(368a) Surface-Mediated Assembly of Site-Modified Green Fluorescent Protein into Two-Dimensional Nanosheets As a Platform for Hierarchical Materials Fabrication

Hierarchical architectures in which individual nanoscale components organize to determine order or function at larger scales have extraordinary potential for the creation of active interfaces and multidimensional structures with unique mechanical, optical, and catalytic properties. High information content macromolecules such as nucleic acids, foldamers, peptides and proteins, are desirable building blocks for such hierarchies due to their monodispersity and programmability. Among these species, proteins are especially valuable owing to their broad range of structures, chemistries and functions, and their amenability to genetic and chemical modifications. To date, the assembly of robust protein-based hierarchies has been challenging. Here, we use a variant of superfolder Green Fluorescent Protein that is modified with 4 equatorial cysteines (sfGFP(4C)) and functionalized with a thiol-reactive linker to mediate efficient 2D assembly. Further, surface interactions are mediated by a solid-binding sequence that is genetically inserted within a permissive loop of the protein. In addition to its inherent optical properties, this system is being used as a platform for the bottom-up construction of active interfaces via oriented integration of light-activated proton pumps solubilized in peptidiscs.