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Methyllycaconitine: a selective probe for neuronal α‐bungarotoxin binding sites
Author(s) -
Ward J.M.,
Cockcroft V.B.,
Lunt G.G.,
Smillie F.S.,
Wonnacott S.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)81231-c
Subject(s) - methyllycaconitine , nicotinic agonist , acetylcholine receptor , bungarotoxin , receptor , binding site , chemistry , pharmacophore , ligand (biochemistry) , epibatidine , biophysics , torpedo , neuroscience , biochemistry , biology , nicotinic acetylcholine receptor
The ability of methyllycaconitine (MLA) to inhibit the binding of [ 125 I]α‐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 ( K i 1.4 × 10 −9 M) than for the muscle receptors ( K i ; 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 α‐bungarotoxinbinding counterpart in the brain, and as such may be a useful structural probe for pursuing the structural and functional properties of the neuronal protein.