Filamentous chaperone protein-based hydrogel stabilizes enzymes against thermal inactivation.

Dawei Xu, Samuel Lim, Yuhong Cao, Abner Abad, Aubrey Nayeon Kang, Douglas S Clark

Chemical communications (Cambridge, England) 2021 Jun 03

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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 (γPFD) from Methanocaldococcus jannaschii, which self-assembles into a fibrous structure. Specific coiled-coil interactions engineered into the wildtype γPFD 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 γPFD.

Citation

Dawei Xu, Samuel Lim, Yuhong Cao, Abner Abad, Aubrey Nayeon Kang, Douglas S Clark. Filamentous chaperone protein-based hydrogel stabilizes enzymes against thermal inactivation. Chemical communications (Cambridge, England). 2021 Jun 03;57(45):5511-5513