Filamentous chaperone protein-based hydrogel stabilizes enzymes against thermal inactivation. Issue 45 (14th May 2021)

• Record Type: Journal Article
• Authors: Xu, Dawei; Lim, Samuel; Cao, Yuhong; Abad, Abner; Kang, Aubrey Nayeon; Clark, Douglas S.
• Is Part Of: Chemical communications. Volume 57:Issue 45(2021)
• Page Start: 5511
• Page End: 5513
• Publication Date: 2021-05-14
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1039/d1cc01288f
• Languages: English
• ISSNs: 1359-7345

Abstract

Abstract : We report a filamentous chaperone-based protein hydrogel capable of stabilizing enzymes against thermal inactivation. Abstract : 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.