Cucurbit[6]uril host-guest interaction assisted N-terminal epitope imprinted particles for cytochrome c recognition prepared by reversible addition-fragmentation chain transfer strategy.

A novel strategy for cytochrome c selective recognition assisted with cucurbit[6]uril by host-guest interaction via N-terminal epitope imprinting and reversible addition-fragmentation chain transfer (RAFT) polymerization was developed. N-terminal nonapeptide of cytochrome c (GI-9) was used as the epitope template to achieve highly selective recognition of cytochrome c. As a common supramolecule in recent years, cucurbit[6]uril can encapsulate the butyrammonium group of lysine residue to capture the peptide and improve the corresponding spatial orientation by the host-guest interaction for GI-9 or cytochrome c recognition.