The accessibility of reactants to the surface of enzymes is crucial for its function. Therefore, in order to exploit the enzymatic properties of proteins in non-biological environments, it is crucial to organize proteins in assemblies that expose their surfaces to the reactants. Here, we describe and analyze two methods to organize enzymatically active proteins in non-biological environments. First, protein functionalization with linkers with reactive end groups is analyzed to organize proteins into open crystalline structures (1). Second, random heteropolymers that mimic unstructured proteins in membraneless organelles are used to assemble functional polymer-protein membranes. In particular, since the enzymatic activity of many proteins is enhanced in organic solvents, we exploit the protein sub-nanometer polar and non-polar surface domains to design random heteropolymers that stabilize proteins’ structures and preserve their enzymatic activities in diverse solvent conditions (2).
(1) Girard, M., et al Annu. Rev. Mater. Res. 47 33-49 (2017); K. Krishnamoorthy, et al. ACS Central Science 4, 378-386 (2018).
(2) B. Panganiban, et al. Science 359: 1239-1243 (2018); T. Nguyen, et al. PNAS 26, 6578-6583 (2018).