(331a) Controlling Hybrid Structure Assembly, Solid Interactions and Inorganic Mineralization with Solid Binding Proteins

The integration of combinatorially selected solid-binding peptides (SBPs) within functional protein scaffolds is a powerful approach to produce hybrid architectures with unique properties, control biotic-abiotic interactions and study and manipulate inorganic precipitation and morphogenesis. Here, I will illustrate each of these processes with an example from our laboratory. In the first vignette, one of two SBPs incorporated within the green fluorescent protein (GFP) framework is used to mineralize luminescent Mn-doped ZnS nanocrystals, a chloramphenicol-specific DNA aptamer is coupled to the protein-coated quantum dots via click chemistry and the second SBP is used to tether these structures to silica beads. The unique optical properties of the resulting assemblies are exploited for sensitive detection of chloramphenicol in a format that is amenable to field-testing. In a second example, proteins fitted with a silica-binding peptide become stably entrapped within a silica sol-gel that they help condense. The kinetics and extent of protein release is finely controlled by chemically disrupting the interaction between silica-binding extension and surface and by changing the size and shape of the particles. In the last example, I will describe how mutagenesis of an SBP and its insertion at multiple locations of the GFP scaffold influences titania precipitation and affects non-equilibrium formation of titania patterns.