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J. Biol. Chem., Vol. 280, Issue 4, 2481-2490, January 28, 2005

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Amyloid Fibril Formation from Sequences of a Natural -Structured Fibrous Protein, the Adenovirus Fiber^*

Katerina Papanikolopoulou, Guy Schoehn¶, Vincent Forge||, V. Trevor Forsyth**, Christian Riekel, Jean-François Hernandez¶¶, Rob W. H. Ruigrok¶, and Anna Mitraki||||

From the Institut de Biologie Structurale, UMR 5075, CEA-CNRS-UJF, 41 Rue Jules Horowitz, 38027 Grenoble, European Molecular Biology Laboratory, 6 Rue Jules Horowitz, 38042 Grenoble, ^||Laboratoire de Biophysique Moléculaire et Cellulaire, Unité Mixte de Recherche 5090, Département Réponse et Dynamique Cellulaires, CEA-Grenoble, 17 Rue des Martyrs, 38054 Grenoble Cedex 9, ^**Institut Laue-Langevin, 6 Rue Jules Horowitz, 38042 Grenoble, France, Lennard-Jones Laboratories, School of Chemistry and Physics, Keele University, Staffordshire ST5 5BG, United Kingdom, European Synchrotron Radiation Facility, 6 Rue Jules Horowitz, 38042 Grenoble, France, and ^¶Laboratoire de Virologie Moléculaire et Structurale, EA 2939, Université Joseph Fourier, Grenoble 1, France

Amyloid fibrils are fibrous -structures that derive from abnormal folding and assembly of peptides and proteins. Despite a wealth of structural studies on amyloids, the nature of the amyloid structure remains elusive; possible connections to natural, -structured fibrous motifs have been suggested. In this work we focus on understanding amyloid structure and formation from sequences of a natural, -structured fibrous protein. We show that short peptides (25 to 6 amino acids) corresponding to repetitive sequences from the adenovirus fiber shaft have an intrinsic capacity to form amyloid fibrils as judged by electron microscopy, Congo Red binding, infrared spectroscopy, and x-ray fiber diffraction. In the presence of the globular C-terminal domain of the protein that acts as a trimerization motif, the shaft sequences adopt a triple-stranded, -fibrous motif. We discuss the possible structure and arrangement of these sequences within the amyloid fibril, as compared with the one adopted within the native structure. A 6-amino acid peptide, corresponding to the last -strand of the shaft, was found to be sufficient to form amyloid fibrils. Structural analysis of these amyloid fibrils suggests that perpendicular stacking of -strand repeat units is an underlying common feature of amyloid formation.

Received for publication, June 7, 2004 , and in revised form, October 27, 2004.

^* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^¶¶ Present address: Laboratoire des Amino Acides, Peptides et Protéines, CNRS UMR 5810, Faculté de Pharmacie, 15 Ave. Charles Flahault, 34093 Montpellier, France.

^|||| Supported by the CNRS, the Direction d'Objectifs Matériaux of the Commissariat à l'Energie Atomique, and from the Délégation Générale pour l'Armement. To whom correspondence should be addressed: Dept. of Materials Science and Technology, the University of Crete, P. O. Box 2208, 710 03 Heraklion, Crete, Greece. E-mail: mitraki{at}materials.uoc.gr.

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