M2 delta, a candidate for the structure lining the ionic channel of the nicotinic cholinergic receptor.
- 1 November 1988
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 85 (22) , 8703-8707
- https://doi.org/10.1073/pnas.85.22.8703
Abstract
A synthetic 23-mer peptide that mimics the sequence of the putative transmembrane M2 segment of the Torpedo californica acetylcholine receptor (AcChoR) .delta. subunit.sbd.Glu-Lys-Met-Ser-Thr-Ala-Ile-Ser-Val-Leu-Leu-Ala-Gln-Ala-Val-Phe-Leu-Leu-Leu-Thr-Ser-Gln-Arg.sbd.forms discrete ionic channels in phosphatidylcholine bilayers. In contrast, a synthetic peptide that mimics the sequence of the putative M1 transmembrane segment of the Torpedo AcChoR .delta. subunit.sbd.Leu-Phe-Tyr-Val-Ile-Asn-Phe-Ile-Thr-Pro-Cys-Val-Leu-Ile-Ser-Phe-Leu-Ala-Ser-Leu-Ala-Phe-Tyr.sbd.does not form channels. The synthetic M2 .delta. channel peptide exhibits features that are characteristic of the authentic AcChoR channel, such as single channel conductances, discrimination of cations over anions, and channel lifetimes for open and closed states in the millisecond time range. Energetic considerations suggest that an aggregate of five amphipathic .alpha.-helices conforms the channel. Thus, the M2 segment may be a component of the AcChoR channel structure.This publication has 35 references indexed in Scilit:
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