Role of Intermolecular Forces in Defining Material Properties of Protein Nanofibrils

• DOI: 10.1126/science.1150057
• Publication Date: 2007-12-21T01:19:52Z
• Authors: Tuomas P. Knowles; Anthony W. Fitzpa...; Sarah Meehan; Helen R. Mott; Michele Vendruscolo; Christopher M. Do...; Mark E. Welland
• Keywords: Models, Molecular; Amyloid; 0303 health sciences; Amyloid beta-Peptides; Chemical Phenomena; Chemistry, Physical; Prions; Protein Conformation; Hydrogen Bonding; Lactoglobulins; Microscopy, Atomic Force; Elasticity; Nanostructures; 03 medical and health sciences; Lactalbumin; Humans; Insulin; Prealbumin; Muramidase; Peptides; Hydrophobic and Hydrophilic Interactions; Peptide Termination Factors

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.