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- McArdle, J.J. et al. (1999) J. Pharmacol. Exp. Ther. 289, 543.
- Molles, B.E. et al. (2002) J. Biol. Chem. 277, 5433
- Alomone Labs Waglerin-I inhibits muscle embryonic α1/β1/γ/δ nAChR currents heterologously expressed in Xenopus oocytes.A. Time course of Waglerin-1 (#STW-001) action on muscle α1/β1/γ/δ nAChR. Current amplitudes were plotted as a function of time. Membrane potential was held at -80 mV and oocytes were stimulated by exposure to 10 μM acetylcholine every 100 seconds. 10 µM (for 3 min) Waglerin-1 were perfused during the period marked by the bar, as indicated. B. Superimposed traces of muscle nAChR channel current in the absence (black) and presence (green) of 10 µM Waglerin-1 (taken from the experiment in A).
- Sellin, L.C. et al. (1996) Biophys. J. 70, 3.
- McArdle, J.J. et al. (1999) J. Pharmacol. Exp. Ther. 289, 543.
- Molles, B.E. et al. (2002) J. Biol. Chem. 277, 5433.
- Ye, J.H. and McArdle, J.J. (1997) J. Pharmacol. Exp. Ther. 282, 74.
Waglerin-1 is a 22 amino acid peptide toxin isolated from the Southeast Asian snake Trimeresurus wagleri1. Two other similar peptides named Waglerin-2 and 3 are isolated from the same snake species1.
Waglerin-1 selectively blocks the nAChRε subunit with an IC50 of 50 nM2 and is a potent blocker of muscle nAChR3. Waglerin-1 is also a modulator of GABA(A) receptors with potentiating and suppressing effects. Its IC50 and EC50 value is 24 μM4.
Waglerin-1 (#STW-001) is a highly pure, synthetic, and biologically active peptide toxin.
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