Site-selective and inducible acylation of thrombin using aptamer-catalyst conjugates

Two acyl-transfer catalysts were conjugated to thrombin-binding DNA aptamers to acylate thrombin. Modification occurred site-selectively on Lys (>Ser) residues proximal to the respective aptamer-thrombin interface, was selective for thrombin in the presence of other proteins, and the activity of both DNA-catalysts could be controlled by an external trigger. Functionalizing a protein-binding aptamer with an acylation catalyst leads to site-selective modification of the target protein in proximity to the aptamer-protein interface. This protein modification can be switched ON or OFF by an external trigger.