Amyloid character of self-assembling proteins based on adenovirus fiber shaft sequences |
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| Authors: | Haris Retsos Katerina Papanikolopoulou Claude Filippini Christian Riekel Kenncorwin H Gardner V Trevor Forsyth Anna Mitraki |
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| Institution: | (1) Institut de Biologie Structurale (UMR 5075, CEA-CNRS-UJF), 41 rue Jules Horowitz, 38027 Grenoble, France;(2) Laboratoire d’études des Propriétés Electroniques des Solides, Centre National de la Recherche Scientifique, 38042 Grenoble Cedex 9, France;(3) European Synchrotron Radiation Facility, 6 rue Jules Horowitz, 38042 Grenoble, France;(4) E.I. du Pont de Nemours and Company, Central Research and Development, 200 Powder Mill Road, Experimental Station, 19880-0302 Wilmington, DE, USA;(5) Present address: Department of Materials Science and Engineering, University of Delaware, 197 16 Newark, DE, USA;(6) Institut Laue-Langevin, 6 rue Jules Horowitz, 38042 Grenoble, France;(7) Lennard-Jones Laboratories, School of Chemistry and Physics, Keele University, ST5 5BG, Staffordshire, United Kingdom;(8) Department of Materials Science and Technology, University of Crete, P.O. Box 2208, 710 03 Heraklion, Crete, Greece |
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| Abstract: | Fibrous proteins found in natural materials such as silk fibroins, spider silks, and viral spikes increasingly serve as a
source of inspiration for the design of novel, artificial fibrous materials. The fiber protein from the adenovirus has previously
served as a model for the design of artificial, self-assembling fibers. The fibrous shaft of this protein consists of 15-amino-acid
sequence repeats that fold into a triple β-spiral motif in their native context. Recombinant proteins based on multimers of
simplified consensus shaft repeats were previously reported to form self-assembling fibrils from which filaments could be
spun. Here, we describe the structural characterization of these fibrils; X-ray fiber diffraction, Raman spectroscopy, and
Congo Red binding strongly suggest an amyloid-type structure for these fibrils, with β-strands arranged perpendicular to the
fibril axis. This amyloid structure is distinct from the native β-spiral fold, and similar to amyloid structures formed by
short, synthetic peptides corresponding to shaft sequences. We discuss implications for the rational design of novel fibrous
materials, based on crystal structure information and knowledge of folding and assembly pathways of natural fibrous proteins. |
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| Keywords: | Adenovirus amyloid biomaterial β -structure fibrous protein self-assembly |
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