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Nanostructured films from hierarchical self-assembly of amyloidogenic proteins.


ABSTRACT: In nature, sophisticated functional materials are created through hierarchical self-assembly of simple nanoscale motifs. In the laboratory, much progress has been made in the controlled assembly of molecules into one-, two- and three-dimensional artificial nanostructures, but bridging from the nanoscale to the macroscale to create useful macroscopic materials remains a challenge. Here we show a scalable self-assembly approach to making free-standing films from amyloid protein fibrils. The films were well ordered and highly rigid, with a Young's modulus of up to 5-7 GPa, which is comparable to the highest values for proteinaceous materials found in nature. We show that the self-organizing protein scaffolds can align otherwise unstructured components (such as fluorophores) within the macroscopic films. Multiscale self-assembly that relies on highly specific biomolecular interactions is an attractive path for realizing new multifunctional materials built from the bottom up.

SUBMITTER: Knowles TP 

PROVIDER: S-EPMC4612398 | biostudies-literature | 2010 Mar

REPOSITORIES: biostudies-literature

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Nanostructured films from hierarchical self-assembly of amyloidogenic proteins.

Knowles Tuomas P J TP   Oppenheim Tomas W TW   Buell Alexander K AK   Chirgadze Dimitri Y DY   Welland Mark E ME  

Nature nanotechnology 20100228 3


In nature, sophisticated functional materials are created through hierarchical self-assembly of simple nanoscale motifs. In the laboratory, much progress has been made in the controlled assembly of molecules into one-, two- and three-dimensional artificial nanostructures, but bridging from the nanoscale to the macroscale to create useful macroscopic materials remains a challenge. Here we show a scalable self-assembly approach to making free-standing films from amyloid protein fibrils. The films  ...[more]

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