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Abstract: Micro-contact imprinting has been used to form thin-film molecular imprints of ovalbumin (OVA) in polymers supported on glass slides. Thermocalorimetric data was used to optimise the choice of functional monomer and cross-linker to maximise selectivity and minimise non-specific recognition. A polymer comprising polyethyleneglycol 400 dimethacrylate (95ávol.%) and methacrylic acid (5ávol.%) showed both maximum recognition for OVA when made as a molecularly imprinted polymer (MIP), and minimal recognition when made as a non-imprinted, i.e. control polymer. OVA rebinding to the molecularly imprinted polymer, from a buffered 2áÁM OVA solution, was 1.55áÎá10-á11ámol cm-á2, while the control polymer showed 10-fold less re-binding, i.e. 0.154áÎá10-á11ámol cm-á2. Experiments in which human serum albumin (HSA), conalbumin, ovomucoid or lysozyme, were re-bound to the polymers, either as single proteins or in competition with OVA, showed them to have low affinity for the polymer formulation used. Of the competing proteins examined, in non-competitive binding experiments, HSA showed the greatest affinity 0.45áÎá10-á11ámol cm-á2 for the OVA imprinted polymer. In two protein competition experiments, i.e. with OVA and a competing protein present at equal concentrations (2áÁM), OVA binding to the OVA imprinted polymer was in all cases significantly greater than that of the competitor
Template and target information: protein, ovalbumin, OVA
Author keywords: molecular imprinting, Ovalbumin, protein, Synthetic molecular recognition, Microcontact