The design of biomaterials from natural building blocks is a growing area of interest with numerous nanotechnological applications. One promising strategy is the use of protein subunits to build readily modifiable scaffolds. Over the last decade, there has been considerable progress towards the rational design of protein-based biomaterials. However, efforts to define a set of universal design principles for protein self-assembly have proven particularly difficult. We have recently developed a novel approach to form disulfide-mediated, ordered 2-D arrays. Arrays are generated from the slow oxidation of cysteine residues installed on the surface of a symmetric protein tetramer. Protein self-assembly can also be accomplished via metal-mediation: surface-exposed histidine residues or covalently attached non-natural ligands provide metal-coordinating motifs to promote material growth upon the addition of transition metal salts. We have expanded this approach to rationally design other symmetric proteins to form ordered materials. Generating a library of materials with a variety of protein geometries presents an exciting new avenue towards developing universal design principles for protein scaffold self-assembly.

Exploring disulfide and metal-mediated bonding as design principles for protein self-assembly

251st National Meeting (2016)

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