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  • Exploring Human Parainfluenza Virus Type-1 Hemagglutinin–Neuraminidase as a Target for Inhibitor Discovery

    Author(s)
    El-Deeb, Ibrahim M
    Guillon, Patrice
    Winger, Moritz
    Eveno, Tanguy
    Haselhorst, Thomas
    Dyason, Jeffrey C
    von Itzstein, Mark
    Griffith University Author(s)
    von Itzstein, Mark
    Dyason, Jeffrey C.
    Haselhorst, Thomas E.
    Guillon, Patrice M.
    El-Deeb, Ibrahim Mustafa
    Winger, Moritz
    Eveno, Tanguy
    Year published
    2014
    Metadata
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    Abstract
    Human parainfluenza virus type 1 is the major cause of croup in infants and young children. There is currently neither vaccine nor clinically effective treatment for parainfluenza virus infection. Hemagglutinin?neuraminidase glycoprotein is a key protein in viral infection, and its inhibition has been a target for 2-deoxy-2,3-didehydro-d-N-acetylneuraminic acid (Neu5Ac2en)-based inhibitor development. In this study, we explore the effect of C-5 modifications on the potency of Neu5Ac2en derivatives that target the human parainfluenza type-1 hemagglutinin?neuraminidase protein. Our study demonstrates that the replacement of ...
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    Human parainfluenza virus type 1 is the major cause of croup in infants and young children. There is currently neither vaccine nor clinically effective treatment for parainfluenza virus infection. Hemagglutinin?neuraminidase glycoprotein is a key protein in viral infection, and its inhibition has been a target for 2-deoxy-2,3-didehydro-d-N-acetylneuraminic acid (Neu5Ac2en)-based inhibitor development. In this study, we explore the effect of C-5 modifications on the potency of Neu5Ac2en derivatives that target the human parainfluenza type-1 hemagglutinin?neuraminidase protein. Our study demonstrates that the replacement of the Neu5Ac2en C-5 acetamido moiety with more hydrophobic alkane-based moieties improves the inhibitory potency for both hemagglutinin?neuraminidase functions. These findings shed light on the importance of C-5 substitution on Neu5Ac2en in the design of novel sialic acid-based inhibitors that target human parainfluenza type-1 hemagglutinin?neuraminidase.
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    Journal Title
    Journal of Medicinal Chemistry
    Volume
    57
    Issue
    18
    DOI
    https://doi.org/10.1021/jm500759v
    Copyright Statement
    Self-archiving of the author-manuscript version is not yet supported by this journal. Please refer to the journal link for access to the definitive, published version or contact the authors for more information.
    Subject
    Cheminformatics and Quantitative Structure-Activity Relationships
    Organic Chemical Synthesis
    Virology
    Medicinal and Biomolecular Chemistry
    Organic Chemistry
    Pharmacology and Pharmaceutical Sciences
    Publication URI
    http://hdl.handle.net/10072/65592
    Collection
    • Journal articles

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