EN
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.