Filamentous chaperone protein-based hydrogel stabilizes enzymes against thermal inactivation

We report a filamentous chaperone-based protein hydrogel capable of stabilizing enzymes against thermal inactivation. The hydrogel backbone consists of a thermostable chaperone protein, the gamma-prefoldin (gamma PFD) from Methanocaldococcus jannaschii, which self-assembles into a fibrous structure. Specific coiled-coil interactions engineered into the wildtype gamma PFD trigger the formation of a cross-linked network of protein filaments. The structure of the filamentous chaperone is preserved through the designed coiled-coil interactions. The resulting hydrogel enables entrapped enzymes to retain greater activity after exposure to high temperatures, presumably by virtue of the inherent chaperone activity of the gamma PFD.

Automated summary

This study presents a filamentous chaperone-based protein hydrogel that can stabilize enzymes against thermal inactivation. The hydrogel backbone is composed of a thermostable chaperone protein, gamma-prefoldin (gamma PFD), which self-assembles into a fibrous structure. Engineered specific coiled-coil interactions in the wildtype gamma PFD trigger the formation of a cross-linked network of protein filaments, preserving the structure of the filamentous chaperone and enabling entrapped enzymes to retain greater activity after exposure to high temperatures.