With extensive research in molecular imprinting these years, remarkable progress has been made in the areas ranging from separation, sensing to biomedical applications. Recently, Molecularly imprinted polymers (MIPs), acting as alternatives to antibodies and biological receptors, extend its recognition species to biomolecules. However, the imprinting of larger molecules like proteins is still a challenge, due to their complex chemical nature, conformational flexibility and the heterogeneous and ineffective binding sites formed after polymerization.
In this study, hydrazone bond-oriented surface imprinting strategy was established for synthesizing MIPs with highly ordered and oriented binding sites. Cytochrome C, an essential component of the electron transport chain in mitochondrion, was selected as the model target protein. Hyrazide functionalized C-terminal peptide fragment of cytochrome C was used as the template and immobilized on the surface of Fe3O4 magnetic core via hydrazone bond. After controllable surface polymerization in tetraethyl orthosilicate (TEOS), a hydrophilic MIP layer was fabricated. The reversible hydrazone bond was cleaved under acidic aqueous solution and the peptide templates were removed. The hydrazone bond oriented MIPs revealed high specific recognition towards cytochrome C and its C-terminal peptide fragment. Benefiting from the homogeneity of the oriented imprinted sites, fast recognition kinetics and high selectivity of MIPs were achieved. This hydrazone bond-oriented surface imprinting approach will provide promising application in molecularly imprinting of biomolecules.
Reference
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[5] Financial supports from NNSFC are appreciated.