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.
Original language | English |
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Pages (from-to) | 203-208 |
Number of pages | 6 |
Journal | ACS Applied Bio Materials |
Volume | 6 |
Issue number | 1 |
DOIs | |
State | Published - 16 Jan 2023 |
Keywords
- biomaterials
- dityrosines
- hydrogels
- prefoldin
- proteins
- silk