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. Author manuscript; available in PMC: 2014 Apr 22.
Published in final edited form as: Chemistry. 2013 Feb 28;19(17):5364–5374. doi: 10.1002/chem.201204070

Figure 7.

Figure 7

Competition of Man3 and 19F-Man3 for 250 μM 19F-Man3 in complex with 25 μM CVNmDB. A) Schematic representation of the competitive binding scenario. Cheng–Prusoff equation based on a competitive site binding model, where [19F-Man3] and [Man3] are the concentrations of the fluorinated and non-fluorinated ligand, and KDF the dissociation constants of 19F-Man3 for the glycan-binding site on domain A of CVNmDB. The data were fitted using the maximum increase in free 19F-Man3 resonance intensity upon Man3 addition, ΔImax, and kd the dissociation constant for Man3 binding as adjustable parameters. B) 19F-NMR spectra were recorded for 19F-Man3:CVNmDB:Man3 molar ratios of 10:1:0, 10:1:0.25, 10:1:0.5, 10:1:0.75, and 10:1:1. In the titration curve the bound fraction of Man3 is derived from the difference in signal intensity of the 19F-Man3 free signal ΔI=Ifree-I0 during the titration, with Ifree the intensity of the 19F-Man3 free signal at each point in the titration, and I0 the intensity of 19F-Man3 free signal at the beginning of the titration.