Protein recognition by synthetic materials is a challenging endeavour, since these materials must bind to a large relatively flat surface domain and recognize a unique distribution of amino acid residues of varying charge, size and shape.One of the most promising approaches is the application of molecular imprinting techniques.In our recent work, bovine serum albumin-imprinted monolithic columns were prepared and evaluated.The monolithic columns presented a large quantity of well-distributed macropores, which were suited to permit proteins in and out.The results indicated that the imprinted column could recognize the template protein from a mixture of proteins, which could not been accomplished by non-imprinted columns prepared in parallel.The recognition mechanism indicated that the formation of multiple hydrogen bonds and the template proteinscomplementary shape of the imprinting cavities created during the imprinting process provided specific recognition toward the template protein.