Horseradish Peroxidase Catalyzed Silk-Prefoldin Composite Hydrogel Networks

Protein-based hydrogel biomaterials provide a platform for different biological applications, including the encapsulation and stabilization of different biomolecules. These hydrogel properties can be modulated by controlling the design parameters to match specific needs; thus, multicomponent hydrogels have distinct advantages over single-component hydrogels due to their enhanced versatility. Here, silk fibroin and gamma-prefoldin chaperone protein based composite hydrogels were prepared and studied. Different ratios of the proteins were chosen, and the hydrogels were prepared by enzyme-assisted cross-linking. The secondary structure of the two proteins, dityrosine bond formation, and mechanical properties were assessed. The results obtained can be used as a platform for the rational design of composite thermostable hydrogel biomaterials to facilitate protection (due to hydrogel mechanics) and retention of bioactivity (e.g., of enzymes and other biomolecules) due to chaperone-like properties of gamma-prefoldin.

Automated summary

Protein-based hydrogel biomaterials offer a versatile platform for various biological applications, with the ability to encapsulate and stabilize biomolecules. In this study, silk fibroin and gamma-prefoldin chaperone protein were used to create composite hydrogels with different protein ratios, using enzyme-assisted cross-linking. The secondary structure, dityrosine bond formation, and mechanical properties were evaluated. The findings provide insights for the rational design of composite thermostable hydrogel biomaterials, allowing for protection and retention of bioactivity.