![[feed]](/style/images/feed-icon-14x14.png){kind=icon}
|
PDF (Original Article)
- Requires a PDF viewer such as GSview, Xpdf or Adobe Acrobat Reader
2MB | |
|
PDF (Supplementary Material)
- Requires a PDF viewer such as GSview, Xpdf or Adobe Acrobat Reader
3MB |
| Item Type: | Article |
|---|---|
| Title: | Mixing Aβ(1-40) and Aβ(1-42) peptides generates unique amyloid fibrils |
| Creators Name: | Cerofolini, L. and Ravera, E. and Bologna, S. and Wiglenda, T. and Böddrich, A. and Purfürst, B. and Benilova, I. and Korsak, M. and Gallo, G. and Rizzo, D. and Gonnelli, L. and Fragai, M. and De Strooper, B. and Wanker, E.E. and Luchinat, C. |
| Abstract: | Recent structural studies show distinct morphologies for the fibrilsof Ab(1-42) and Ab(1-40), which are believed not to co-fibrillize.We describe here a novel, structurally-uniform 1 : 1 mixed fibrillarspecies, which differs from bothpure fibrils. It forms preferen-tially even when Ab(1-42) : Ab(1-40) peptides are mixed in a non-stoichiometric ratio. |
| Keywords: | Amyloid beta-Peptides, Molecular Models, Peptide Fragments, Protein Aggregates, Secondary Protein Structure |
| Source: | Chemical Communications |
| ISSN: | 1359-7345 |
| Publisher: | Royal Society of Chemistry |
| Volume: | 56 |
| Number: | 62 |
| Page Range: | 8830-8833 |
| Date: | 11 August 2020 |
| Official Publication: | https://doi.org/10.1039/d0cc02463e |
| PubMed: | View item in PubMed |
Repository Staff Only: item control page
Download Statistics
Download Statistics
