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  • Synthesis and evaluation of novel 3-C-alkylated-Neu5Ac2en derivatives as probes of influenza virus sialidase 150-loop flexibility

    Author(s)
    Rudrawar, Santosh
    Kerry, Philip S
    Rameix-Welti, Marie-Anne
    Maggioni, Andrea
    Dyason, Jeffrey C
    Rose, Faith J
    van der Werf, Sylvie
    Thomson, Robin J
    Naffakh, Nadia
    Russell, Rupert JM
    von Itzstein, Mark
    Griffith University Author(s)
    von Itzstein, Mark
    Thomson, Robin J.
    Dyason, Jeffrey C.
    Maggioni, Andrea
    Rose, Faith J.
    Rudrawar, Santosh
    Year published
    2012
    Metadata
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    Abstract
    Novel 3-C-alkylated-Neu5Ac2en derivatives have been designed to target the expanded active site cavity of influenza virus sialidases with an open 150-loop, currently seen in X-ray crystal structures of influenza A virus group-1 (N1, N4, N5, N8), but not group-2 (N2, N9), sialidases. The compounds show selectivity for inhibition of H5N1 and pdm09 H1N1 sialidases over an N2 sialidase, providing evidence of the relative 150-loop flexibility of these sialidases. In a complex with N8 sialidase, the C3 substituent of 3-phenylally-Neu5Ac2en occupies the 150-cavity while the central ring and the remaining substituents bind the active ...
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    Novel 3-C-alkylated-Neu5Ac2en derivatives have been designed to target the expanded active site cavity of influenza virus sialidases with an open 150-loop, currently seen in X-ray crystal structures of influenza A virus group-1 (N1, N4, N5, N8), but not group-2 (N2, N9), sialidases. The compounds show selectivity for inhibition of H5N1 and pdm09 H1N1 sialidases over an N2 sialidase, providing evidence of the relative 150-loop flexibility of these sialidases. In a complex with N8 sialidase, the C3 substituent of 3-phenylally-Neu5Ac2en occupies the 150-cavity while the central ring and the remaining substituents bind the active site as seen for the unsubstituted template. This new class of inhibitors, which can 'trap' the open 150-loop form of the sialidase, should prove useful as probes of 150-loop flexibility.
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    Journal Title
    Organic & Biomolecular Chemistry
    Volume
    10
    Issue
    43
    DOI
    https://doi.org/10.1039/c2ob25627d
    Subject
    Medicinal and biomolecular chemistry
    Biologically active molecules
    Organic chemistry
    Publication URI
    http://hdl.handle.net/10072/48643
    Collection
    • Journal articles

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