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| Item Type: | Article |
|---|---|
| Title: | Mixing Aβ(1-40) and Aβ(1-42) peptides generates unique amyloid fibrils |
| Creators: |
Cerofolini, L.  ORCID: https://orcid.org/0000-0002-0795-9594, Ravera, E. ORCID: https://orcid.org/0000-0001-7708-9208, Bologna, S. ORCID: https://orcid.org/0000-0002-2709-8322, Wiglenda, T. ORCID: https://orcid.org/0000-0002-8460-9459, Böddrich, A. ORCID: https://orcid.org/0000-0001-9118-050X, Purfürst, B. ORCID: https://orcid.org/0000-0002-9887-7577, Benilova, I. ORCID: https://orcid.org/0000-0001-7159-5820, Korsak, M., Gallo, G. ORCID: https://orcid.org/0000-0001-6956-3686, Rizzo, D. ORCID: https://orcid.org/0000-0001-7843-3509, Gonnelli, L. ORCID: https://orcid.org/0000-0002-0765-6614, Fragai, M. ORCID: https://orcid.org/0000-0002-8440-1690, De Strooper, B. ORCID: https://orcid.org/0000-0001-5455-5819, Wanker, E.E. ORCID: https://orcid.org/0000-0001-8072-1630 and Luchinat, C. ORCID: https://orcid.org/0000-0003-2271-8921
|
| 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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