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ReportsRole of Intermolecular Forces in Defining Material Properties of Protein Nanofibrils![]() ![]()
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.
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Science. ISSN 0036-8075 (print), 1095-9203 (online)