(650f) Engineering Ultrastable Protein Scaffolds for the Controlled Assembly of Multifunctional Nanobiomaterials

Self-assembling protein templates are of increasing interest in the field of nanoscale fabrication of biomaterials, where precise patterning of functional biomolecules, such as enzymes, is often desired. In particular, protein building blocks can be strategically chosen to exhibit desired functionality, while engineering their assembly allows for the controllable positioning of the subunits. The filamentous protein g-prefoldin (g-PFD) from the hyperthermophilic archaeon Methanocaldococcus jannaschii is an excellent candidate for such a tunable scaffold. Its remarkable stability, unique modularity, and self-assembly into filaments with chaperone activity render it an ideal candidate for the bottom-up construction of novel protein nanostructures.

We have recently reported the assembly of g-PFD monomers into geometrically defined templates of tunable dimensions and symmetry, as well as the controlled positioning of nanoparticles along the filaments. We aim to achieve more complex patterning, while expanding the applicability of g-PFD templates to diverse enzymatic systems. Fusing different enzymes to each subunit should enable periodic positioning of multiple enzymes along the filament to catalyze sequential reactions and metabolic pathways. In addition, we have demonstrated the ability to position cytochrome C proteins at high density along the filament as a first step to creating novel conductive nanowires. Finally, we are studying g-PFDâ??s ability to form 3D crosslinked multifunctional protein hydrogels. Ultimately, the ability to position functional molecules in a controlled manner will considerably enhance our ability to fabricate advanced multifunctional nanobiomaterials.