Enzymes have an extraordinary ability to utilize aromatic interactions for molecular recognition and catalysis. We here report molecularly imprinted nanoparticle receptors. The aromatic "wall" material in the imprinted binding site is used to enhance the molecular recognition of aromatic guests that have similar charges, shapes, and sizes but differ in π-electron density. Additionally, aromatic interactions are employed to activate an electron-rich aryl leaving group on a glycoside, mimicking the nucleoside hydrolase of the parasite Trypanosoma vivax.