Binding inhibition of various influenza viruses by sialyllactose-modified trimer DNAs |
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Authors: | Miyuki Yamabe Kunihiro Kaihatsu Yasuhito Ebara |
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Affiliation: | 1. Graduate School of Human Development and Environment, Kobe University, 3-11 Tsurukabuto, Kobe, Hyogo 657-8501, Japan;2. Department of Organic Fine Chemicals, The Institute of Scientific and Industrial Research, Osaka University, 8-1 Mihogaoka, Ibaraki, Osaka 567-0047, Japan |
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Abstract: | 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. |
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Keywords: | Influenza virus Hemagglutinin Sialic acid DNA scaffold |
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