-5-azido-3-methoxymethoxy-cyclohex-1-enecarboxylic acid methyl ester 
• 187226-91-1 (3R,4S,5R)-5-Azido-4-methanesulfonyloxy-3-methoxymethoxy-cyclohex-1-enecarboxylic acid methyl ester 
• 187226-89-7 (3R,4S,5R)-5-Azido-4-hydroxy-3-methoxymethoxy-cyclohex-1-enecarboxylic acid methyl ester 

Relevant academic research and scientific papers

Novel compound, its synthetic method and therapeutic use (by machine translation)

Novel compounds are described. The compounds generally comprise an acidic group, a basic group, a substituted amino or N-acyl and a group having an optionally hydroxylated alkane moiety. Pharmaceutical compositions comprising the inhibitors of the invention are also described. Methods of inhibiting neuraminidase in samples suspected of containing neuraminidase are also described. Antigenic materials, polymers, antibodies, conjugates of the compounds of the invention with labels, and assay methods for detecting neuraminidase activity are also described.

Structure-activity relationship studies of novel carbocyclic influenza neuraminidase inhibitors

A series of influenza neuraminidase inhibitors with the cyclohexene scaffold containing lipophilic side chains have been synthesized and evaluated for influenza A and B neuraminidase inhibitory activity. The size and geometry of side chains have been modified systematically in order to investigate structure-activity relationships of this class of compounds. The X-ray crystal structures of several analogues complexed with neuraminidase revealed that the lipophilic side chains bound to the hydrophobic pocket consisted of Glu276, Ala246, Arg224, and Ile222 of the enzyme active site. The structure-activity relationship studies of this series have also demonstrated remarkably different inhibitory potency between influenza A and B neuraminidase. This indicated that the lipophilic side chains had quite different hydrophobic interactions with influenza A and B neuraminidase despite their complete homology in the active site. Influenza B neuraminidase appeared to be much more sensitive toward the increased steric bulkiness of inhibitors compared to influenza A neuraminidase. From the extensive structure-activity relationship investigation reported in this article, GS 4071 emerged as one of the most potent influenza neuraminidase inhibitors against both influenza A and B strains.