A modified nicotinic acetylcholine receptor lacking the ‘ion channel amphipathic helices’

AbstractAntibodies to a synthetic peptide from the ‘amphipathic helix’ of the α-chain of the nicotinic acetylcholine receptor (nAChR) bound both to detergent-solubilised and membrane-bound nAChR, indicating that this region, suggested as a component of the transmembrane ion channel in one model, is not buried in the membrane. Trypsinisation of membranes prior to affinity purification yielded preparations lacking the amphipathic helices of the α- and β-chains and probably also of the γ-and δ-chains. Such material should allow direct testing, by reconstitution experiments, of the importance of these regions for channel activity