Nanomaterial Templated Assembly of Protein-Based Biomaterials

Jacob Forstater (University of North Carolina)

Immobilized enzymes are widely used as catalysts in industrial chemical production, diagnostic devices, and biosensors. Immobilization improves an enzyme's stability and creates an insoluble enzyme-based material that is easier to manipulate and recover. This is typically achieved by either covalently immobilizing enzymes to the surface of an inorganic carrier or by conning them within an inorganic scaold. Both of these strategies are problematic { surface adsorption limits immobilization to a monolayer, while connement prevents access to the enzymatically active site.

The desired approach would be to assemble enzymes, without chemical modication, into solid enzyme-based materials with an accessible microstructure. We have developed a novel nanomaterial whose unique surface chemistry appears to template the non-covalent assembly of enzymes into stable, micron-sized structures that contain more than 99% enzyme by weight and have enhanced catalytic activity. This process occurs in two stages { at low enzyme concentrations, enzyme multilayers form around the nanomaterial; above a critical enzyme concentration the enzyme-coated nanomaterial and any additional free enzyme assemble into large ellipsoidal structures. We have extensively characterized this phenomenon and the material surface chemistry using a variety of techniques, including dynamic light scattering, microcalorimetry, quantitative adsorption measurements, and solid-state NMR. Our ndings present a nanotechnology-enabled mechanism for creating stable protein-based materials. In this talk I will detail the assembly of these structures, the role of the nanomaterial's surface chemistry, and the design rules suggested by these ndings for creating other nanomaterial templates for biomolecule assembly.

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