Porous Protein Framework Materials as Tunable Scaffolds for Abiotic Dual Catalysis
Abstract
Merging biomolecular scaffolds with abiotic components is a promising strategy to drive new chemical transformations that are difficult or impossible using either conventional synthesis or biocatalysis alone. Tremendous advances have been made in combining soluble protein scaffolds with abiotic catalysts, but it remains challenging to incorporate multiple abiotic groups into a single protein active site. If new biomolecular scaffolds could be created that display multiple abiotic groups, they would grant access to the enhanced reactivity provided by Òdual catalysis,Ó a burgeoning field in synthetic chemistry whereby multiple abiotic catalysts work synergistically. Furthermore, it would be advantageous if scaffolded dual catalytic active sites could be created within a solid framework material that is robust, recyclable, and features a high active site density. Here, I propose porous protein framework materials as scaffolds for abiotic dual catalysis. We will employ protein-based materials that are thermally and chemically stable, preparable on multi-gram scale, more resistant to denaturation than most soluble proteins, and compatible with diverse solvents and reaction conditions. We will tether reactive abiotic catalysts in precise locations in the pores, enabling dual catalysis with enhanced reaction rate and specificity compared to conventional synthesis, and with reactivity that is unprecedented in biomolecular systems. Numerous dual catalytic mechanisms can be explored using this general approach, including selective reactions that have remained elusive using conventional synthetic methods. Overall, my proposed materials should engender fundamentally new reactivity by pre-organizing multiple abiotic catalysts within tunable biomolecular scaffolds. The diverse selection of dual catalytic mechanisms will create fundamentally new opportunities for synthesis of energetic materials, precursors to energetic materials, polymers, and composites. In the long term, I envision the creation of protein framework catalysts that mimic natural enzymes by displaying not just two, but three or more reactive groups into a single cavity. I ultimately envision the precise tailoring of these cavities to orient substrates for specific cyclization reactions to form high-energy structures, or regioselective modifications of complex small molecule architectures that are impossible using existing synthetic methods.
Document Details
- Document Type
- DoD Grant Award
- Publication Date
- Jun 25, 2021
- Source ID
- W911NF2110139
Entities
People
- Jeffrey Martell
Organizations
- Army Contracting Command
- United States Army
- University of Wisconsin–Madison