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Microscale structural model of Alzheimer Abeta(1–40) amyloid fibril

Appl. Phys. Lett. 94, 243904 (2009); doi:10.1063/1.3148641

Published 16 June 2009

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Raffaella Paparcone and Markus J. Buehler
Department of Civil and Environmental Engineering, Laboratory for Atomistic and Molecular Mechanics, Massachusetts Institute of Technology, 77 Massachusetts Ave. Room 1-235A&B, Cambridge, Massachusetts 02139, USA
Amyloid fibril formation and characterization are crucial due to their association with severe degenerative disorders such as Alzheimer's, type II diabetes, and Parkinson's disease. Here we present an atomistic-based multiscale analysis, utilized to predict the structure of Alzheimer Abeta(1–40) fibrils. Our study provides a structural model of amyloid fibers with lengths of hundreds of nanometers at atomistic resolution. We report a systematic analysis of the energies, structural changes and H-bonding for varying fibril lengths, elucidating their size dependent properties. Our model predicts the formation of twisted amyloid microfibers with a periodicity of [approximate]82 nm, in close agreement with experimental results. ©2009 American Institute of Physics
History: Received 29 April 2009; accepted 12 May 2009; published 16 June 2009
Permalink: http://link.aip.org/link/?APPLAB/94/243904/1
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KEYWORDS and PACS

Keywords
PACS
  • 87.15.B-
    Structure of biomolecules
  • 87.15.hp
    Conformational changes of biomolecules
  • 87.15.Fh
    Bonding of biomolecules; mechanisms of bond breakage
  • 87.14.E-
    Proteins
  • YEAR: 2009

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PUBLICATION DATA

ISSN:
0003-6951 (print)   1077-3118 (online)
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REFERENCES (19)
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  1. M. Fandrich, M. A. Fletcher, and C. M. Dobson, Nature (London) 410, 165 (2001)
  2. C. M. Dobson, ibid. 426, 884 (2003).
  3. M. J. Buehler and Y. C. Yung, Nature Mater. 8, 175 (2009).
  4. R. Nelson, M. R. Sawaya, M. Balbirnie, A. O. Madsen, C. Riekel, R. Grothe, and D. Eisenberg, Nature (London) 435, 773 (2005).
  5. A. T. Petkova, Y. Ishii, J. J. Balbach, O. N. Anzutkin, R. D. Leapman, F. Delaglio, and R. Tycko, Proc. Natl. Acad. Sci. U.S.A. 99, 16742 (2002).
  6. C. P. Jaroniec, C. E. MacPhee, N. S. Astrof, C. M. Dobson, and R. G. Griffin, Proc. Natl. Acad. Sci. U.S.A. 99, 16748 (2002).
  7. A. Paravastu, R. D. Leapman, W. -M. Yau, and R. Tycko, Proc. Natl. Acad. Sci. U.S.A. 105, 18349 (2008).
  8. D. M. Fowler, A. V. Koulov, W. E. Balch, and J. W. Kelly, Trends Biochem. Sci. 32, 217 (2007)
  9. F. Chiti and C. M. Dobson, Annu. Rev. Biochem. 75, 333 (2006).
  10. B. R. Brooks, R. E. Bruccoleri, B. D. Olafson, D. J. States, S. Swaminathan, and M. Karplus, J. Comput. Chem. 4, 187 (1983)
  11. T. Lazaridis and M. Karplus, Proteins: Struct., Funct., Genet. 35, 133 (1999).
  12. C. Chothia, J. Mol. Biol. 75, 295 (1973).
  13. F. R. Salemme, Prog. Biophys. Mol. Biol. 42, 95 (1983).
  14. P. H. Maccallum, R. Poet, and E. J. Milner-White, J. Mol. Biol. 248, 374 (1995)
  15. K. C. Chou, G. Nemethy, and H. A. Scheraga, ibid. 168, 389 (1983).
  16. A. S. Yang and B. Honig, J. Mol. Biol. 252, 366 (1995)
  17. L. Wang, T. Oconnell, A. Tropsha, and J. Hermans, ibid. 262, 283 (1996).
  18. E. Koh and T. Kim, Proteins 61, 559 (2005).
  19. X. Periole, A. Rampioni, M. Vendruscolo, and A. E. Mark, J. Phys. Chem. B 113, 1728 (2009).
  20. S. Keten and M. J. Buehler, Nano Lett. 8, 743 (2008)
  21. Phys. Rev. E 78, 061913 (2008)
    22. Phys. Rev. Lett. 100, 198301 (2008).
  22. PDB files of the microscale amyloid fibrils are available from the authors upon request.
  23. S. Kumar and P. R. LeDuc, Exp. Mech. 49, 11 (2009).
  24. R. Tycko, Biochemistry 42, 3151 (2003)
  25. O. N. Antzutkin, J. J. Balbach, R. D. Leapman, N. W. Rizzo, J. Reed, and R. Tycko, Proc. Natl. Acad. Sci. U.S.A. 97, 13045 (2000).

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