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Disrupting the Conserved Salt Bridge in the Trimerization of Influenza A Nucleoprotein

tetano

Editor, Senior Moderator
J Med Chem. 2019 Nov 26. doi: 10.1021/acs.jmedchem.9b01244. [Epub ahead of print] [h=1]Disrupting the Conserved Salt Bridge in the Trimerization of Influenza A Nucleoprotein.[/h]
Woodring J, Lu SH, Krasnova L, Wang SC, Chen JB, Chou CC, Huang YC, Cheng TJ, Wu YT, Chen YH, Fang JM, Tsai MD, Wong CH.
[h=3]Abstract[/h] Antiviral drug resistance in influenza infections has been a major threat to public health. In order to develop a broad-spectrum inhibitor of influenza to combat the problem of drug resistance, we previously identified the highly conserved E339…R416 salt bridge of the nucleoprotein trimer as a target, and compound 1 as an inhibitor disrupting the salt bridge with an EC[SUB]50[/SUB] = 2.7 ?M against influenza A (A/WSN/1933). We have further modified this compound via a structure-based approach and performed an antiviral activity screen to identify compounds 29 and 30 with EC[SUB]50[/SUB] values of 110 and 120 nM respectively and without measurable host cell cytotoxicity. Compared to the clinically used neuraminidase inhibitors, these two compounds showed better activity profiles against drug-resistant influenza A strains, as well as influenza B, and improved survival of influenza-infected mice.


PMID: 31769665 DOI: 10.1021/acs.jmedchem.9b01244
 
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