Trapping of an open-channel blocker at the frog neuromuscular acetylcholine channel

A. Neely, C. J. Lingle

Research output: Contribution to journalArticlepeer-review

48 Scopus citations


At the ganglionic nicotinic acetylcholine channel (Gurney, A. M., and H. P. Rang, 1984, Br. J. Pharmacol., 82:623–642) and on some cholinergic neuromuscular synapses of Crustacea (Lingle, C., 1983a, J. Physiol. (Lond.), 339:395–417; Lingle, C., 1983b, J. Physiol. (Lond.), 339:419–437), some agents that block cholinergic currents by an open-channel block mechanism appear to become trapped within the channel when it subsequently closes. It is unknown whether trapping of some open-channel blockers might also occur at the neuromuscular nicotinic acetylcholine channel. Here we show that the long-lived cholinergic blocking action of chlorisondamine, a ganglionic nicotinic blocker, can in part be most simply explained by an open-channel block mechanism followed by a subsequent trapping of the blocking molecule within the closed ion channel. Unique structural characteristics of the chlorisondamine molecule place several provocative constraints on the mechanism by which trapping may be occurring.

Original languageEnglish
Pages (from-to)981-986
Number of pages6
JournalBiophysical Journal
Issue number5
StatePublished - 1986


Dive into the research topics of 'Trapping of an open-channel blocker at the frog neuromuscular acetylcholine channel'. Together they form a unique fingerprint.

Cite this