Quenched hydrogen-deuterium exchange NMR of a disease-relevant Aß(1-42) amyloid polymorph
- Author(s)
- M. A. Waelti, J. Orts, R. Riek
- Abstract
Alzheimer’s disease is associated with the aggregation into amyloid fibrils of Aβ(1–42) and Aβ(1–40) peptides. Interestingly, these fibrils often do not obtain one single structure but rather show different morphologies, so-called polymorphs. Here, we compare quenched hydrogen-deuterium (H/D) exchange of a disease-relevant Aβ(1–42) fibril for which the 3D structure has been determined by solid-state NMR with H/D exchange previously determined on another structural polymorph. This comparison reveals secondary structural differences between the two polymorphs suggesting that the two polymorphisms can be classified as segmental polymorphs.
- Organisation(s)
- External organisation(s)
- Eidgenössische Technische Hochschule Zürich
- Journal
- PLoS ONE
- Volume
- 12
- No. of pages
- 11
- ISSN
- 1932-6203
- DOI
- https://doi.org/10.1371/journal.pone.0172862
- Publication date
- 03-2017
- Peer reviewed
- Yes
- Austrian Fields of Science 2012
- 106006 Biophysics, 106002 Biochemistry
- Keywords
- ASJC Scopus subject areas
- General Agricultural and Biological Sciences, General, General Biochemistry,Genetics and Molecular Biology
- Portal url
- https://ucrisportal.univie.ac.at/en/publications/ccba117e-8ce4-4640-b2f4-ef6394316ba0