Protein-directed, hydrogen-bonded biohybrid framework

Here, we describe a versatile protein-directed assembly strategy that enables the organization of different types of proteins and organic linkers into a highly crystalline hybrid framework through hydrogen-bond interaction. The whole assembly process is protein actuated but is independent of the protein-surface property. Advanced low-electron-dose cryoelectron microscopy techniques clearly witness the crystallographic structure of hybrid framework at a single-molecular level, and we demonstrate that the proteins are independently and tightly isolated in the crystalline frameworks, with a record-high protein content in the reported biohybrid framework materials. In addition, the hybrid framework has ultrahigh chemical stability, and its aperture structure and protein confinement tightness are controllable through modulating the organic linkers. When using enzymes as the building block, the obtained enzyme framework shows significantly improved stability compared with the free enzymes and displays notable advantages for biocatalysis compared with the burgeoning enzyme-MOF biohybrids in terms of active ingredient content, robustness, and catalytic efficiency.

Automated summary

A versatile protein-directed assembly strategy is described, allowing the organization of different types of proteins and organic linkers into a highly crystalline hybrid framework through hydrogen-bond interaction. The resulting hybrid framework exhibits record-high protein content and ultrahigh chemical stability, with controllable aperture structure and protein confinement tightness through modulating organic linkers. Enzyme frameworks obtained using this strategy show significantly improved stability and notable advantages for biocatalysis compared to enzyme-MOF biohybrids in terms of active ingredient content, robustness, and catalytic efficiency.