Modulation of amyloid-β 1-42 structure and toxicity by proline-rich whey peptides
Date
2013
Authors
Bharadwaj, P.
Head, R.
Martins, R.
Raussens, V.
Sarroukh, R.
Jegasothy, H.
Waddington, L.
Bennett, L.
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Journal article
Citation
Food and Function, 2013; 4(1):92-103
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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.
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Link to a related website: https://dipot.ulb.ac.be/dspace/bitstream/2013/130099/1/2013_Bharadwaj_et_al_Food_and_Function_4_92.pdf, Open Access via Unpaywall
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Copyright 2013 The Royal Society of Chemistry