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Summary
We investigated potentials of fusing protein oligomerization domain with coiled-coil-forming domain for the formation of nanostructures. This combination should form a two- or three-dimensional lattice if the coiled-coil-forming domain forms an antiparallel homodimer. Particular advantage of this approach is that we can incrementally extend or modify the coiled coil-forming domain, which results in modification of the size of the lattice unit as well as in the size of pores enclosed by coiled-coil segments.
We designed and prepared fusion protein between p53 tetramerization domain and antiparallel coiled-coil domain. This type of nanomaterial contains nanopores of defined size, which could be used to separate molecules or molecular assemblies according to their size. We assembled the material by a refolding procedure and tested it in a real world application as ultrafiltration membrane. The membranes efficiently remove large molecules and viruses from the sample.
Figure: The self-assembled polypeptide membrane and its efficacy in removing viruses from solution. A) The polypeptide material composed of tetramerization domain linked to coiled-coil-forming domain . B) The removal of viruses from the solution with the self-assembled polypeptide membrane.
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Idea and Approach
Results
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