Document Detail

Modulation of amyloid-β 1-42 structure and toxicity by proline-rich whey peptides.
MedLine Citation:
PMID:  23014463     Owner:  NLM     Status:  Publisher    
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.
Prashant Bharadwaj; Richard Head; Ralph Martins; Vincent Raussens; Rabia Sarroukh; Hema Jegasothy; Lynne Waddington; Louise Bennett
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-9-27
Journal Detail:
Title:  Food & function     Volume:  -     ISSN:  2042-650X     ISO Abbreviation:  Food Funct     Publication Date:  2012 Sep 
Date Detail:
Created Date:  2012-9-27     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101549033     Medline TA:  Food Funct     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
CSIRO Preventative Health Flagship, Material Science and Engineering, 343 Royal Parade, Parkville, Victoria 3052, Australia.
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