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Studying binding affinities of aptamers to diverse targets with a large molecular size range using MicroScale Thermophoresis
EP23884
Poster Title: Studying binding affinities of aptamers to diverse targets with a large molecular size range using MicroScale Thermophoresis
Submitted on 08 Mar 2016
Author(s): Clemens Entzian, Corinna Kuttenberger, Tobias Mauerer, Lukas Kniep, Estefanía Muciño, Dr. Thomas Schubert
Affiliations: 2bind GmbH
This poster was presented at 3rd Aptamers Oxford Congress, UK
Poster Views: 1,854
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Poster Information
Abstract: Aptamers have become important tools in research, diagnostics and therapeutics. Biophysical characterization of the binding parameters of aptamers is essential for the well functioning of these in diverse applications. MicroScale Thermophoresis (MST) is a rapid and precise method to analyze aptamer-target interactions in solution at microliter scale. The basis of this technology is a physical effect referred to as thermophoresis, which describes the directed movement of molecules through temperature gradients. The thermophoretic properties of a molecule depend besides - on its size - also on charge and hydration shell. Upon binding of a ligand at least one of these parameters is altered, which enables MST to analyze virtually any aptamer target interaction independent of the target size. We present the characterization of multiple aptamers to various targets from small molecules to large protein complexes following a specific protocol designed for the quantitative study of binding parameters of aptamer–target interactions in a highly sensitive cost- and time-efficient performance.Summary: MicroScale Thermophoresis is a rapid and precise method to analyze aptamer-target interactions in solution at microliter scale. Upon binding of a ligand at least one of these parameters is altered, which enables MicroScale Thermophoresis to analyze virtually any aptamer target interaction independent of the target size. We present the characterization of multiple aptamers to various targets from small molecules to large protein complexes.References: Alsager, Omar A.; Kumar, Shalen; Zhu, Bicheng; Travas-Sejdic, Jadranka; McNatty, Kenneth P.; Hodgkiss, Justin M. (2015): Ultrasensitive Colorimetric Detection of 17β-Estradiol. The Effect of Shortening DNA Aptamer Sequences. In Anal. Chem. 87 (8), pp. 4201–4209. DOI: 10.1021/acs.analchem.5b00335.

Breitsprecher, Dennis; Schlinck, Nina; Witte, David; Duhr, Stefan; Baaske, Philipp; Schubert, Thomas (2016): Aptamer Binding Studies Using MicroScale Thermophoresis. In Günter Mayer (Ed.): Nucleic acid aptamers. Selection, characterization, and application / edited by Günter Mayer, vol. 1380. New York, NY: Springer New York (Methods in Molecular Biology, 1380), pp. 99–111.

Entzian, Clemens; Schubert, Thomas (2015): Studying small molecule–aptamer interactions using MicroScale Thermophoresis (MST). In Methods. DOI: 10.1016/j.ymeth.2015.08.023.

Lennarz, Sabine; Heider, Elena; Blind, Michael; Mayer, Günter (2015): An Aptamer to the MAP Kinase Insert Region. In ACS Chem
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