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Abstract: Selective recognition of proteins by synthetic molecularly imprinted polymers is one of the interesting topics in biosciences. Carnosine (β-alanyl-l-histidine) and related histidine containing peptides are distributed in a wide range of tissues in vertebrate organisms. These peptides have been extensively studied because of their important physiological properties besides their metal chelation property. In this study, preparation of carnosine specific imprinted polymers (MIPs) for the recognition of imidazole containing peptides with and without copper ion is reported. Carnosine and copper-carnosine complex were employed as template molecules where 4-vinylpyridine and ethylenglycol dimethacrylate were chosen as monomer and crosslinker, respectively. The selectivity and binding studies of copper-carnosine imprinted polymer showed high selectivity toward both carnosine (template peptide) and the cupric ion. The selectivity of copper-carnosine imprinted polymer was 65% and carnosine imprinted polymer was approximately 40%. These results indicate that specific recognition of carnosine is depending on the basis of metal coordination
Template and target information: peptide, carnosine, β-alanyl-l-histidine, carnosine-copper complex, copper-carnosine
Author keywords: Carnosine, Metal-ion imprinting, copper, molecular recognition, selectivity