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. Author manuscript; available in PMC: 2021 Oct 22.
Published in final edited form as: J Med Chem. 2020 Oct 15;63(20):11522–11547. doi: 10.1021/acs.jmedchem.0c00531

Figure 7.

Figure 7.

Compound 21a disrupts FGF14 binding to the CTD of Nav1.6 as determined by SPR. Increasing concentrations of FGF14 (15 – 1500 nM) were flown over Nav1.6 protein bound to CM5 chips. Association and dissociation times for each sample were held at 120 and 150 s, respectively. Kinetic analysis of each ligand/analyte interaction was obtained by fitting the response data to the simplest Langmuir 1:1 interaction model (KD = koff/kon). Representative binding sensorgrams (left) and steady-state saturation plots (right) are shown for each compound against each protein. The resulting equilibrium dissociation constants (KD), as well as kinetic association (kon) and dissociation (koff) rates are provided in Table 7. Steady-state saturation plot for comparison of FGF14 alone (WT, black) versus FGF14 in complex with 21a (10 μM; blue) binding to Nav1.6 with response units (RU) relative to the maximal binding response of FGF14 alone.