Maurotoxin

Maurotoxin. Maurotoxin (MTX) is a 34 amino acid long toxin, isolated from the venom of the scorpion Scorpio Maurus palmatus, and is classified as alpha-KTx6.2 scorpion toxin family, having four disulfide bridges.

MTX activity was extensively assayed on a large array of K\\^+\\ channels, including K\\_ca\\ (K\\_ca\\1.1, K\\_ca\\2.1, K\\_ca\\2.2, K\\_ca\\3.1), K_v1 (K\\_v\\1.1, K\\_v\\1.2 and K\\_v\\1.3) and Shaker B K\\^+\\ currents.
MTX inhibits the binding of \\_125\\I-Apamin and \\_125\\I-Kaliotoxin to rat brain synaptosomal membranes with an IC₅₀ of 5 nM and 30 pM, respectively.

Furthermore, MTX blocks KCNA1 (K\\_V\\1.1), KCNA2 (K\\_V\\1.2) and KCNA3 (K\\_V\\1.3) expressed in Xenopus oocyes with an IC₅₀ of 45 nM, 0.8 nM, and 180 nM, respectively.
Maurotoxin blocks Shaker-B K\\^+\\ current with an IC₅₀ of 2 nM. In contrast to previous reports, MTX was recently shown to have no effect on K\\_ca\\1.1, K\\_ca\\2.1 and K\\_ca\\2.2 small conductance K\\_ca\\ channels up to 300 nM in physiologically relevant ionic strength buffers, but rather produces a high and specific block towards K\\_ca\\3.1 (IK\\_ca\\1, SK4) and KCNA2 (K\\_V\\1.2) with IC₅₀ of 1 nM and 0.1 nM, respectively.
Furthermore, MTX was shown to block Gardos channel in human red blood cells and to inhibit the K\\_ca\\ in activated human T-lymphocytes without affecting the voltage-gated K\\^+\\ current encoded by KCNA3. Moreover, MTX inhibition was shown to be pH-dependent.

In conclusion, Maurotoxin seems to be a very potent blocker of both K\\_Ca\\3.1 and K\\_v\\1.2 channels.

Ion Channel Modulators; K\\^+\\ Channel Blockers

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