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    The inhibitory properties of acidic functionalised calix[4]arenes on human papillomavirus pentamer formation

    80321.pdf (484.6Kb)
    Access Status
    Open access
    Authors
    Goh, Ching Yong
    Fu, D.Y.
    Duncan, Caitlin
    Tinker, Adam
    Li, F.
    Mocerino, Mauro
    Ogden, Mark
    Wu, Y.
    Date
    2020
    Type
    Journal Article
    
    Metadata
    Show full item record
    Citation
    Goh, C.Y. and Fu, D.Y. and Duncan, C.L. and Tinker, A. and Li, F. and Mocerino, M. and Ogden, M.I. et al. 2020. The inhibitory properties of acidic functionalised calix[4]arenes on human papillomavirus pentamer formation. Supramolecular Chemistry. 32 (5): pp. 345-353.
    Source Title
    Supramolecular Chemistry
    DOI
    10.1080/10610278.2020.1779930
    ISSN
    1061-0278
    Faculty
    Faculty of Science and Engineering
    School
    School of Molecular and Life Sciences (MLS)
    Remarks

    This is an accepted manuscript of an article published by Taylor & Francis in Supramolecular Chemsitry on 03/07/2020 available online at http://www.tandfonline.com/10.1080/10610278.2020.1779930.

    URI
    http://hdl.handle.net/20.500.11937/80239
    Collection
    • Curtin Research Publications
    Abstract

    © 2020 Informa UK Limited, trading as Taylor & Francis Group. Human Papillomavirus (HPV) is the leading cause of cervical cancer, with only some HPV types prevented with vaccines and no treatments for the viral infection itself. One way to target viral infection is by inhibiting the assembly of the L1 monomer into a pentamer, which forms the viral capsid. Four calix[4]arene compounds functionalised with D- and L-aspartic and glutamic acid and an iminodiacetic functionalised calix[4]arene were synthesised and tested for L1 pentamer formation inhibition. The amino acid functionalised calix[4]arene derivatives showed millimolar inhibition (IC50 = 0.72 to 2.67 mM) of pentamer formation, with little difference between the stereoisomers. The iminodiacetic acid calix[4]arene derivative showed no inhibitory properties, despite sharing structural similarities with the four other calix[4]arenes. Confirmation of binding the negatively charged compounds to the positive residues of the L1 protein was achieved by trypsin digestion. This study is helpful in the development of cost-effective inhibitors to prevent HPV assembly.

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