Mixing Aβ(1–40) and Aβ(1–42) peptides generates unique amyloid fibrils

Author:

Cerofolini Linda1234ORCID,Ravera Enrico12345ORCID,Bologna Sara12345ORCID,Wiglenda Thomas6789ORCID,Böddrich Annett6789ORCID,Purfürst Bettina101189ORCID,Benilova Iryna121314ORCID,Korsak Magdalena15164,Gallo Gianluca12345ORCID,Rizzo Domenico12345ORCID,Gonnelli Leonardo12345ORCID,Fragai Marco12345ORCID,De Strooper Bart1213141718ORCID,Wanker Erich E.6789ORCID,Luchinat Claudio12345ORCID

Affiliation:

1. Magnetic Resonance Center (CERM)

2. University of Florence and Interuniversity Consortium for Magnetic Resonance of Metalloproteins (CIRMMP)

3. Sesto Fiorentino (FI)

4. Italy

5. Department of Chemistry “Ugo Schiff”

6. Neuroproteomics

7. Max Delbrück Center for Molecular Medicine

8. 13125 Berlin

9. Germany

10. Core Facility Electron Microscopy

11. Max-Delbrück Center for Molecular Medicine

12. VIB Center for Brain and Disease Research

13. 3000 Leuven

14. Belgium

15. Giotto Biotech S.R.L.

16. 50019 Sesto Fiorentino (FI)

17. KULeuven

18. Department of Neurology

Abstract

Solid-state NMR experiments reveal that the two isoforms of the beta-amyloid peptide (Aβ(1–40) and Aβ(1–42)) are able to form unique interlaced mixed fibrils.

Funder

Fonds Wetenschappelijk Onderzoek

Ministero della Salute

Bundesministerium für Bildung und Forschung

Helmholtz Association

European Commission

Ministero dell'Istruzione, dell'Università e della Ricerca

Publisher

Royal Society of Chemistry (RSC)

Subject

Materials Chemistry,Metals and Alloys,Surfaces, Coatings and Films,General Chemistry,Ceramics and Composites,Electronic, Optical and Magnetic Materials,Catalysis

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