Proteins are highly efficient macromolecular machines responsible for daily functions in biological organisms. People have long been looking for ways to exploit their potentials in catalysis and sensing under cell-free conditions. However, these functions highly rely on the stability of the three-dimensional structures in proteins, which can easily be impaired under non-native conditions outside cells. Metal–Organic Frameworks (MOFs), as a family of porous crystalline material, have shown great promise as a host matrix for protein immobilization due to their tunable properties and high loading capacity. MOF with a hierarchical pore structure was shown to protect proteins against denaturing conditions and enhance their catalytic activity. Properties of mesoporous MOFs were also turned through functionalization, a process that offers means to systematically investigate interactions between the protein and its host material. This work showcases these advantages of MOFs as well-defined platforms for protein immobilization study.

Metal-organic frameworks for biological macromolecule immobilization

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