Solid binding proteins are genetically engineered chimera that incorporate one or more combinatorially-selected solid-binding peptide (SBP) at defined locations of their framework. These macromolecules are powerful tools to study the fundamentals of biotic-abiotic interactions because they allow for SBP presentation within solubilizing and structurally defined contexts. They are also useful to control inorganic morphogenesis and to assemble hybrid architectures that harness the “built-in” function and topology of the host scaffold. The development of solid-binding proteins that support the dynamic reconfiguration of hybrid materials has however proven more challenging. I will describe here how we used a combination of theory, simulations, mutagenesis and experiments to develop a detailed understanding of how a silica-binding peptide called Car9 interacts with silica surfaces, how we exploited this knowledge to build solid-binding proteins that support repeated cycles of silica nanoparticle assembly and disassembly upon small changes of pH, and how we rationally tuned the characteristics of these hybrid aggregates by manipulating solution conditions, particle size, host scaffold identity, and SBP sequence.

Reconfigurable hybrid colloids: Using solid-binding proteins to control nanoparticle assembly and disassembly

2019 Fall National Meeting

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