Structural control of materials on the sub-micron scale may afford exquisite control over a broad spectrum of material properties, including porosity, mechanical properties, affinity for biological and non-biological molecules, and presentation of ligands. Control over these characteristics would influence a wide variety of applications in fields ranging from materials science to biotechnology, including biosensor development and tissue engineering. The guiding hypothesis of this proposal is that specific intermolecular interactions, such as protein tetramerization and ligand-induced conformational changes, can be employed to design protein units that self-assemble into dynamic 2-dimensional and 3-dimensional materials. I propose to identify candidate proteins that, based on their inter-subunit interactions and symmetry, are most likely to assemble into predictable 2-dimensional or 3-dimensional structures. Subunits of these proteins will then be linked to allow for self assembly into an extended protein matrix with controlled nanometer-scale structure. The linkage regions between the protein building blocks will be designed to contain units that undergo conformational changes in response to ligand binding to create dynamic structures, or units that mediate cell adhesion to create substrates for cell culture and tissue engineering.
| Murphy, William L; Mercurius, Kwesi O; Koide, Shohei et al. (2004) Substrates for cell adhesion prepared via active site-directed immobilization of a protein domain. Langmuir 20:1026-30 |
