Methods for measuring aptamer-protein equilibria: A review

Research output: Contribution to journalShort surveypeer-review

118 Scopus citations

Abstract

Aptamers are single stranded DNA or RNA molecules that have been selected using in vitro techniques to bind target molecules with high affinity and selectivity, rivaling antibodies in many ways. In order to use aptamers in research and clinical applications, a thorough understanding of aptamer-target binding is necessary. In this article, we review methods for assessing aptamer-protein binding using separation based techniques such as dialysis, ultrafiltration, gel and capillary electrophoresis, and HPLC; as well as mixture based techniques such as fluorescence intensity and anisotropy, UV-vis absorption and circular dichroism, surface plasmon resonance, and isothermal titration calorimetry. For each method the principle, range of application and important features, such as sample consumption, experimental time and complexity, are summarized and compared.

Original languageEnglish (US)
Pages (from-to)9-18
Number of pages10
JournalAnalytica Chimica Acta
Volume686
Issue number1-2
DOIs
StatePublished - Feb 7 2011

Keywords

  • Aptamer
  • Dissociation constant
  • Equilibrium constant
  • Nucleic acids
  • Protein
  • SELEX

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