Methyllycaconitine: a selective probe for neuronal alpha-bungarotoxin binding sites

FEBS Lett. 1990 Sep 17;270(1-2):45-8. doi: 10.1016/0014-5793(90)81231-c.


The ability of methyllycaconitine (MLA) to inhibit the binding of [125I]alpha-bungarotoxin to rat brain membranes, frog and human muscle extracts and the human muscle cell line TE671 has been measured. MLA showed a markedly higher affinity for the rat brain site (Ki 1.4 x 10(-9) M) than for the muscle receptors (Ki 10(-5)-10(-6) M). Structure modelling techniques were used to fit the structure of MLA to a nicotinic pharmacophore model. MLA is the first low molecular weight ligand to be shown to discriminate between muscle nicotinic receptors and their alpha-bungarotoxin-binding counterpart in the brain, and as such may be a useful structural probe for pursuing the structural and functional properties of the neuronal protein.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aconitine / analogs & derivatives*
  • Aconitine / metabolism
  • Animals
  • Anura
  • Binding, Competitive
  • Bungarotoxins / metabolism*
  • Humans
  • In Vitro Techniques
  • Models, Molecular
  • Muscles / metabolism
  • Neurons / metabolism*
  • Rats
  • Receptors, Cholinergic / metabolism*
  • Receptors, Nicotinic*
  • alpha7 Nicotinic Acetylcholine Receptor


  • Bungarotoxins
  • Chrna7 protein, human
  • Chrna7 protein, rat
  • Receptors, Cholinergic
  • Receptors, Nicotinic
  • alpha7 Nicotinic Acetylcholine Receptor
  • methyllycaconitine
  • Aconitine