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Genetic Fusion of Thermoresponsive Polypeptides Mediates 1-D Assembly of Coiled Coil Bundlemers

The ability to thermally trigger a conformational changeand collapse in a constituent resilin-like protein (RLP) providesthe opportunity to build, and eventually move, a bundlemer nanostructure.

Bundlemer peptides can still assemble into coiled coil bundles even with RLPs attached to all four constituent peptides in each bundle.  This is a clear demonstration that biosynthesis can be used for bundlemer building block production for future study.

  • This ability affords a mechanism for the formation (and disassembly) of bundlemer-based nanomaterials through temperature responsive proteins
  • The ability to thermally trigger a conformational change/collapse in a constituent polymer/protein provides the opportunity to purposefully move a bundlemer nanostructure in future Aim 2 efforts.
  • This is a major step towards success of Aim 2 in which nanostructures will be purposefully moved.  The thermal collapse of the RLP can be used to both form structure (Aim 1) and to move structure (Aim 2).
  • The successful biosynthesis from E. Coli of the bundlemer peptide and RLP constructs clearly affords future success in peptide/protein production with biosynthesis for scale up and study.