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| Item Type: | Article |
|---|---|
| Title: | Mixing Aβ(1-40) and Aβ(1-42) peptides generates unique amyloid fibrils |
| Creators Name: | Cerofolini, L., Ravera, E., Bologna, S., Wiglenda, T., Böddrich, A., Purfürst, B., Benilova, I., Korsak, M., Gallo, G., Rizzo, D., Gonnelli, L., Fragai, M., De Strooper, B., 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 |
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