Protein assemblies, and protein-inorganic hybrid materials, are the basis of a variety of biological processes and are an inspiration for supramolecular and inorganic chemists. Based on this premise, we devised an approach that merges the fields of supramolecular coordination chemistry and protein design to engineer the hierarchical assembly of a monomeric, porphyrin-containing protein into functional materials. In this approach, metal ions serve as a template for the formation of stable protein oligomers, which then further assemble via interfacial metal ions into crystalline supramolecular arrays. This strategy incorporates many of the advantages of metal-ligand bonds, including tunable strength, reversibility, directionality and responsiveness to chemical stimuli. By taking advantage of these attributes, we are able to tailor assembly pathways that favor the formation of crystalline materials with uniform morphologies, including helical nanotubes, 2-D arrays or 3-D crystals, from a single molecular precursor. The use of metal bonding interactions for the formation of these materials imparts a degree chemical and thermal stability on both the protein arrays themselves, as well as the protein building blocks, which are rare in biological assemblies. Rather than serving as a purely structural building block, the inherent redox activity of the proteins incorporated into these materials was used to control the spatiotemporal growth of inorganic nanostructures on the surface of the arrays. This work provides a strategy for the design of a unique class of materials that assemble from and stabilize protein subunits, and incorporate their inherent functionalities.

Hierarchical assembly of functional, protein-based materials via coordination chemistry and computational design

248th National Meeting (2014)

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