Table 3.

Biophysical characterization of peptidomimetic binding to FGF14 and Nav1.6 by Surface Plasmon Resonance (SPR).

	FGF14			Nav1.6
Compound	KD a (µM)	kon (M−1 s−1)	koff (s−1)	KD a (µM)	kon (M−1 s−1)	koff (s−1)
12	2.98 ± 0.10 b	6.44 × 103	1.86 × 10−2	9.69 ± 0.34 e	4.29 × 103	4.23 × 10−2
17	14.3 ± 0.96 c	6.03 × 103	8.80 × 10−2	54.4 ± 10.2 f	9.01 × 103	7.83 × 10−2
19	6.49 ± 0.39 d	2.06 × 103	1.30 × 10−2	2.20 ± 0.08 g	6.65 × 103	1.50 × 10−2
22	>100	6.90 × 102	1.09 × 10−1	>100	7.30 × 102	1.30 × 10−1

^a The equilibrium dissociation constants (K_D) were derived from data shown in Figure 4. The K_D shown for each compound is an average of that calculated using the simplest Langmuir 1:1 interaction model (K_D = k_off/k_on, where K_D is the dissociation constant, and k_off and k_on are the first-order rate constants for the dissociation and association, respectively, of the protein:ligand complex) and the steady-state saturation model. ^b p < 0.005 compared to 17.^c p < 0.05 compared to 19. ^d p < 0.05 compared to 12. ^e p < 0.05 compared to 17. ^f p < 0.05 compared to 19. ^g p < 0.005 compared to 12.