title: Role of intermolecular forces in defining material properties of protein nanofibrils.
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.
authors: Nanoscience Centre, University of Cambridge, J. J. Thomson Avenue, Cambridge CB3 0FF, UK.
authors: Tuomas P
authors: TP
authors: Knowles
authors: Anthony W
authors: AW
authors: Fitzpatrick
authors: Sarah
authors: S
authors: Meehan
authors: Helen R
authors: HR
authors: Mott
authors: Michele
authors: M
authors: Vendruscolo
authors: Christopher M
authors: CM
authors: Dobson
authors: Mark E
authors: ME
authors: Welland
mesh_terms: D000682:Amyloid / Q000737:chemistry*; D016229:Amyloid beta-Peptides / Q000737:chemistry; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D004548:Elasticity; D006801:Humans; D006860:Hydrogen Bonding; D057927:Hydrophobic and Hydrophilic Interactions; D007328:Insulin / Q000737:chemistry; D007768:Lactalbumin / Q000737:chemistry; D007782:Lactoglobulins / Q000737:chemistry; D018625:Microscopy, Atomic Force; D008958:Models, Molecular; D009113:Muramidase / Q000737:chemistry; D049329:Nanostructures / Q000737:chemistry*; D010454:Peptide Termination Factors; D010455:Peptides / Q000737:chemistry*; D011228:Prealbumin / Q000737:chemistry; D011328:Prions / Q000737:chemistry; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry; D013500:Surface Tension; D038203:alpha-Crystallin B Chain / Q000737:chemistry
chemical_list: D000682:Amyloid; D016229:Amyloid beta-Peptides; D007328:Insulin; D007782:Lactoglobulins; D010454:Peptide Termination Factors; D010455:Peptides; D011228:Prealbumin; D011328:Prions; C068068:SUP35 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D038203:alpha-Crystallin B Chain; D007768:Lactalbumin; D009113:Muramidase