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Updated: Jan 27, 2026

Mapping the Binding Site of an Aptamer on ATP Using MicroScale Thermophoresis
Published on: January 7, 2017
Stability Is Not Everything: The Case of the Cyclisation of a Thrombin-Binding Aptamer
Claudia Riccardi1, Albert Meyer2, Jean-Jacques Vasseur2
1Department of Chemical Sciences, University of Naples Federico II, Via Cintia 21, 80126, Napoli, Italy.
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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