Journal
ANALYTICAL METHODS
Volume 11, Issue 24, Pages 3061-3065Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c9ay00861f
Keywords
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Funding
- National Natural Science Foundation of China [U1507203, 21405166, 21676273]
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A surface plasmon resonance (SPR) competition experiment in a steady state was developed to determine the binding dissociation constants between a protein and its DNA aptamers. The affinities of a large set of trypsin aptamers selected by magnetic beads-systematic evolution of ligands by exponential enrichment (MB-SELEX) and capillary electrophoresis (CE-SELEX) are obtained only on one single chip. A large number of chips and a considerable amount of time are saved compared with a typical SPR experiment. Additionally, this approach does not require prior knowledge of parameters, such as on or off rates, using a nonlinear fitting with a known dissociation constant and the protein concentration as input. Knowledge on the specificity of protein-aptamer interaction is also obtained by the SPR competition experiment.
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