ABSTRACT
Besides mainstream, molecular imprinting based on man-made synthetic polymers or silica-imprinted materials, proteins too can be considered as building blocks to prepare artificial molecular recognition systems. The technique of bioimprinting is based on reversible changes in the three dimensional structure of a protein induced by noncovalent interactions with a ligand in mild denaturing conditions such as lyophilization or precipitation with a polar solvent. After these changes, a protein shows altered binding properties, with a reversal of enantioselectivity, enhancement of enzyme activity or de novo binding features. The principles of bioimprinting, nature of the protein and of the template, experimental tech niques (lyophilization or solvent precipitation) and some progress, such as interfacial bioimprinting, stabilization by cross-linking and polysaccharide-based bioimprinting are dis cussed referring to examples reported in literature for enzymes and binding proteins.
