α-Conotoxin PIA

A Selective nAChRα6 Antagonist
Cat #: STC-870
  • Lyophilized Powder
  • Bioassay Tested
  • Origin Synthetic peptide originated from Conus purpurascens (Purple cone).
    MW: 1981 Da.
    Purity: >98% (HPLC)
    Effective concentration 0.20-1 µM.
    Sequence RDPCCSNPVCTVHNPQIC.
    Modifications Disulfide bonds between Cys4-Cys10 and Cys5-Cys18. Cys18 – C-terminal amidation.
    Molecular formula C79H125N27O25S4.
    CAS No.: 669050-68-4.
    Activity α-Conotoxin PIA is a selective antagonist of α6-containing nAChR1,2.
      • Dowell, C. et al. (2003) J. Neurosci. 23, 8445.

      • Chi, S.W. et al. (2005) Biochem. Biophys. Res. Commun. 338, 1990.

    Shipping and storage Shipped at room temperature. Product as supplied can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C.
    Solubility Any other aqueous buffer. Centrifuge all product preparations before use (10000 g x 5 min).
    Storage of solutions Up to two weeks at 4°C or three months at -20°C.
      • Alomone Labs α-Conotoxin PIA inhibits α3/β2 nAChR heterologously expressed in Xenopus oocytes.
        A. Time course of α-Conotoxin PIA (#STC-870) blocking action on α3/β2 nAChR. Current amplitude were plotted as a function of time. Membrane potential was held at -80 mV and oocyte were stimulated by exposure to 10 µM ACh every 50 sec. 0.2 µM (red) and 1 µM (green) (each for 3 min) α-Conotoxin PIA were perfused during the period marked by the bar, as indicated. B. Superimposed traces of α3/β2 nAChR channel current in the absence (black) and presence of different concentrations of α-Conotoxin PIA (taken from experiment in A).
      • Dowell, C. et al. (2003) J. Neurosci. 23, 8445.
      • Chi, S.W. et al. (2005) Biochem. Biophys. Res. Commun. 338, 1990.
      • Yang, K.C. et al. (2009) Acta Pharmacol. Sin. 30, 740.
      • α-Conotoxin PIA is a peptide toxin originally isolated from Conus purpurascens and belongs to the A superfamily of conotoxins. It is a selective antagonist for heteromeric α6 subunit -containing nicotinic acetylcholine receptors (nAChR). α-Conotoxin PIA binds on the extracellular portion of the nAChR and distinguishes α6 from α3 subunits due to its lower affinity for α3.

        The alpha-conotoxin PIA has an "omega-shaped" overall topology, containing spacing of Cys residues, disulfide connectivity, and the SNPV (serine, asparagine, proline, valine) sequence in the first peptide loop. The second loop demonstrates a kink in Pro15 that provides a distinct steric and electrostatic environment1-3.

        Evidence has shown that α-conotoxin PIA has the ability to potently block nicotine-stimulated dopamine release in rat striatal synaptosomes with low nanomolar potency1. Indeed, the IC50 value for α-conotoxin PIA of human chimeric α6/α3/β2/β3 nAChRs is 1.7 nM1.

        Nicotinic acetylcholine receptors containing α6 subunits in the CNS are involved in a variety of physiological functions, and considered to play an important role in cognitive function, motor activity, pain perception, analgesia and the reinforcing properties of nicotine.

        They are implicated in the pathophysiology and treatment of diseases like chronic Parkinson's, and Alzheimer's1.

    Target α6 nAChR
    Net Peptide Content: 100%
    Last update: 30/06/2019

    α-Conotoxin PIA (#STC-870) is a highly pure, synthetic, and biologically active peptide toxin.

    For research purposes only, not for human use