Abstract
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 language | English (US) |
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Pages (from-to) | 69-75 |
Number of pages | 7 |
Journal | International Journal of Biological Macromolecules |
Volume | 57 |
DOIs | |
State | Published - Jun 2013 |
Keywords
- Aptamer
- Fluorescence anisotropy
- Isothermal titration calorimetry
- Vascular endothelial growth factor
ASJC Scopus subject areas
- Structural Biology
- Biochemistry
- Molecular Biology
- Economics and Econometrics
- General Energy