Overview
Disulfide bonds location - Cys1-Cys16, Cys8-Cys19, Cys15-Cys26
- Silmara, R. S. et al. (2018) Sci. Rep., 8, 13397.
Alomone Labs ω-Conotoxin MoVIA inhibits CaV2.2 channel currents heterologously expressed in Xenopus oocytes.A. Representative time course of ω-Conotoxin MoVIA (#STC-150) inhibition of CaV2.2 (α1B + α2δ1 + β1) channels current. Membrane potential was held at -100 mV, current was elicited by a 100 ms voltage ramp to +60 mV every 10 sec, and inhibited by 1 µM ω-Conotoxin MoVIA (green).
B. Superimposed traces of CaV2.2 currents after application of control (black) and of 1 µM ω-Conotoxin MoVIA (green), taken from the recording in A.
- Silmara, R. S. et al. (2018) Sci. Rep., 8, 13397.
- Adams, D.J. and Berecki, G. (2013) Biochim. Biophys. Acta. 1828, 1619.
ω-Conotoxin MoVIA (MoVIA) is a 29 amino acid peptidyl toxin originally isolated from the venom of the western Pacific vermivorous (worm-hunting) cone snail, Conus moncuri. MoVIA is a specific and potent blocker of mammalian N-type voltage-gated Ca2+ channels (CaV2.2)1.
MoVIA has an arginine at position 13 instead of a tyrosine, which has been previously shown to be functionally critical for the potent Cav2.2 inhibitor activity of ω-conotoxins including ω-Conotoxin MVIIA (#C-670) and ω-Conotoxin GVIA (#C-300) from piscivorous (fish-hunting) species1.
CaV2.2 are predominantly expressed in nerve terminals and are involved in the regulation of neuronal excitability and nociceptive signaling. These channels are multifunctional and play important roles in the transduction of acute and chronic pain perception. They are able to transduce electrical activity into other cellular functions, regulate calcium homeostasis and process pain information. Since ω-conotoxins selectively inhibit Cav2.2 in nociceptors, they are considered attractive molecules for drug design2.
Omega-conotoxin MoIVA (#STC-150) is a highly pure, synthetic, and biologically active peptide toxin.
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