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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amyloid / chemistry*
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Amyloid beta-Peptides / chemistry
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Chemical Phenomena
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Chemistry, Physical
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Elasticity
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Humans
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Hydrogen Bonding
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Hydrophobic and Hydrophilic Interactions
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Insulin / chemistry
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Lactalbumin / chemistry
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Lactoglobulins / chemistry
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Microscopy, Atomic Force
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Models, Molecular
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Muramidase / chemistry
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Nanostructures / chemistry*
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Peptide Termination Factors
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Peptides / chemistry*
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Prealbumin / chemistry
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Prions / chemistry
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Protein Conformation
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Protein Structure, Tertiary
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Saccharomyces cerevisiae Proteins / chemistry
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Surface Tension
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alpha-Crystallin B Chain / chemistry
Substances
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Amyloid
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Amyloid beta-Peptides
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Insulin
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Lactoglobulins
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Peptide Termination Factors
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Peptides
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Prealbumin
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Prions
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SUP35 protein, S cerevisiae
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Saccharomyces cerevisiae Proteins
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alpha-Crystallin B Chain
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Lactalbumin
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Muramidase