Aiming at novel approaches to obtain improved aptamers, we developed a cyclic TBA analogue (cycTBA) by exploiting a Cu(I)-assisted azide-alkyne cycloaddition. Its markedly increased serum resistance and exceptional thermal stability of its G-quadruplex vs. TBA were associated to halved thrombin inhibition, suggesting that some flexibility in TBA structure is necessary for protein recognition.

Stability is not everything the case of the cyclization of the thrombin binding aptamer

Riccardi, Claudia;Russo Krauss, Irene;Paduano, Luigi;Oliva, Rosario;Petraccone, Luigi;Montesarchio, Daniela
2019

Abstract

Aiming at novel approaches to obtain improved aptamers, we developed a cyclic TBA analogue (cycTBA) by exploiting a Cu(I)-assisted azide-alkyne cycloaddition. Its markedly increased serum resistance and exceptional thermal stability of its G-quadruplex vs. TBA were associated to halved thrombin inhibition, suggesting that some flexibility in TBA structure is necessary for protein recognition.
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11588/747267
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