Evaluation of acrylamide-based molecularly imprinted polymer thin-sheets for specific protein capture-a myoglobin model

We evaluate a series of thin-sheet hydrogel molecularly imprinted polymers (MIPs), using a family of acrylamide-based monomers, selective for the target protein myoglobin (Mb). The simple production of the thin-sheet MIP offers an alternative biorecognition surface that is robust, stable and uniform, and has the potential to be adapted for biosensor applications. The MIP containing the functional monomer N-hydroxymethylacrylamide (NHMAm), produced optimal specific rebinding of the target protein (Mb) with 84.9% (+/- 0.7) rebinding and imprinting and selectivity factors of 1.41 and 1.55, respectively. The least optimal performing MIP contained the functional monomer N,N-dimethylacrylamide (DMAm) with 67.5% (+/- 0.7) rebinding and imprinting and selectivity factors of 1.11 and 1.32, respectively. Hydrogen bonding effects, within a protein-MIP complex, were investigated using computational methods and Fourier transform infrared (FTIR) spectroscopy. The quantum mechanical calculations predictions of a red shift of the monomer carbonyl peak is borne-out within FTIR spectra, with three of the MIPs, acrylamide, N-(hydroxymethyl) acrylamide, and N-(hydroxyethyl) acrylamide, showing peak downshifts of 4, 11, and 8 cm(-1), respectively.

Automated summary

The evaluation of thin-sheet hydrogel molecularly imprinted polymers (MIPs) shows that those containing NHMAm monomer performed optimally for specific rebinding of the target protein, while those containing DMAm monomer showed the least optimal performance. Computational methods and FTIR spectroscopy were utilized to investigate hydrogen bonding effects within protein-MIP complexes, with predictions of red shifts in the monomer carbonyl peak being confirmed in the FTIR spectra.