Journal
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
Volume 57, Issue -, Pages 69-75Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.ijbiomac.2013.02.016
Keywords
Aptamer; Vascular endothelial growth factor; Fluorescence anisotropy; Isothermal titration calorimetry
Funding
- Welch foundation [E-1264]
- NASA
- NSF
- Directorate For Engineering
- Div Of Chem, Bioeng, Env, & Transp Sys [1133965] Funding Source: National Science Foundation
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The binding of the well-studied DNA aptamer aHt (5'-ATACCAGTCTATTCAATTGGGCCCGTCCGTATGGTGGGTGTGCTGGCCAG-3'), which has been demonstrated to recognize human vascular endothelial growth factor (VEGF(165)) 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. (C) 2013 Published by Elsevier B.V.
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