Figure 6. Inhibition of rNav1.8 by... | Rockefeller University Press

Figure 6.

$Figure 6. Inhibition of rNav1.8 by ProTx-I. (A) Inhibition of rNav1.8 currents by 100 nM ProTx-I at +15 mV (holding voltage was −90 mV). (B and C) Current–voltage relationship (B) and deduced G-V relationship (C) of rNav1.8 before (black) and after (green) the application of 100 nM ProTx-I. n = 3–5, and error bars represent SEM. (D) Concentration dependence for ProTx-I inhibition of rNav1.8 plotted as fraction unbound (Fu) measured at negative voltages. Dotted line is a fit of the Hill equation to the data (IC50 = 10.9 ± 0.5 nM; slope = 1.3 ± 0.1). Solid line is a fit with a three-binding site model (Kd = 45.1 ± 2.7 nM). See Materials and methods for more information. (E) Effect of 100 nM ProTx-I on Kv2.1 channels containing paddle motifs from rNav1.8. Normalized tail current voltage–activation relationships are shown before and after the application of the toxin. n = 4, and error bars represent SEM.$

Inhibition of rNav1.8 by ProTx-I. (A) Inhibition of rNav1.8 currents by 100 nM ProTx-I at +15 mV (holding voltage was −90 mV). (B and C) Current–voltage relationship (B) and deduced G-V relationship (C) of rNav1.8 before (black) and after (green) the application of 100 nM ProTx-I. n = 3–5, and error bars represent SEM. (D) Concentration dependence for ProTx-I inhibition of rNav1.8 plotted as fraction unbound (Fu) measured at negative voltages. Dotted line is a fit of the Hill equation to the data (IC₅₀ = 10.9 ± 0.5 nM; slope = 1.3 ± 0.1). Solid line is a fit with a three-binding site model (K_d = 45.1 ± 2.7 nM). See Materials and methods for more information. (E) Effect of 100 nM ProTx-I on Kv2.1 channels containing paddle motifs from rNav1.8. Normalized tail current voltage–activation relationships are shown before and after the application of the toxin. n = 4, and error bars represent SEM.