tetano
Editor, Senior Moderator
J Med Chem. 2017 Dec 8. doi: 10.1021/acs.jmedchem.7b00908. [Epub ahead of print]
[h=1]Aniline-based inhibitors of influenza H1N1 virus acting on hemagglutinin-mediated fusion.[/h] Leiva R, Barniol-Xicota M, Codony S, Ginex T, Vanderlinden E, Montes M, Caffrey M, Luque FJ, Naesens L, Vazquez S.
[h=3]Abstract[/h] Two series of easily accessible anilines were identified as inhibitors of influenza A virus subtype H1N1, and extensive chemical synthesis and analysis of the structure-activity relationship were performed. The compounds were shown to interfere with low pH-induced membrane fusion mediated by the H1 and H5 (group 1) hemagglutinin (HA) subtypes. A combination of virus resistance, HA interaction and molecular dynamics simulation studies elucidated the binding site of these aniline-based influenza fusion inhibitors, which significantly overlaps with the pocket occupied by some H3 HA-specific inhibitors, indicating the high relevance of this cavity for drug design.
PMID: 29220568 DOI: 10.1021/acs.jmedchem.7b00908
[h=1]Aniline-based inhibitors of influenza H1N1 virus acting on hemagglutinin-mediated fusion.[/h] Leiva R, Barniol-Xicota M, Codony S, Ginex T, Vanderlinden E, Montes M, Caffrey M, Luque FJ, Naesens L, Vazquez S.
[h=3]Abstract[/h] Two series of easily accessible anilines were identified as inhibitors of influenza A virus subtype H1N1, and extensive chemical synthesis and analysis of the structure-activity relationship were performed. The compounds were shown to interfere with low pH-induced membrane fusion mediated by the H1 and H5 (group 1) hemagglutinin (HA) subtypes. A combination of virus resistance, HA interaction and molecular dynamics simulation studies elucidated the binding site of these aniline-based influenza fusion inhibitors, which significantly overlaps with the pocket occupied by some H3 HA-specific inhibitors, indicating the high relevance of this cavity for drug design.
PMID: 29220568 DOI: 10.1021/acs.jmedchem.7b00908