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  • O-GlcNAcylation of truncated NAC segment alters peptide-dependent effects on α-synuclein aggregation

    Thumbnail
    Author(s)
    Ryan, Philip
    Xu, Ming-Ming
    Davey, Andrew K
    Kassiou, Michael
    Mellick, George D
    Rudrawar, Santosh
    Griffith University Author(s)
    Davey, Andrew
    Ryan, Philip
    Rudrawar, Santosh
    Mellick, George
    Xu, Manny
    Year published
    2019
    Metadata
    Show full item record
    Abstract
    Numerous post-translational modifications (PTMs) of the Parkinson’s disease (PD) associated α-synuclein (α-syn) protein have been recognised to play critical roles in disease aetiology. Indeed, dysregulated phosphorylation and proteolysis are thought to modulate α-syn aggregation and disease progression. Among the PTMs, enzymatic glycosylation with N-acetylglucosamine (GlcNAc) onto the protein’s hydroxylated amino acid residues is reported to deliver protective effects against its pathogenic processing. This modification has been reported to alter its pathogenic self-assembly. As such, manipulation of the protein’s O-GlcNAcylation ...
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    Numerous post-translational modifications (PTMs) of the Parkinson’s disease (PD) associated α-synuclein (α-syn) protein have been recognised to play critical roles in disease aetiology. Indeed, dysregulated phosphorylation and proteolysis are thought to modulate α-syn aggregation and disease progression. Among the PTMs, enzymatic glycosylation with N-acetylglucosamine (GlcNAc) onto the protein’s hydroxylated amino acid residues is reported to deliver protective effects against its pathogenic processing. This modification has been reported to alter its pathogenic self-assembly. As such, manipulation of the protein’s O-GlcNAcylation status has been proposed to offer a PD therapeutic route. However, targeting upstream cellular processes can lead to mechanism-based toxicity as the enzymes governing O-GlcNAc cycling modify thousands of acceptor substrates. Small glycopeptides that couple the protective effects of O-GlcNAc with the selectivity of recognition sequences may prove useful tools to modulate protein aggregation. Here we discuss efforts to probe the effects of various O-GlcNAc modified peptides on wild-type α-synuclein aggregation.
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    Journal Title
    Bioorganic Chemistry
    DOI
    https://doi.org/10.1016/j.bioorg.2019.103389
    Note
    This publication has been entered into Griffith Research Online as an Advanced Online Version.
    Subject
    Medicinal and Biomolecular Chemistry
    Medicinal and Biomolecular Chemistry
    Medicinal and Biomolecular Chemistry
    Organic Chemistry
    O-GlcNAcylation
    Parkinson’s disease
    α-Synuclein aggregation
    Neurodegenerative diseases
    Publication URI
    http://hdl.handle.net/10072/389426
    Collection
    • Journal articles

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