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Structural characterization of GNNQQNY amyloid fibrils by magic angle spinning NMR
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van der Wel, Patrick C. A., Lewandowski, Józef R. and Griffin, Robert G. (2010) Structural characterization of GNNQQNY amyloid fibrils by magic angle spinning NMR. Biochemistry, Vol.49 (No.44). pp. 9457-9469. doi:10.1021/bi100077x ISSN 0006-2960.
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Official URL: http://dx.doi.org/10.1021/bi100077x
Abstract
Several human diseases are associated with the formation of am bid aggregates. but experimental characterization of these amyloid fibrils and their oligomeric precursors has remained challenging. Experimental and computational analysis of simpler model systems has therefore been necessary, for instance, on the peptide fragment GNNQQNY(7-13) of yeast prion protein Sup35p. Expanding on a previous publication, we report here a detailed structural characterization of GNNQQNY fibrils using magic angle spinning (MAS) NMR. On the basis of additional chemical shift assignments we confirm the coexistence of three distinct peptide conformations within the fibrillar samples, as reflected in substantial chemical shift differences. Backbone torsion angle measurements indicate that the basic structure of these coexisting conformers is an extended beta-sheet. We structurally characterize a previously identified localized distortion of the beta-strand backbone specific to one of the conformers. Intermolecular contacts are consistent with each of the conformers being present in its own parallel and in-register sheet. Overall the M AS NMR data indicate a substantial difference between the structure of the fibrillar and crystalline forms of these peptides, with a clearly increased complexity in the GNNQQNY fibril structure. These experimental data can provide guidance for future work, both experimental and theoretical, and provide insights into the distinction between fibril growth a id Crystal formation.
| Item Type: | Journal Article | ||||
|---|---|---|---|---|---|
| Subjects: | Q Science > QD Chemistry | ||||
| Divisions: | Faculty of Science, Engineering and Medicine > Science > Chemistry | ||||
| Library of Congress Subject Headings (LCSH): | Amyloid -- Structure, Nuclear magnetic resonance spectroscopy, Peptides -- Structure | ||||
| Journal or Publication Title: | Biochemistry | ||||
| Publisher: | American Chemical Society | ||||
| ISSN: | 0006-2960 | ||||
| Official Date: | 9 November 2010 | ||||
| Dates: |
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| Volume: | Vol.49 | ||||
| Number: | No.44 | ||||
| Page Range: | pp. 9457-9469 | ||||
| DOI: | 10.1021/bi100077x | ||||
| Status: | Peer Reviewed | ||||
| Publication Status: | Published | ||||
| Access rights to Published version: | Restricted or Subscription Access | ||||
| Funder: | National Institutes of Health (U.S.) (NIH) | ||||
| Grant number: | EB-003151 (NIH), EB-002026 (NIH) |
Data sourced from Thomson Reuters' Web of Knowledge
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