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Updated: Mar 30, 2026

Mapping the Binding Site of an Aptamer on ATP Using MicroScale Thermophoresis

Mapping the Binding Site of an Aptamer on ATP Using MicroScale Thermophoresis

Published on: January 7, 2017

Aptamer Binding Studies Using MicroScale Thermophoresis.

Dennis Breitsprecher¹, Nina Schlinck¹, David Witte¹

¹NanoTemper Technologies GmbH, Flößergasse 4, 81369, Munich, Germany.

Methods in Molecular Biology (Clifton, N.J.)

|November 11, 2015

Summary

This summary is machine-generated.

MicroScale Thermophoresis (MST) quantifies aptamer-target binding strength, crucial for developing specific aptamers. This method analyzes molecular interactions in solution using thermophoresis, aiding in optimizing buffer conditions for aptamer selection.

Keywords:

Aptamer–target interactions Binding assay Dissociation constant Interaction affinity MicroScale Thermophoresis

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Last Updated: Mar 30, 2026

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Published on: August 15, 2013

Area of Science:

Biochemistry
Molecular Biology
Biophysics

Background:

Characterizing aptamer-target interactions is essential for aptamer development.
MicroScale Thermophoresis (MST) is a precise technique for quantifying biomolecular interactions in solution.
Thermophoresis, the movement of molecules in a temperature gradient, forms the basis of MST.

Purpose of the Study:

To provide a detailed protocol for using MST to obtain quantitative binding parameters for aptamer-target interactions.
To demonstrate a rapid screening approach for determining optimal buffer conditions for aptamer selection.
To utilize DNA aptamers HD1 and HD22 targeting human thrombin as model systems.

Main Methods:

MicroScale Thermophoresis (MST) was employed to measure binding affinities.
Quantitative binding parameters were determined for aptamer-target interactions.
A screening approach was used to identify optimal buffer conditions.

Main Results:

MST successfully quantified the binding strength between aptamers and their targets.
The study demonstrated a straightforward method for optimizing buffer conditions for aptamer-target interactions.
Model aptamers HD1 and HD22 against human thrombin were analyzed.

Conclusions:

MST is a versatile and effective method for characterizing aptamer-target interactions.
The protocol facilitates the determination of quantitative binding parameters and optimal buffer conditions.
This approach supports the development of highly specific aptamers for various applications.