BmP02
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BmP02, also known as α-KTx 9.1 or Bmkk(6), is a toxin from the Buthus martensi Karsch (BmK) scorpion. The toxin acts on potassium channels, blocking Kv1.3 and slowing the deactivation of Kv4.2. BmP02 is not toxic to humans or mice.
BmP02, also known as α-KTx 9.1 or Bmkk(6), is a toxin from the Buthus martensi Karsch (BmK) scorpion. The toxin acts on potassium channels, blocking Kv1.3 and slowing the deactivation of Kv4.2. BmP02 is not toxic to humans or mice. BmP02 targets potassium channels. Its activity has been shown in Kv1.1-Kv1.3, Kv4.2, Shaker-IR (Inactivation Removed) type, and SKCa. BmP02 blocks Kv1.1-Kv1.3 with nanomolar affinity but has no effect on Kv1.4 isoform of the channel. Kv1.3 (IC50 = 7 ± 0.6 nm) and Kv4.2 (EC50 = 845 nM) channels are the most sensitive targets to this toxin.
SKCa
SKCa channel can be found in the brain. It has been experimentally shown that BmP02 can bind to SKCa with micromolar affinity. However, unlike BmP05, BmP02 does not generate toxic effects in mice. This loss of toxicity has been ascribed to the differential coupling of the disulfide bridge between BmP05 and BmP02. This lowers the affinity of BmP02 for the SKCa channel and removes its pharmacological effect. Furthermore, it has been shown that after intracerebroventricular injection in mice it could very well compete to binding to the SKCa channel with the toxin iodinated apamin.
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