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Characteristics
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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.
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