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    Modulation of amyloid-ß 1-42 structure and toxicity by proline-rich whey peptides

    Access Status
    Fulltext not available
    Authors
    Bharadwaj, Prashant
    Head, R.
    Martins, R.
    Raussens, V.
    Sarroukh, R.
    Jegasothy, H.
    Waddington, L.
    Bennett, L.
    Date
    2013
    Type
    Journal Article
    
    Metadata
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    Citation
    Bharadwaj, P. and Head, R. and Martins, R. and Raussens, V. and Sarroukh, R. and Jegasothy, H. and Waddington, L. et al. 2013. Modulation of amyloid-ß 1-42 structure and toxicity by proline-rich whey peptides. Food and Function. 4 (1): pp. 92-103.
    Source Title
    Food and Function
    DOI
    10.1039/c2fo30111c
    ISSN
    2042-6496
    School
    School of Biomedical Sciences
    URI
    http://hdl.handle.net/20.500.11937/25238
    Collection
    • Curtin Research Publications
    Abstract

    A proline-rich peptide product prepared from bovine whey protein that was enriched in several hydrophobic amino acids including proline (whey proline-rich peptide, wPRP) was shown to modulate the folding pathway of human amyloid beta peptide 1-42 (Aß42) into oligomers. Concentration-dependent changes in ThT-binding to Ab42 by wPRP indicated suppression of oligomerisation, that was supported by Transmission Electron Microscopy. Suppression of ß-sheet and specifically, anti-parallel ß-sheet structures by wPRP was demonstrated by ATR-FTIR spectroscopy, where evidence for capacity of wPRP to dissociate pre-existing ß-sheet structures in Aß42 was also apparent. Suppression of anti-parallel ß-sheets of oligomeric Aß42 was associated with rescue of yeast and SH-SY5Y neuronal cells providing important evidence for the association between anti-parallel ß-sheet structure and oligomer toxicity. It was proposed that the interaction of wPRP with Aß42 interfered with the anti-parallel folding pathway of oligomeric Aß42 and ultimately produced 'off-pathway' structures of lowered total ß-sheet content, with attenuated cellular toxicity. © 2013 The Royal Society of Chemistry.

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