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Alpha-Conotoxin Vc1.1

ACV1, Vc1.1, Alpha-Conotoxin Vc1.1, α-Conotoxin Vc1.1

A Potent Antagonist of α9α10 nAChR, a Weak Antagonist of other nAChRs and an Agonist of GABAB receptors.

Cat #: STV-500
Alternative Name ACV1, Vc1.1, Alpha-Conotoxin Vc1.1, α-Conotoxin Vc1.1
Lyophilized Powder yes
  • Bioassay Tested
  • Origin Conus victoriae
    Source Synthetic
    MW: 1807 Da
    Purity: >98% (HPLC)
    Form Lyophilized Powder
    Effective concentration 20 nM – 1 µM
    Modifications Disulfide bonds between Cys2-Cys8 and Cys3-Cys16 
    Cys16 – C-terminal amide
    Molecular formula C71H103N23O25S4
    CAS No.: 740980-24-9
    Activity A specific antagonist of α9α10 nAChR that also selectively modulate high-voltage-activated (HVA) calcium channel acting as agonists via G-protein -coupled GABAB receptors 1,2.
    1. Sandall, D.W. et al. (2003) Biochemistry, 42, 6904.
    2. Callaghan, B. et al. (2008) J. Neurosci., 28, 10943.
    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 Soluble in DDW. 
    Centrifuge all products before use (10000 x g, 5 min). Avoid multiple freezing and thawing. 
    Storage of solutions Store at 4°C for up to 1 week. For longer periods, small aliquots should be stored at -20°C.
    Our bioassay
    • Alomone Labs Alpha-Conotoxin Vc1.1 inhibits α3/β2 nAChR heterologously expressed in Xenopus oocytes.
      Alomone Labs Alpha-Conotoxin Vc1.1 inhibits α3/β2 nAChR heterologously expressed in Xenopus oocytes.
      1. Time course of Alpha-Conotoxin Vc1.1 (#STV-500) action on α3/β2 nAChR currents, elicited every 50 sec by a transient application of 10 µM ACh, while membrane potential was held at -80 mV. Application of 2 µM (green) and 10 µM (magenta) Alpha-Conotoxin Vc1.1 significantly inhibits the currents.
      2. Superimposed traces of α3/β2 nAChR currents evoked by ACh (arrow) after application of control, 2 µM (green) and 10 µM (magenta) Alpha-Conotoxin Vc1.1 (taken from the experiment in A).
    References - Scientific background
    1. Sandall, D.W. et al. (2003) Biochemistry, 42, 6904.
    2. Vincler, M. et al. (2006) PNAS, 103(47), 17780.
    3. Callaghan, B. et al. (2008) J. Neurosci., 28, 10943.
    4. Sadeghi, M. et al. (2018) ACS Chem. Biol., 13, 1577.
    5. Satkunanathan, N. et al. (2005) Brain Res., 1059, 149.
    6. Castro, J. et al. (2017) Gut, 66, 1083.
    Scientific background

    α-Conotoxin Vc1.1 (Vc1.1) is a 16 amino acid synthetic version of a conopeptide, which was first discovered from a PCR screen of cDNA from the venom ducts of the tropical marine snail, Conus victoriae1. Vc1.1 adopts the archetypal three-dimensional structure of a-conotoxins, which consists of a helical region stabilized by two disulfide bonds. The α-conotoxin family members are defined, in part, by their pharmacological targets, the nicotinic acetylcholine receptors (nAChRs). Vc1.1 is a neuronal nAChR antagonist that displays selectivity for the α9α10 subtype2. A subset of α-conotoxins have been shown to inhibit high-voltage-activated (HVA) calcium channel currents via activation of the γ-aminobutyric acid (GABA) receptor B (GABABR). GABABRs are G-protein-coupled receptors (GPCRs) for GABA, the main inhibitory neurotransmitter in the brain. GABABRs are promising targets for the treatment of various neurological and psychiatric disorders, including pain, depression, and drug addiction. Vc1.1 was the first α-conotoxin shown to inhibit HVA calcium channels (CaV2.2 and CaV2.3) via GABABR activation3,4.

    Vc1.1 alleviates neuropathic pain in three human neuropathic pain rat models and accelerates the functional recovery of injured neurons5. This toxin has been tested in human clinical trials for the treatment of neuropathic pain, where it exhibited both clean safety and side effect profiles. In addition to its antinociceptive and antihyperalgesic actions in neuropathic pain models, Vc1.1 inhibits human DRG neurons via activation of the GABABR, which are the primary transducers at the start of the pain processing pathway6.

    Target α9α10 nAChRs, GABA(B) receptors, Neuronal nAChR, Cav2.2, Cav2.3
    Peptide Content: 100%
    Last update: 29/08/2021

    Vc1.1 (#STV-500) is a highly pure, synthetic, and biologically active peptide toxin.

    For research purposes only, not for human use
    Shipping and Ordering information