Cryo-electron microscopy (left) and artificial intelligence-based simulation (right) confirm biophysical analyses showing that reflectin switches from open-chain monomers to tightly condensed multimers, with expulsion of water.
This project seeks to understand and control the complicated factors that govern transient assembly and disassembly of the protein reflectin in porous polymeric or organosilica microspheres. This is motivated by potential applications for new materials with responsive and reversible coloration properties, which would enable dynamically adaptable camouflage or other signature management applications. To achieve such properties requires that numerous reflectin molecules be incorporated into robust and processable synthetic matrices, within which the assembly or disassembly of the protein molecules can be triggered. The resulting scientific insights and materials are expected to aid the development of functional soldier apparel, photo-responsive coatings and other applications relevant to the Army.
Our primary objectives are to incorporate reflectin and its genetically engineered derivatives into robust, but flexible, synthetic host materials. Understanding and optimizing reflectin-host compositions, structures, and physicochemical interactions are prerequisites for the development of a new generation of responsive fibers, fabrics, and/or thin-film devices for Army use.