Self-assembly of protein-based suprastructures

Strategies for self-assembly of protein-based suprastructures were developed. Recombinant protein building blocks were designed, produced, and self-assembled into various suprastructures, which include spheres, vesicles, nanosheets and porous particles. Morphology was manipulated by engineering protein building blocks, controlling self-assembly processes, and combining inorganic nanocrystals into hybrid materials. Self-assembly of spherical protein coacervates was achieved in the extracellular matrix, mediated by spontaneous diffusion-coacervation and high-affinity binding of building blocks. Vesicles and two-dimensional nanosheets were self-assembled from recombinant protein complexes, whose molecular geometry dictated the morphologies of self-assembled structures. Self-clustering hybrid flower-shaped nanoparticles were prepared and further assembled into hierarchically structured porous supraparticles. All the suprastructures were created as modular systems which enabled incorporation folded functional proteins. Enzymes incorporated in the porous supraparticles showed enhanced inactivation of a pro-inflammatory cytokine, tumor necrosis factor-α. The modular design approach, combined with manipulation of morphology, offer opportunities for practical applications.Ph.D