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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. ISSN 0002-7863

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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
Divisions: Faculty of 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
Volume: Vol.132
Number: No.16
Page Range: pp. 5556-5557
Identification Number: 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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URI: http://wrap.warwick.ac.uk/id/eprint/40593

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