Engineering a structure switching mechanism into a steroid-binding aptamer and hydrodynamic analysis of the ligand binding mechanism.

@article{Reinstein2011EngineeringAS,
  title={Engineering a structure switching mechanism into a steroid-binding aptamer and hydrodynamic analysis of the ligand binding mechanism.},
  author={Oren Reinstein and Miguel A.D. Neves and Makbul Saad and Sherry N Boodram and Stephanie Lombardo and Simone A. Beckham and Jason James Brouwer and Gerald F Audette and Patrick D. Groves and Matthew C. J. Wilce and Philip Edward Johnson},
  journal={Biochemistry},
  year={2011},
  volume={50 43},
  pages={
          9368-76
        }
}
The steroid binding mechanism of a DNA aptamer was studied using isothermal titration calorimetry (ITC), NMR spectroscopy, quasi-elastic light scattering (QELS), and small-angle X-ray spectroscopy (SAXS). Binding affinity determination of a series of steroid-binding aptamers derived from a parent cocaine-binding aptamer demonstrates that substituting a GA base pair with a GC base pair governs the switch in binding specificity from cocaine to the steroid deoxycholic acid (DCA). Binding of DCA to… CONTINUE READING
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