Appearance: White lyophilized solid
AA sequence: Ala-Ala-Pro-Cys4-Phe-Cys6-Ser-Gly-Lys-Pro-Gly-Arg-Gly-Asp-Leu-Trp-Ile-Leu-Arg-Gly-Thr-Cys22-Pro-Gly-Gly-Tyr-Gly-Tyr-Thr-Ser-Asn-Cys32-Tyr-Lys-Trp-Pro-Asn-Ile-Cys39-Cys40-Tyr-Pro-His-OH
Disulfide bonds: Cys4-Cys39, Cys6-Cys32, Cys22-Cys40
Length (aa): 43
BDS-1 is a 43 amino acid peptide which was originally isolated from the venom of the sea anemona Anemonia Viridis. BDS-1 was originally described as a highly selective blocker of the rapidly inactivating voltage-gated potassium channel Kv3.4/ KCNC4, a potential therapeutic target for major CNS disorders (Alzheimer and Parkinson diseases). The toxin acts as gating modifiers, mainly by shifting the voltage-dependence of activation. Channel block occurs with high affinity (IC50 of 43 nM) and is rapid and reversible. BDS-1 also blocks the Kv3.1 and Kv3.2 channels albeit with a lower affinity (>200 nM). Finally, in a more recent study, it was demonstrated that BDS-1 is a selective gating activator of the Nav1.7 channel subtype, an important target for pain management. On the human isoform, modulation is witnessed by a drastic slowing of channel inactivation which occurs with an IC50 of 3 nM.