Overview
Disulfide bonds location- Cys2-Cys8, Cys3-Cys16
- Cartier, G.E. et al. (1996) J. Biol. Chem., 271, 7522.
- Kuryatov, A. et al. (2000) Neuropharmacol., 39, 2570.
- McIntosh, J.M. et al. (2000) Eur. J. Pharmacol. 393, 205.
Alomone Labs α-conotoxin MII inhibits α3/β2 nAChRs expressed in Xenopus oocytes.A. Representative time course of α3/β2 current inhibition by 20 nM α-conotoxin MII (#STC-040). Currents were elicited every 50 sec by transient applications of 20 µM ACh, while membrane potential was held at -80 mV, and inhibited by 20 nM (green) α-conotoxin MII.
B. Superimposed traces of α3/β2 currents evoked by ACh (arrow) after application of control (black) and 20 nM (green) α-conotoxin MII (Taken from the recording in A).
- Cartier, G.E. et al. (1996) J. Biol. Chem., 271, 7522.
- Kuryatov, A. et al. (2000) Neuropharmacology, 39, 2570.
- McIntosh, J.M. et al. (2000) Eur. J. Pharmacol. 393, 205.
- Zoli, M. et al. (2015) Neuropharmacology, 96, 302.
- Gotti, C. et al. (2009) Biochem. Pharmacol., 78, 703.
- Levin, E.D. et al. (2006) Psychopharmacology 184, 523.
α-conotoxin MII is a 16 amino acid peptidyl toxin originally isolated from the venom of the marine snail, Conus magus1. This toxin was initially thought to be a selective antagonist for α3β2 nicotinic acetylcholine receptors (nAChRs)1. Subsequently, it has been shown that α-conotoxin MII is also an α6β2* nAChR subtype selective antagonist2 and it potently blocks β3-containing neuronal nAChRs3.
Neuronal nAChRs are a heterogeneous family of ligand-gated cation channels that are expressed throughout the brain and involved in a wide range of physiological and pathophysiological processes. These different receptor subtypes have a pentameric structure consisting of the homomeric or heteromeric combination of 12 different subunits (α2–α10, β2–β4)4.
nAChRs are critically important for neuronal survival and cognitive function, as well as regulation of neurodegenerative diseases, including Alzheimer’s and Parkinson’s. The nAChR subtypes share a common basic structure, but their biophysical and pharmacological properties depend on their subunit composition. Thus, the subunit makeup of the nAChR subtypes is central to understanding their function in the nervous system and for discovering new subtype-selective drugs4-6.
α-Conotoxin MII (#STC-040) is a highly pure, synthetic, and biologically active peptide toxin
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