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Science 21 December 2007:
Vol. 318. no. 5858, pp. 1900 - 1903
DOI: 10.1126/science.1150057
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Reports

Role of Intermolecular Forces in Defining Material Properties of Protein Nanofibrils

Tuomas P. Knowles,1,2* Anthony W. Fitzpatrick,2* Sarah Meehan,3 Helen R. Mott,4 Michele Vendruscolo,3 Christopher M. Dobson,3{dagger} Mark E. Welland1{dagger}

Protein molecules have the ability to form a rich variety of natural and artificial structures and materials. We show that amyloid fibrils, ordered supramolecular nanostructures that are self-assembled from a wide range of polypeptide molecules, have rigidities varying over four orders of magnitude, and constitute a class of high-performance biomaterials. We elucidate the molecular origin of fibril material properties and show that the major contribution to their rigidity stems from a generic interbackbone hydrogen-bonding network that is modulated by variable side-chain interactions.

1 Nanoscience Centre, University of Cambridge, J. J. Thomson Avenue, Cambridge CB3 0FF, UK.
2 Cavendish Laboratory, University of Cambridge, Madingley Road, Cambridge CB3 0HE, UK.
3 Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
4 Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1GA, UK.

* These authors contributed equally to this work.

{dagger} To whom correspondence should be addressed. E-mail: cmd44{at}cam.ac.uk (C.M.D.); mew10{at}cam.ac.uk (M.E.W.)

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