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Published online before print November 10, 2004, 10.1110/ps.041024904
Protein Science (2004), 13:3314-3321. Published by Cold Spring Harbor Laboratory Press. Copyright © 2004 The Protein Society
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FTIR reveals structural differences between native {beta}-sheet proteins and amyloid fibrils

Giorgia Zandomeneghi1, Mark R.H. Krebs2, Margaret G. McCammon3 and Marcus Fändrich1

1 Institut für Molekulare Biotechnologie (IMB), D-07745 Jena, Germany
2 Polymers and Colloids (P&C) Group, Cavendish Laboratory, and 3 Department of Chemistry, University of Cambridge, Cambridge, United Kingdom

(RECEIVED July 30, 2004; FINAL REVISION August 26, 2004; ACCEPTED August 26, 2004)

The presence of {beta}-sheets in the core of amyloid fibrils raised questions as to whether or not {beta}-sheet-containing proteins, such as transthyretin, are predisposed to form such fibrils. However, we show here that the molecular structure of amyloid fibrils differs more generally from the {beta}-sheets in native proteins. This difference is evident from the amide I region of the infrared spectrum and relates to the distribution of the {phi}/{psi} dihedral angles within the Ramachandran plot, the average number of strands per sheet, and possibly, the {beta}-sheet twist. These data imply that amyloid fibril formation from native {beta}-sheet proteins can involve a substantial structural reorganization.

Keywords: protein structure/folding; prions; aggregation; amyloid; conformational disease; infrared spectroscopy

Abbreviations: TTR, transthyretin • FTIR, fourier-transformed infrared • NMR, Nuclear Magnetic Resonance • EM, Electron Microscopy

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.041024904.

Reprint requests to Marcus Fändrich, Institut für Molekulare Biotechnologie (IMB), Beutenbergstraße 11, D-07745 Jena, Germany; e-mail: fandrich{at}imb-jena.de; fax: +49-3641-656310.


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