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Fibrillar vs crystalline full-length β-2-microglobulin studied by high-resolution solid-state NMR spectroscopy
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Barbet-Massin, Emeline, Ricagno, Stefano, Lewandowski, Józef R., Giorgetti, Sofia, Bellotti, Vittorio, Bolognesi, Martino, Emsley, Lyndon and Pintacuda, Guido (2010) Fibrillar vs crystalline full-length β-2-microglobulin studied by high-resolution solid-state NMR spectroscopy. Journal of the American Chemical Society, Vol.132 (No.16). pp. 5556-5557. doi:10.1021/ja1002839
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Official URL: http://dx.doi.org/10.1021/ja1002839
Abstract
Elucidating the fine structure of amyloid fibrils as well as understanding their processes of nucleation and growth remains a difficult yet essential challenge, directly linked to our current poor insight into protein misfolding and aggregation diseases. Here we consider beta-2-microglobulin (beta 2m), the MHC-1 light chain component responsible for dialysis-related amyloidosis, which can give rise to amyloid fibrils in vitro under various experimental conditions, including low and neutral pH. We have used solid-state NMR to probe the structural features of fibrils formed by full-length beta 2m (99 residues) at pH 2.5 and pH 7.4. A close comparison of 2D (13)C-(13)C and (15)N-(13)C correlation experiments performed on beta 2m, in both the crystalline and fibrillar states, suggests that, in spite of structural changes affecting the protein loops linking the protein B-strands, the protein chain retains a substantial share of its native secondary structure in the fibril assembly. Moreover, variations in the chemical shifts of the key Pro32 residue suggest the involvement of a cis-trans isomerization in the process of beta 2m fibril formation. Lastly, the analogy of the spectra recorded on beta 2m fibrils grown at different pH values hints at a conserved architecture of the amyloid species thus obtained.
| Item Type: | Journal Article | ||||
|---|---|---|---|---|---|
| Subjects: | Q Science > QD Chemistry Q Science > QP Physiology |
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| Divisions: | Faculty of Science, Engineering and Medicine > Science > Chemistry | ||||
| Library of Congress Subject Headings (LCSH): | Amyloid -- Structure, Nuclear magnetic resonance spectroscopy, Solid state chemistry, Globulins | ||||
| Journal or Publication Title: | Journal of the American Chemical Society | ||||
| Publisher: | American Chemical Society | ||||
| ISSN: | 0002-7863 | ||||
| Official Date: | 28 April 2010 | ||||
| Dates: |
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| Volume: | Vol.132 | ||||
| Number: | No.16 | ||||
| Page Range: | pp. 5556-5557 | ||||
| DOI: | 10.1021/ja1002839 | ||||
| Status: | Peer Reviewed | ||||
| Publication Status: | Published | ||||
| Access rights to Published version: | Restricted or Subscription Access | ||||
| Funder: | France. Agence nationale de la recherche (ANR), Fondazione Cassa di risparmio delle provincie lombarde, Sixth Framework Programme (European Commission) (FP6), European Union (EU) | ||||
| Grant number: | ANR 08-BLAN-0035-01 (ANR), 2007-5151 (FC), RII3-026145 (FP6), PIRG03-GA-2008-231026 (EU) |
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