ATP-binding peptide-hydrogel composite synthesized by molecular imprinting on beads

Abstract Molecular imprinting has been recognized as a useful technique to produce synthetic mimics of functional proteins, such as antibodies and enzymes. However, only a few studies have examined peptides as starting materials for synthesizing molecularly imprinted polymers in spite of the expectation that peptides would be suitable materials for realizing water-compatibility and proteinlike functions. In this study, molecular imprinting was performed using a vinyl-end-capped on-beads-peptide as functional monomer to produce an on-beads-peptide hydrogel composite selective for ATP; the on-beadspeptide peptide, of which sequence was designed to possess both an adenine-recognition site and phosphate recognition site, was co-polymerized with NIPAM and BIS in the presence of ATP as a template species. The resultant ATP-imprinted composite showed 14-times higher affinity and an enhanced selectivity towards ATP, suggesting that the peptide conformation, i.e. a mutual orientation of the two binding sites, was pre-organized and immobilized in a manner where the ATP binding is more favored.