| Chapter title |
Nucleic Acid Aptamers
|
|---|---|
| Chapter number | 8 |
| Book title |
Nucleic Acid Aptamers
|
| Published in |
Methods in molecular biology, January 2016
|
| DOI | 10.1007/978-1-4939-3197-2_8 |
| Pubmed ID | |
| Book ISBNs |
978-1-4939-3196-5, 978-1-4939-3197-2
|
| Authors |
Breitsprecher, Dennis, Schlinck, Nina, Witte, David, Duhr, Stefan, Baaske, Philipp, Schubert, Thomas, Dennis Breitsprecher, Nina Schlinck, David Witte, Stefan Duhr, Philipp Baaske, Thomas Schubert |
| Abstract |
The characterization and development of highly specific aptamers requires the analysis of the interaction strength between aptamer and target. MicroScale Thermophoresis (MST) is a rapid and precise method to quantify biomolecular 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 on its size, charge, and hydration shell. Since at least one of these parameters is altered upon binding of a ligand, this method can be used to analyze virtually any biomolecular interaction in any buffer or complex bioliquid. This section provides a detailed protocol describing how MST is used to obtain quantitative binding parameters for aptamer-target interactions. The two DNA-aptamers HD1 and HD22, which are targeted against human thrombin, are used as model systems to demonstrate a rapid and straightforward screening approach to determine optimal buffer conditions. |
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