Role of Intermolecular Forces in Defining Material Properties of Protein Nanofibrils

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
DOI: 10.1126/science.1150057 Publication Date: 2007-12-21T01:19:52Z
ABSTRACT
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.
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