Covalent Imprinting and Covalent Rebinding of Benzyl Mercaptan: Towards a Facile Detection of Proteins

A novel synthetic benzyl mercaptan receptor with tunable binding sites was prepared by covalent imprinting using a disulfide linkage which was cleaved and able to recognize the benzyl mercaptan templates by reforming disulfide bonds through thiol–disulfide exchange. These covalently molecularly imprinted polymers were prepared using ambient ultraviolet radiation in comparison with thermal cross-linking at 80°C. Subsequent reduction of disulfide bonds resulted in the formation of surface thiol groups, followed by modification forming sodium thiolate as covalent binding sites. Covalent imprinting was found to be complementary in size, spatial effects, and chemical reactivity to benzyl mercaptan. This covalent rebinding and other various guest molecules were prepared by reforming disulfide bonds at room temperature in protic solvents. The results showed that rapid covalent rebinding is more efficient than other noncovalent interactions.