Cucurbit[6]uril-mediated reversible addition-fragmentation chain transfer polymerization of temperature-sensitive epitope imprinted particles for dual-mechanism recognition of cytochrome c

A novel strategy for cytochrome c (Cyt c) selective recognition with the epitope imprinting and host-guest interaction dual-mechanism recognition was developed via reversible addition-fragmentation chain transfer polymerization regulated by a cucurbit[6]uril-functionalized chain transfer agent (CB[6]-CPAD). CB[6]-CPAD attaches to N-terminal epitope GI-9 through host-guest interactions between cucurbit[6]uril and lysine-residue. It regulates the imprinted polymers via the modulatory effect of disulfide esters, thereby enhancing the accessibility of cucurbit[6]uril within the imprinted sites. After polymerization and template removal, the imprinted particles exhibited well binding affinity for GI-9 (8.40 mg⋅g -1 , IF = 1.62) and Cyt c (11.32 mg⋅g -1 , IF = 1.62) at 45°C and obvious selective recognition of Cyt c over other proteins with a significantly higher IF, which were driven by the combination of molecular imprinting and host-guest interactions. It indicated that the construction of temperature-sensitive dual-mechanism recognition combining epitope imprinting and host-guest interactions can effectively achieve selective recognition of the target protein.