Jump to main content
Jump to site search

Issue 24, 2019
Previous Article Next Article

Affinity analysis between trypsin and aptamers using surface plasmon resonance competition experiments in a steady state

Author affiliations

Abstract

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.

Graphical abstract: Affinity analysis between trypsin and aptamers using surface plasmon resonance competition experiments in a steady state

Back to tab navigation

Publication details

The article was received on 24 Apr 2019, accepted on 10 May 2019 and first published on 10 May 2019


Article type: Communication
DOI: 10.1039/C9AY00861F
Anal. Methods, 2019,11, 3061-3065

  •   Request permissions

    Affinity analysis between trypsin and aptamers using surface plasmon resonance competition experiments in a steady state

    Y. Fa, M. Guan, H. Zhao, F. Li and H. Liu, Anal. Methods, 2019, 11, 3061
    DOI: 10.1039/C9AY00861F

Search articles by author

Spotlight

Advertisements