Isothermal titration calorimetry studies of aptamer-small molecule interactions: practicalities and pitfalls

PROTOCOL/METHOD

OpenAccess

ISSN: 2514-3247
Aptamers 
(2018), Vol 2, 45-51

Published online: 12 June 2018

Full Text (PDF ~452kb) | (PubMed Central Record HTML) | (PubMed) | (References)

Sladjana Slavkovic and Philip E Johnson*

Department of Chemistry and Centre for Research on Biomolecular Interactions, York University, Toronto, Ontario, Canada, M2R 1A1

*Correspondence to: Philip Johnson, Email: pjohnson@yorku.ca, Tel: 1 416 736 2100 x33119


Received: 31 January 2018 | Revised: 09 June 2018 | Accepted: 11 June 2018


© Copyright The Author(s). This is an open access article, published under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0). This license permits non-commercial use, distribution and reproduction of this article, provided the original work is appropriately acknowledged, with correct citation details.


ABSTRACT

Isothermal titration calorimetry (ITC) is a powerful technique for studying binding interactions. From a single ITC experiment it is possible to quantify the affinity and thermodynamics of a binding event. Here, we outline an experimental approach for performing ITC experiments with a focus on aptamer-small molecule interactions. We also discuss some common problems that can be encountered and how to resolve these issues.

KEYWORDS: Aptamers, isothermal titration calorimetry, binding thermodynamics


 

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