Polymorphism in an amyloid-like fibril-forming model peptide

Angewandte Chemie - International Edition

Volumn 47, Issue 31, 2008, Pages 5842-5845

  Verel, René ^a   Tomka, Ivan T ^a   Bertozzi, Carlo ^a   Cadalbert, Riccardo ^a   Kammerer, Richard A ^b   Steinmetz, Michel O ^c   Meier, Beat H ^a  

^a ETH ZURICH   (Switzerland)

^b UNIVERSITY OF MANCHESTER   (United Kingdom)

^c PAUL SCHERRER INSTITUTE   (Switzerland)

Author keywords

Fibrils; NMR spectroscopy; Peptides; Protein structures; Structural biology

Indexed keywords

FIBRILS; NMR SPECTROSCOPY; PEPTIDES; PROTEIN STRUCTURES; STRUCTURAL BIOLOGY;

AMINES; GLYCOPROTEINS; HYDROGEN; NUCLEAR MAGNETIC RESONANCE; POLYMORPHISM;

NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;

AMYLOID; PEPTIDE;

ARTICLE; CHEMICAL MODEL; CHEMISTRY; METHODOLOGY; NUCLEAR MAGNETIC RESONANCE;

AMYLOID; MODELS, CHEMICAL; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDES;

EID: 53549096811     PISSN: 14337851     EISSN: None     Source Type: Journal    
DOI: 10.1002/anie.200800021     Document Type: Article

References (26)

1. F. Chiti, C. M. Dobson, Annu. Rev. Biochem. 2006, 75, 333.
2. C. M. Dobson, Nature 2003, 426, 884.
3. U. Baxa, T. Cassese, A. V. Kajava, A. C. Steven, J. M. S. Andrey Kajava, A. D. P. David in Advances in Protein Chemistry, Vol. 73, Academic Press, 2006, p. 125.
4. R. Morales, K. Abid, C. Soto, Biochim. Biophys. Acta Mol. Basis Dis. 2007, 1772, 681.
5. B. H. Toyama, M. J. S. Kelly, J. D. Gross, J. S. Weissman, Nature 2007, 449, 233.
6. A. K. Paravastu, A. T. Petkova, R. Tycko, Biophys. J. 2006, 90, 4618.
7. A. T. Petkova, R. D. Leapman, Z. Guo, W.-M. Yau, M. P. Mattson, R. Tycko, Science 2005, 307, 262.
8. P. C. A. van der Wel, J. R. Lewandowski, R. G. Griffin, J. Am. Chem. Soc. 2007, 129, 5117.
9. O. N. Antzutkin, R. D. Leapman, J. J. Balbach, R. Tycko, Biochemistry 2002, 41, 15436.
10. A. T. Petkova, G. Buntkowsky, F. Dyda, R. D. Leapman, W. M. Yau, R. Tycko, J. Mol. Biol. 2004, 335, 247.
11. R. A. Kammerer, D. Kostrewa, J. Zurdo, A. Detken, C. Garcia-Echeverria, J. D. Green, S. A. Muller, B. H. Meier, F. K. Winkler, C. M. Dobson, M. O. Steinmetz, Proc. Natl. Acad. Sci. USA 2004, 101, 4435.
12. R. A. Kammerer, M. O. Steinmetz, J. Struct. Biol. 2006, 155, 146.
13. M. Sunde, L. C. Serpell, M. Bartlam, P. E. Fraser, M. B. Pepys, C. C. F. Blake, J. Mol. Biol. 1997, 273, 729.
14. M. O. Steinmetz, C. García-Echeverría, R. A. Kammerer, Int. J. Pept. Res. Ther. 2005, 11, 43.
15. M. O. Steinmetz, Z. Gattin, R. Verel, B. Ciani, T. Stromer, J. M. Green, P. Tittmann, C. Schulze-Briese, H. Gross, W. F. van Gunsteren, B. H. Meier, L. C. Serpell, S. A. Muller, R. A. Kammerer, J. Mol. Biol. 2008, 376, 898.
16. T. Gullion, J. Schaefer, J. Magn. Reson. 1989, 81, 196.
17. T. Gullion, J. Schaefer, Adv. Magn. Reson. 1989, 13, 57.
18. A. Detken, R. Verel, B. Bianchi, C. García-Echeverría, R. A. Kammerer, M. O. Steinmetz, B. H. Meier, unpublished results.
19. M. R. Sawaya, S. Sambashivan, R. Nelson, M. I. Ivanova, S. A. Sievers, M. I. Apostol, M. J. Thompson, M. Balbirnie, J. J. W. Wiltzius, H. T. McFarlane, A. O. Madsen, C. Riekel, D. Eisenberg, Nature 2007, 447, 453.
20. J. J. Balbach, Y. Ishii, O. N. Antzutkin, R. D. Leapman, N. W. Rizzo, F. Dyda, J. Reed, R. Tycko, Biochemistry 2000, 39, 13748.
21. R. Tycko, Y. Ishii, J. Am. Chem. Soc. 2003, 125, 6606.
22. T. Gullion, D. B. Baker, M. S. Conradi, J. Magn. Reson. 1990, 89, 479.
23. S. A. Smith, T. O. Levante, B. H. Meier, R. R. Ernst, J. Magn. Reson. Ser. A 1994, 106, 75.
24. P. Güntert, C. Mumenthaler, K. Wüthrich, J. Mol. Biol. 1997, 273, 283.
25. W. Humphrey, A. Dalke, K. Schulten, J. Molec. Graphics 1996, 14, 33.
26. The nomenclature of the register is relative to an in-register antiparallel β sheet. The sign of the shift gives the direction in which the neighboring β strands are offset. This is based on the fact that the sum of the position number of two residues which are aligned on neighboring β strands in an antiparallel β sheet are a constant for any given β sheet register. For example, the in-register antiparallel β sheet of ccβ gives a sum of 18 (Ser1 is aligned with Gly17, Ile2 aligned with Ile16, etc.). The +3-or gives a sum of 21 (e.g. Ala7 aligned with Leu14), 18 + 3 = 21. The -2-or gives a sum of 18-2 = 16 (e.g. Ile2 aligned with Leu14). Incidentally, this also indicates which residues form hydrogen bonds and which are outside of the aligned region. For example, in the +3-or, Ser1 cannot be aligned, because to reach a sum of 21 it would need a residue 20, which does not exist.