Switching the recognition ability of a photoswitchable receptor towards phosphorylated anions

An azobenzene based photoswitchable macrocyclic receptor displays different binding affinities in its E and Z forms towards various phosphorylated coenzymes under physiological conditions with remarkable selectivity for ATP in the E -form and selectivity towards GTP in the photoisomerized Z -form. Linear discriminant analysis clearly separated the analytes using the E -form. An application of this method enabled monitoring the progress of enzymatic phosphorylation using a tyrosine kinase enzyme. Altering the recognition ability towards various phosphorylated anions using photoswitchable receptors that can be modulated by light is demonstrated.