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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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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

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

Dates:

Date	Event
28 April 2010	Published

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)

References:

(1) Merlini, G.; Bellotti, V. N. Engl. J. Med. 2003, 349, 583–96.
(2) Bjorkman, P. J.; Saper, M. A.; Samraoui, B.; Bennett, W. S.; Strominger,
J. L.; Wiley, D. C. Nature 1987, 329, 506–12.
(3) Chatani, E.; Goto, Y. Biochim. Biophys. Acta 2005, 1753, 64–75.
(4) Kad, N. M.; Myers, S. L.; Smith, D. P.; Smith, D. A.; Radford, S. E.;
Thomson, N. H. J. Mol. Biol. 2003, 330, 785–97.
(5) Yamaguchi, K.; Naiki, H.; Goto, Y. J. Mol. Biol. 2006, 363, 279–88.
(6) Jahn, T. R.; Tennent, G. A.; Radford, S. E. J. Biol. Chem. 2008, 283, 17279–86.
(7) White, H. E.; Hodgkinson, J. L.; Jahn, T. R.; Cohen-Krausz, S.; Gosal,
W. S.; Muller, S.; Orlova, E. V.; Radford, S. E.; Saibil, H. R. J. Mol. Biol.
2009, 389, 48–57.
(8) (a) Kad, N. M.; Thomson, N. H.; Smith, D. P.; Smith, D. A.; Radford, S. E.
J. Mol. Biol. 2001, 313, 559–71. (b) Relini, A.; Canale, C.; De Stefano, S.;
Rolandi, R.; Giorgetti, S.; Stoppini, M.; Rossi, A.; Fogolari, F.; Corazza, A.;
Esposito, G.; Gliozzi, A.; Bellotti, V. J. Biol. Chem. 2006, 281, 16521–9.
(9) (a) McDermott, A. E. Curr. Opin. Struct. Biol. 2004, 14, 554–61. (b) Lange,
A.; Giller, K.; Hornig, S.; Martin-Eauclaire, M. F.; Pongs, O.; Becker, S.;
Baldus, M. Nature 2006, 440, 959–62. (c) Bo¨ckmann, A. Angew. Chem.,
Int. Ed. 2008, 47, 6110–3.
(10) (a) Heise, H.; Hoyer, W.; Becker, S.; Andronesi, O. C.; Riedel, D.; Baldus,
M. Proc. Natl. Acad. Sci. U.S.A. 2005, 102, 15871–6. (b) Petkova, A. T.;
Leapman, R. D.; Guo, Z.; Yau, W. M.; Mattson, M. P.; Tycko, R. Science
2005, 307, 262–5. (c) van der Wel, P. C.; Lewandowski, J. R.; Griffin,
R. G. J. Am. Chem. Soc. 2007, 129, 5117–30. (d) Heise, H. ChemBioChem
2008, 9, 179–189. (e) Wasmer, C.; Lange, A.; Van Melckebeke, H.; Siemer,
A. B.; Riek, R.; Meier, B. H. Science 2008, 319, 1523–6. (f) Loquet, A.;
Bousset, L.; Gardiennet, C.; Sourigues, Y.; Wasmer, C.; Habenstein, B.;
Schutz, A.; Meier, B. H.; Melki, R.; Böckmann, A. J. Mol. Biol. 2009,
394, 108–18.
(11) Iwata, K.; Fujiwara, T.; Matsuki, Y.; Akutsu, H.; Takahashi, S.; Naiki, H.;
Goto, Y. Proc. Natl. Acad. Sci. U.S.A. 2006, 103, 18119–24.
(12) Katou, H.; Kanno, T.; Hoshino, M.; Hagihara, Y.; Tanaka, H.; Kawai, T.;
Hasegawa, K.; Naiki, H.; Goto, Y. Protein Sci. 2002, 11, 2218–29.
(13) Sarkar, S. K.; Torchia, D. A.; Kopple, K. D.; Vanderhart, D. L. J. Am.
Chem. Soc. 1984, 106, 3328–3331.
(14) Hoshino, M.; Katou, H.; Hagihara, Y.; Hasegawa, K.; Naiki, H.; Goto, Y.
Nat. Struct. Biol. 2002, 9, 332–6.
(15) Kameda, A.; Morita, E. H.; Sakurai, K.; Naiki, H.; Goto, Y. Protein Sci.
2009, 18, 1592–601.
(16) (a) Kameda, A.; Hoshino, M.; Higurashi, T.; Takahashi, S.; Naiki, H.; Goto,
Y. J. Mol. Biol. 2005, 348, 383–97. (b) Eakin, C. M.; Berman, A. J.; Miranker,
A. D. Nat. Struct. Mol. Biol. 2006, 13, 202–8. (c) Jahn, T. R.; Parker, M. J.;
Homans, S. W.; Radford, S. E. Nat. Struct. Mol. Biol. 2006, 13, 195–201. (d)
Eichner, T.; Radford, S. E. J. Mol. Biol. 2009, 386, 1312–26.
(17) Myers, S. L.; Jones, S.; Jahn, T. R.; Morten, I. J.; Tennent, G. A.; Hewitt,
E. W.; Radford, S. E. Biochemistry 2006, 45, 2311–21.