Non-Technical: This award by the Biomaterials Program in the Division of Materials Research to Colorado State University is to design new materials by encoding the assembly of building block proteins. This award is cofunded by US Army Natick Soldier Research, Development & Engineering Center. The intended crystalline biomaterials are so precisely organized that they will diffract X-rays, allowing high-resolution determination of the molecular structure details. While there are many possible applications for such materials, this proposal focuses on (1) determining the extent to which the position of constituent building blocks can be programmed, and (2) assessing applications for the protein crystal pore network. Specifically, the project will produce and characterize close-packed hexagonal arrays of nanowires that may form useful ultra-high surface area materials for catalysis or battery applications. Porous protein crystals may also offer advantages as multifunctional delivery materials, combining high capacity with the possibility of extensive nanostructure control. The project provides educational opportunities from high school and the University due to integration with AP Chemistry and Biomolecular Engineering courses, as well as broad dissemination via an open-source software platform (SHARPEN) for protein modeling and design.
The proposed research will study proteins as building blocks to assemble crystalline materials in which it is possible to exert sub-nanometer control over the location of constituent domains. This research will also exploit the highly anisotropic pore structure of existing protein crystals in pursuit of nanostructured material applications. The project will produce and characterize close-packed hexagonal arrays of nanowires via synthesis of conductive polymers or the capture of carbon nanotubes within a parallel array of nanopores. Additionally, the research will determine the suitability of porous crystals to serve as depots for the controlled release of antimicrobial peptides under challenging operational conditions. Specifically, the project will assess the extent to which protein crystals with very different pore sizes adsorb antimicrobial peptides, conditionally gate guest peptide release, and withstand demanding conditions including denaturants, heat, freeze-thaw cycles, and desiccation. This proposal also includes a software engineering effort to improve accessibility of the SHARPEN platform, further extending the impact of protein design methodology improvements. Research training will encompass cutting-edge areas of bionanotechnology, molecular modeling, and nanostructure imaging.
