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;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.
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11588/892853
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