- Diochot, S. et al. (1998) J. Biol. Chem. 273, 6744.
- BDS-II inhibits KV3.4 channels heterologously expressed in Xenopus oocytes.Left: Example traces before (red) and during (black) bath perfusion of 1 µM BDS-II (#B-450). Holding potential was -100 mV, test potential to 0 mV (100 ms) was delivered every 10 seconds. Recordings were made while perfusing ND 96 Buffer. Right: Time course for the experiment shown on the left. The vertical bar indicates the period of BDS-II perfusion.
- Alomone Labs BDS-II inhibits NaV1.7 channels stably expressed in HEK 293 cells.A. Time course of BDS-II (#B-450) action on NaV1.7 currents. Current amplitudes were plotted as a function of time. Membrane potential was held at -100 mV and cells were stimulated by a 20 ms voltage step to -20 mV. 100 nM BDS-II was perfused as indicated by the bar (green) for 80 sec. B. Superimposed examples of NaV1.7 channel current in the absence (control) and presence of 100 nM BDS-II (taken from the experiment in A).
BDS-II is a 43 amino acid peptidyl toxin isolated from the sea anemone Anemonia sulcata venom. BDS-II was shown to be a specific KV3.4 blocker. BDS-II blocked 70% of the KV3.4 current in COS-transfected cells at a concentration of 2.8 µM. The blocking effect was rapid, direct and reversible1. Recently it was shown that BDS-II blocks other KV3 channels with similar potencies.2
The closely related BDS-I was shown to modulate voltage-gated Na+ channels. It enhanced TTX-sensitive Na+ channels (highly effective on NaV1.7 channels), and weakly inhibited TTX-resistant NaV channels3. As such, we showed that BDS-II also potently inhibits NaV1.7 channels (see Our Bioassay).
BDS-II (#B-450) is a highly pure, natural, and biologically active peptide toxin.