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Issue 1, 2013
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Modulation of amyloid-β 1-42 structure and toxicity by proline-rich whey peptides

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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 (Aβ42) 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 β-sheet and specifically, anti-parallel β-sheet structures by wPRP was demonstrated by ATR-FTIR spectroscopy, where evidence for capacity of wPRP to dissociate pre-existing β-sheet structures in Aβ42 was also apparent. Suppression of anti-parallel β-sheets of oligomeric Aβ42 was associated with rescue of yeast and SH-SY5Y neuronal cells providing important evidence for the association between anti-parallel β-sheet structure and oligomer toxicity. It was proposed that the interaction of wPRP with Aβ42 interfered with the anti-parallel folding pathway of oligomeric Aβ42 and ultimately produced ‘off-pathway’ structures of lowered total β-sheet content, with attenuated cellular toxicity.

Graphical abstract: Modulation of amyloid-β 1-42 structure and toxicity by proline-rich whey peptides

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Publication details

The article was received on 18 May 2012, accepted on 05 Sep 2012 and first published on 07 Sep 2012


Article type: Paper
DOI: 10.1039/C2FO30111C
Citation: Food Funct., 2013,4, 92-103
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    Modulation of amyloid-β 1-42 structure and toxicity by proline-rich whey peptides

    P. Bharadwaj, R. Head, R. Martins, V. Raussens, R. Sarroukh, H. Jegasothy, L. Waddington and L. Bennett, Food Funct., 2013, 4, 92
    DOI: 10.1039/C2FO30111C

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