Study on protein release from hydrolytically degradable hydrogels governed by substituent effects in trehalose-based crosslinker and network properties

摘要

Five acid-labile diacetal crosslinkers containing disaccharide trehalose were synthesized. Effects of different substituents on aromatic ring on hydrolysis kinetics were compared using time-dependent H-1 NMR spectroscopy. A model protein (bovine serum albumin, BSA) was physically entrapped within bulk acrylamide-type hydrogels during redox-initiated free-radical polymerization. Under acidic conditions, hydrogel degradation occurred via cleavage of diacetal crosslinks to aqueous-soluble polymeric chains and free trehalose. The relationship between hydrogel degradation and protein release at around physiological pHs was studied. It was shown that selecting an appropriate crosslinker structure and main monomer type allows the tailoring of protein release profiles.