Protein stabilization and refolding in a gigantic self-assembled cage

Spatial isolation of molecules is often a powerful strategy for regulating their molecular behavior. Biological systems employ such mechanisms well; however, scientists have yet to rival nature, particularly for macromolecular substrates. We demonstrated that the encapsulation of a protein in a molecular cage with an open framework stabilizes the tertiary structure of the protein and improves its enzymatic activity. Particularly, when the three-dimensionally confined enzyme was exposed to an organic solvent, its half-life was prolonged 1,000-fold. Kinetic and spectroscopic analysis of the enzymatic reaction revealed that the key to this stability is the isolated space; this is reminiscent of chaperonins, which use their large internal cavities to assist the folding of client proteins. The single-molecule protein caging affords a new type of protein-based nanobiotechnology that accelerates molecular biology research as well as industrial applications.

Automated summary

Encapsulation of a protein in a molecular cage with an open framework stabilizes its tertiary structure and enhances its enzymatic activity, particularly in organic solvents. The key to this stability lies in the isolated space, reminiscent of chaperonins. This new protein-based nanobiotechnology accelerates molecular biology research and industrial applications.