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

Journal 2025 · IF 6.1 · 发表于 2025 年 1 月 10 日
作者: Nurimangul Muntiza,Wenbin Zhang,Yuzeng Li,Wenquan Ji,Jin Zhao,Hongfeng Zhang,Qinran Li,Qiliang Deng,Donglan Sun,Tianjun Liu
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摘要

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. After cucurbit[6]uril modification and epitope immobilization, the imprinted polymer was synthesized by RAFT polymerization with 2-dodecylsulfanylcarbothioylsulfanyl-2-methylpropanoic acid as chain transfer agent. After template removal, the obtained imprinted particles showed good binding ability to GI-9 (20.28 mg g −1 , IF = 4.11) and cytochrome c (36.12 mg g −1 , IF = 3.91). With the successive addition of cucurbit[6]uril and RAFT agent, the step-by-step improvement of the IF for cytochrome c recognition further illustrated the effects of supramolecular host-guest interaction and regulation of imprinted polymer chain. The imprinted polymers showed obvious advantages for cytochrome c recognition compared to competitive proteins and had good reusability with the repeated reproduction rate 80.8 % after five cycles of adsorption and desorption. Furthermore, the selective recognition for cytochrome c in adult bovine serum proved its potentiality to be applied in practical samples. All these results demonstrated that the combination of epitope imprinting, cucurbit[6]uril host-guest interaction and RAFT strategy presented an efficient new feasible control method for protein recognition with good selectivity, stability and reusability.

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