Abstract
We report experimental results from a de novo designed oligopeptide that intermolecularly self-assembles into rigid hydrogel networks after an intramolecular folding event. Microscopy and neutron scattering reveal a fibril local structure that is approximately 3 nm in diameter and over several hundred nanometers in length. Oscillatory rheology suggests that the peptidic network viscoelastic behavior follows that theoretically predicted for heavily cross-linked, semiflexible polymer networks.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Binding Sites
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Computer Simulation
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Crystallization / methods*
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Crystallography / methods*
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Elasticity
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Models, Chemical*
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Models, Molecular*
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Molecular Sequence Data
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Multiprotein Complexes / analysis
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Multiprotein Complexes / chemistry
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Multiprotein Complexes / ultrastructure
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Oligopeptides / analysis
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Oligopeptides / chemistry*
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Protein Binding
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Protein Structure, Secondary
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Structure-Activity Relationship
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Viscosity
Substances
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Multiprotein Complexes
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Oligopeptides