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    A phosphorylation-induced turn defines the Alzheimer's disease AT8 antibody epitope on the tau protein

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    Fulltext not available
    Authors
    Gandhi, Neha
    Landrieu, I.
    Byrne, C.
    Kukic, P.
    Amniai, L.
    Cantrelle, F.
    Wieruszeski, J.
    Mancera, Ricardo
    Jacquot, Y.
    Lippens, G.
    Date
    2015
    Type
    Journal Article
    
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    Citation
    Gandhi, N. and Landrieu, I. and Byrne, C. and Kukic, P. and Amniai, L. and Cantrelle, F. and Wieruszeski, J. et al. 2015. A phosphorylation-induced turn defines the Alzheimer's disease AT8 antibody epitope on the tau protein. Angewandte Chemie - International Edition. 54 (23): pp. 6819-6823.
    Source Title
    Angewandte Chemie - International Edition
    DOI
    10.1002/anie.201501898
    ISSN
    1433-7851
    School
    School of Biomedical Sciences
    URI
    http://hdl.handle.net/20.500.11937/8408
    Collection
    • Curtin Research Publications
    Abstract

    Post mortem biochemical staging of Alzheimer’s disease is currently based on immunochemical analysis of brain slices with the AT8 antibody. The epitope of AT8 is described around the pSer202/pThr205 region of the hyperphosphorylated form of the neuronal protein tau. In this study, NMR spectroscopy was used to precisely map the AT8 epitope on phosphorylated tau, and derive its defining structural features by a combination of NMR analyses and molecular dynamics. A particular turn conformation is stabilized by a hydrogen bond of the phosphorylated Thr205 residue to the amide proton of Gly207, and is further stabilized by the two Arg residues opposing the pSer202/pThr205.

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