With the aim of developing a new approach to obtain improved aptamers, a cyclic thrombin-binding aptamer (TBA) analogue (cycTBA) has been prepared by exploiting a copper(I)-assisted azide-alkyne cycloaddition. The markedly increased serum resistance and exceptional thermal stability of the G-quadruplex versus TBA were associated with halved thrombin inhibition, which suggested that some flexibility in the TBA structure was necessary for protein recognition.
Stability Is Not Everything: The Case of the Cyclisation of a Thrombin-Binding Aptamer / Riccardi, Claudia; Meyer, Albert; Vasseur, Jean-Jacques; Russo Krauss, Irene; Paduano, Luigi; Oliva, Rosario; Petraccone, Luigi; Morvan, François; Montesarchio, Daniela. - In: CHEMBIOCHEM. - ISSN 1439-7633. - 20:14(2019), pp. 1789-1794. [10.1002/cbic.201900045]
Stability Is Not Everything: The Case of the Cyclisation of a Thrombin-Binding Aptamer
Riccardi, Claudia;Russo Krauss, Irene;Oliva, Rosario;Petraccone, Luigi;Montesarchio, Daniela
2019
Abstract
With the aim of developing a new approach to obtain improved aptamers, a cyclic thrombin-binding aptamer (TBA) analogue (cycTBA) has been prepared by exploiting a copper(I)-assisted azide-alkyne cycloaddition. The markedly increased serum resistance and exceptional thermal stability of the G-quadruplex versus TBA were associated with halved thrombin inhibition, which suggested that some flexibility in the TBA structure was necessary for protein recognition.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
