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.
J. F. Keijzer, J. Firet and B. Albada, Chem. Commun., 2021, 57, 12960 DOI: 10.1039/D1CC05446E
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