Molecularly imprinted hydrogel sensor for proteins

Abstract

The approach toward the molecular imprinting of hydrogel with different proteins erects the template-size cavities inside the matrix. The cavities provide the binding sites to adsorb the protein perfectly in the hydrogel. To intensify the adsorption efficiency of protein bovine serum albumin (BSA), cobalt ions (Co) play an essential role. In contrast, 2-(Dimethylamino) ethyl methacrylate (DMAEMA) provides pH sustainability as an assistant monomer. Results elucidate that incorporating Co in preparation can enhance the hydrogel’s imprinting effect or adsorption efficiency compared to others due to the development of coordinated covalent bonding. Hydrogel adsorption capacity is an essential factor in this study. In this research, the obtained BSA-imprinted hydrogel also observed a high protein adsorption capacity. The Co concentration and pH of the hydrogel system are the main factors affecting proteins’ adsorption efficiency. Their optimizations are the main concerns, and their successful implementations are confirmed by UV/Vis spectroscopy. The imprinted BSA protein was removed by using 500 mmol/L NaCl solution. The two and three-parameter isothermal models were implemented to predict the mechanism of the adsorption process.