Overview
- Utkin, Y.N. et al. (2012) J. Biol. Chem. 287, 27079.
- Alomone Labs Azemiopsin inhibits fetal muscle nAChR (α1/β1/γ/δ) heterologously expressed in Xenopus oocytes.Time course of Azemiopsin (#STA-100) action on fetal muscle α1/β1/γ/δ nAChR. Current amplitudes were plotted as a function of time. Membrane potential was held at -60 mV and oocytes were stimulated by exposure to 100 µM acetylcholine every 200 seconds. 1 µM (for 5 min) Azemiopsin was perfused during the period marked by the bar.
- Utkin, Y.N. et al. (2012) J. Biol. Chem. 287, 27079.
Azemiopsin is a 21 amino acid peptidyl toxin, isolated from the Azemiops feae viper venom1 and is a synthetic version of the peptide. Unlike similar venom isolates, it does not contain cysteine residues1.
Azemiopsin efficiently competes with α-Bungarotoxin (#B-100) for binding to Torpedo nAChR and with lower efficiency to human α7 nAChR. It dose-dependently blocks ACh-induced currents in Xenopus oocytes heterologously expressing human muscle-type nAChR and is more potent against the adult form than the fetal form1. The peptide has no effect on GABA(A) receptors or on 5-HT3 receptors1.
Azemiopsin resembles Waglerin-1 (#STW-001) (a disulfide-containing peptide from the Tropidechis wagleri venom) in its biological activity.
Azemiopsin (#STA-100) is a highly pure, synthetic, and biologically active peptide toxin.