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; Meyer, Albert; Vasseur, Jean-Jacques; Russo Krauss, Irene; Paduano, Luigi; Oliva, Rosario; Petraccone, Luigi; Morvan, Francois; Montesarchio, Daniela. - In: CHEMBIOCHEM. - ISSN 1439-4227. - 20:14(2019), pp. 1789-1794. [10.1002/cbic.201900045]
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.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
