Modulation of amyloid-ß 1-42 structure and toxicity by proline-rich whey peptides
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 change...
| Main Authors: | , , , , , , , |
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| Format: | Journal Article |
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2013
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| Online Access: | http://hdl.handle.net/20.500.11937/25238 |
| _version_ | 1848751653152358400 |
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| author | Bharadwaj, Prashant Head, R. Martins, R. Raussens, V. Sarroukh, R. Jegasothy, H. Waddington, L. Bennett, L. |
| author_facet | Bharadwaj, Prashant Head, R. Martins, R. Raussens, V. Sarroukh, R. Jegasothy, H. Waddington, L. Bennett, L. |
| author_sort | Bharadwaj, Prashant |
| building | Curtin Institutional Repository |
| collection | Online Access |
| description | 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. |
| first_indexed | 2025-11-14T07:56:08Z |
| format | Journal Article |
| id | curtin-20.500.11937-25238 |
| institution | Curtin University Malaysia |
| institution_category | Local University |
| last_indexed | 2025-11-14T07:56:08Z |
| publishDate | 2013 |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | curtin-20.500.11937-252382018-03-29T09:08:51Z Modulation of amyloid-ß 1-42 structure and toxicity by proline-rich whey peptides Bharadwaj, Prashant Head, R. Martins, R. Raussens, V. Sarroukh, R. Jegasothy, H. Waddington, L. Bennett, L. 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. 2013 Journal Article http://hdl.handle.net/20.500.11937/25238 10.1039/c2fo30111c restricted |
| spellingShingle | Bharadwaj, Prashant Head, R. Martins, R. Raussens, V. Sarroukh, R. Jegasothy, H. Waddington, L. Bennett, L. Modulation of amyloid-ß 1-42 structure and toxicity by proline-rich whey peptides |
| title | Modulation of amyloid-ß 1-42 structure and toxicity by proline-rich whey peptides |
| title_full | Modulation of amyloid-ß 1-42 structure and toxicity by proline-rich whey peptides |
| title_fullStr | Modulation of amyloid-ß 1-42 structure and toxicity by proline-rich whey peptides |
| title_full_unstemmed | Modulation of amyloid-ß 1-42 structure and toxicity by proline-rich whey peptides |
| title_short | Modulation of amyloid-ß 1-42 structure and toxicity by proline-rich whey peptides |
| title_sort | modulation of amyloid-ß 1-42 structure and toxicity by proline-rich whey peptides |
| url | http://hdl.handle.net/20.500.11937/25238 |