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
AUTHORS (7)
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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