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Binding inhibition of various influenza viruses by sialyllactose-modified trimer DNAs

tetano

Editor, Senior Moderator
Bioorg Med Chem Lett. 2019 Jan 2. pii: S0960-894X(18)31026-6. doi: 10.1016/j.bmcl.2018.12.064. [Epub ahead of print]
[h=1]Binding inhibition of various influenza viruses by sialyllactose-modified trimer DNAs.[/h] Yamabe M[SUP]1[/SUP], Kaihatsu K[SUP]2[/SUP], Ebara Y[SUP]3[/SUP].
[h=3]Author information[/h]

[h=3]Abstract[/h] Sialyllactose (SL)-modified trimer DNAs with a similar SL presentation as their binding sites on influenza virus hemagglutinin (HA) trimer were designed and synthesized. These trimer DNAs showed high affinity for various influenza viruses, including A/Puerto Rico/08/34 (H1N1), A/Beijing/262/95 (H1N1), A/Yokohama/77/2008 (H1N1), and A/Panama/2007/99 (H3N2). Thus, presentation of SL residues on three vertexes of the scaffold as well as sialic acid binding sites on the HA trimer regardless of a tri-branched or triangular scaffold are important for high affinity for influenza viruses. These compounds have the potential for use in detection and as inhibitors of a broad spectrum of influenza viruses.
Copyright ? 2019 Elsevier Ltd. All rights reserved.


[h=4]KEYWORDS:[/h] DNA scaffold; Hemagglutinin; Influenza virus; Sialic acid

PMID: 30655214 DOI: 10.1016/j.bmcl.2018.12.064
 
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