Biophysical characterization of VEGF-aHt DNA aptamer interactions

Indhu Kanakaraj, Wen Hsiang Chen, Mohan Poongavanam, Sagar Dhamane, Loren J. Stagg, John E. Ladbury, Katerina Kourentzi, Ulrich Strych, Richard C. Willson

Research output: Contribution to journalArticlepeer-review

9 Scopus citations


The binding of the well-studied DNA aptamer aHt (5'-ATACCAGTCTATTCAATTGGGCCCGTCCGTAT GGTGGGTGTGCTGGCCAG-3'), which has been demonstrated to recognize human vascular endothelial growth factor (VEGF165) to recombinant VEGF was characterized using fluorescence anisotropy, isothermal titration calorimetry and analytical ultracentrifugation. The negatively-charged DNA aptamer is selective for VEGF and does not recognize positively-charged hen egg lysozyme, or bovine serum albumin. In contrast to the VEGF association of the previously-described aV DNA aptamer, where the binding is enthalpically driven and sequence-specific, the binding of the aHt aptamer to VEGF is entropically-driven and not abolished by scrambling of the sequence.

Original languageEnglish (US)
Pages (from-to)69-75
Number of pages7
JournalInternational Journal of Biological Macromolecules
StatePublished - Jun 2013


  • Aptamer
  • Fluorescence anisotropy
  • Isothermal titration calorimetry
  • Vascular endothelial growth factor

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Structural Biology


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