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.

Designed amyloid fibers as materials for selective carbon dioxide capture

“…Applications of amyloid fibers have been explored in the fields including conductive nanowires (34), nanostructured protein films (35), light-harvesting nano-device (36,37), and retroviral gene transfer boosting (38). The properties demonstrated here of amyloid fibers for carbon dioxide capture fall short of those needed in a practical material operating in the demanding conditions of water, acid, and temperature of flue gas.…”

Failure of Aβ(1-40) amyloid fibrils under tensile loading

“…The results of the atomistic simulations, combined with a simple theoretical model, allow us to define different size scales on the basis of the key mechanisms dominating the failure of the fibril. The insight derived here has important implications for the development of models of larger-scale amyloid plaques where thousands of fibrils supposedly approach the micrometer scale [52] and interact determining the observed stiffness of amyloid plaques [30,53].…”

“…According to earlier experimental and theoretical studies these mechanical properties are related to their molecular structure [10,12]. The exceptional mechanical properties of amyloids make them good candidates for a wide range of potential technological applications, and specifically as new bionanomaterials utilizing them as nanowires [13][14][15][16], gels [17][18][19][20][21], scaffolds and biotemplates [13,[22][23][24][25][26][27], liquid crystals [28], adhesives [29] and biofilm materials [30]. These applications often imply the functionalization of the amyloid fibrils with the introduction of additional elements, including enzymes, metal ions, fluorophores, biotin or cytochromes.…”

Lyotropic phase behaviour of dilute, aqueous hen lysozyme amyloid fibril dispersions

“…Inspired by such potentially useful qualities, more recently, amyloid fibrils have been extensively investigated as functional materials that direct supra-molecular self-assembly [4][5][6], or serve as templates for, e.g. metal nanoparticles [7][8][9] and conjugated (poly)electrolytes [10][11][12][13][14]. Such prepared nanofibrils are of particular interest for applications in biotechnology and organic opto-electronics because of their characteristic feature sizes, i.e.…”