Analysis of Aptamer-Small Molecule Binding Interactions Using Isothermal Titration Calorimetry.

Publisher: Humana Press Country of Publication: United States NLM ID: 9214969 Publication Model: Print Cited Medium: Internet ISSN: 1940-6029 (Electronic) Linking ISSN: 10643745 NLM ISO Abbreviation: Methods Mol Biol Subsets: MEDLINE

Publication: Totowa, NJ : Humana Press
Original Publication: Clifton, N.J. : Humana Press,

Aptamers, Nucleotide*/chemistry ; Cocaine*/chemistry ; Nucleic Acids*/metabolism; Calorimetry/methods ; Ligands ; Protein Binding ; Quinine/chemistry ; Thermodynamics

Isothermal titration calorimetry (ITC) is a technique where the heat given off, or absorbed, during a binding event is measured and used to determine the binding thermodynamics and affinity associated with binding. This protocol focuses on ITC applications for studying aptamer interactions with small molecule ligands where ITC has the advantage of being a label-free solution-based technique. The limitation of ITC using a relatively large amount of material compared to other analytical techniques is not applicable here as large amounts of nucleic acids, especially DNA, can be readily obtained. In this chapter we describe how to use ITC methods to measure the thermodynamics and affinity of binding using the interaction of quinine with a DNA cocaine-binding aptamer as an example.
(© 2023. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.)

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Keywords: Aptamers; Isothermal titration calorimetry; Ligand binding; Small molecule interactions

0 (Aptamers, Nucleotide)
0 (Ligands)
0 (Nucleic Acids)
A7V27PHC7A (Quinine)
I5Y540LHVR (Cocaine)

Date Created: 20220926 Date Completed: 20220928 Latest Revision: 20220929

20240829

10.1007/978-1-0716-2695-5_8

36156777