Engineering Reversible Assembly of Reflectin in Robust Abiotic Host Materials for Signature Management Applications
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 measure, understand and control the molecular-, meso- and micro-scale compositions, structures and processes that govern the reversible assembly and disassembly of reflectin protein molecules in abiotic materials with macroscopic color-changing properties. This is motivated by potential applications for new materials with precise, responsive, and reversible properties, which biology has evolved strategies to achieve. For the case of reflectin assemblies in monodisperse organosilica microcapsules with dimensions in the range of 200–700 nm, this would enable dynamically adaptable camouflage or other signature management applications. Understanding and optimizing reflectin-host compositions, structures, and physicochemical interactions are prerequisites for the development of dynamic color-changing fibers, fabrics, and/or thin-film devices.
The resulting materials and scientific insights are expected to aid the development of functional soldier apparel, photo-responsive coatings, and other applications relevant to the Army. Dynamic color-changing fibers, fabrics, and/or thin-film devices are envisioned, with spatial resolution and temporal response to be controlled by optimizing reflectin-host compositions, structures, and physicochemical interactions.
Our primary objectives are to understand and control the factors that govern transient assembly and disassembly of the protein reflectin under abiotic conditions. To engineer robust abiotic host materials to encapsulate reflectin molecules and trigger their reversible assembly and disassembly. And finally, to integrate the reflectin-host materials into bulk matrices or at surfaces to produce color changes that are tunable and reversible. To achieve such properties requires that numerous reflectin molecules be incorporated into robust and processable synthetic materials with characteristic dimensions on the order of visible light and within which the assembly or disassembly of the protein molecules can be reversibly initiated.
