Design of crystalline materials represents a major goal common to numerous scientific disciplines. Proteins are especially attractive building blocks for crystalline materials as they provide high chemical and structural diversity and possess inherent functions such as catalysis, electron transfer, and molecular recognition. Importantly, the formation of ordered, 3D protein crystals is the foundation as well as the rate-limiting step of protein crystallography, providing a strong motivation for their rational design. Although effective methodologies have been developed for facilitating protein crystallization, successes in obtaining 3D protein crystals by design have been rare. In contrast, coordination polymers such as metal-organic frameworks (MOFs) benefit from a high degree of modularity, where component nodes/struts can be interchanged to produce structurally unique architectures with vastly different materials properties. Inspired by MOFs, we developed a method for the formation of crystalline protein arrays based on the construction principles of MOFs, wherein transition-metal loaded spherical protein nodes are interconnected by small ditopic organic linkers possessing metal-binding functional groups. Akin to traditional MOFs, the modularity of these lattices stems from the multiple interchangeable components, which dictate both the crystalline structure and material properties of the protein–MOFs. Research on this new class of materials aims to exploit their highly modular nature, whereby the metal, ligand, and protein scaffold can be systematically varied to assemble unique lattices with different structures and functions.
Principal members: Jake, Ling, Jie, Jerika
J.B. Bailey, L. Zhang, J.A. Chiong, S. Ahn, F.A. Tezcan. Synthetic Modularity of Protein–Metal–Organic Frameworks, J. Am. Chem. Soc. (2017).[PDF]
P.A. Sontz*, J.B. Bailey*, S. Ahn, F.A. Tezcan. A Metal Organic Framework with Spherical Protein Nodes: Rational Chemical Design of 3D Protein Crystals, J. Am. Chem. Soc. (2015).[PDF]