| Abstract: | This study presents the hydrogelation of bovine serum albumin by using a natural‐derived photo‐initiator system based on riboflavin and l ‐arginine that ensures the preparation of biocompatible hydrogels. Fourier transform infrared spectroscopy reveals that the synthesis conditions do not induce protein denaturation and confirms the potential UV‐crosslinking mechanism for albumin hydrogels realization. Thermal and morphological characterization indicates the formation of thermodynamically stable hydrogels with interconnected inner structure which presents a riboflavin concentration‐dependent porosity. The evolution of the hydrogel's decomposition products is analyzed by thermogravimetric analysis coupled with Fourier transform infrared spectroscopy and mass spectrometry and reveals a degradation pathway characterized by deamination of unreacted amino moieties and peptide ? NH? groups, condensation, decomposition of the condensation products, and oxidation of N‐containing residues. The kinetics and pH‐responsive behavior of hydrogels are investigated by water uptake dynamics revealing a swelling mechanism which can be switched from a less Fickian to a non‐Fickian process by varying the crosslinker concentration. In vivo tests prove the high degree of biocompatibility of the new hydrogels, after oral administration in mice. |
