Abstract
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.
Original language | English |
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Pages (from-to) | 12960-12963 |
Number of pages | 4 |
Journal | Chemical Communications |
Volume | 57 |
Issue number | 96 |
DOIs | |
Publication status | Published - 14 Dec 2021 |