AI Article Synopsis
- Researchers developed a method to enhance the function of a DNA aptamer that binds to thrombin, which is important for regulating blood clotting.
- By creating and incorporating amino acid-nucleic acid hybrids (ANHs) into the aptamer, they observed a significant increase in its anticoagulation activity—up to three times better than the original aptamer.
- The study utilized advanced experimental techniques to assess the binding affinity of the modified aptamer, showcasing a systematic approach to designing improved aptamers based on amino acid properties.
Article Abstract
Chemical modifications of innate DNA/RNA aptamers facilitate the improvement of their function. Herein, we report our modular strategy to manipulate a thrombin-binding DNA aptamer (TBA) to improve its anticoagulation activity and binding affinity. A set of amino acid conjugates, termed amino acid-nucleic acid hybrids or ANHs, was synthesized and incorporated into a TBA loop sequences. We found that substitutions with hydrophobic amino acids in the loop region possessed significantly enhanced antithrombin activity, up to 3-fold higher than the native TBA. We investigated the correlations between thrombin-binding affinity and the features of our amino-acid conjugates using experimental techniques including circular dichroism spectroscopy, surface plasmon resonance assay, and molecular modeling. The present study demonstrates a systematic approach to aptamer design based on amino-acid characteristics, allowing the development of advanced aptamers.
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| http://dx.doi.org/10.1021/acsbiomaterials.1c00060 | DOI Listing |
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