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- W4313271123 abstract "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 γ-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 γ-prefoldin." @default.
- W4313271123 created "2023-01-06" @default.
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- W4313271123 date "2022-12-29" @default.
- W4313271123 modified "2023-10-06" @default.
- W4313271123 title "Horseradish Peroxidase Catalyzed Silk–Prefoldin Composite Hydrogel Networks" @default.
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- W4313271123 doi "https://doi.org/10.1021/acsabm.2c00836" @default.
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