6533b832fe1ef96bd129a44f
RESEARCH PRODUCT
Incorporation of the acetylcholine receptor dimer from Torpedo californica in a peptide supported lipid membrane investigated by surface plasmon and fluorescence spectroscopy
Eberhard NeumannA. MaelickeAndreas OffenhäusserAlfred JonczykE. K. SchmidtE. K. SchmidtRenate L. C. NaumannAndreas KukolThorsten LiebermannMaximilian KreiterWolfgang Knollsubject
Electric OrganLiposomeChemistryLipid BilayersSurface plasmonBiomedical EngineeringBiophysicsMembranes ArtificialGeneral MedicineReceptors NicotinicSurface Plasmon ResonanceTorpedoFluorescence spectroscopylaw.inventionNicotinic acetylcholine receptorSpectrometry FluorescenceBiochemistrylawElectrochemistryAnimalsLipid bilayerTorpedoIon channelBiotechnologyAcetylcholine receptordescription
Abstract The dimer species (Mr 580 000) of the nicotinic acetylcholine receptor, isolated from the electric organ of Torpedo californica, was incorporated into a thiopeptide supported lipid bilayer. The incorporation was achieved by fusion of liposomes with reconstituted receptor onto a gold-supported thiopeptide lipid monolayer. Surface plasmon resonance spectroscopy (SPS) was used to monitor in real time the fusion process as well as the specific binding of the antagonist α-bungarotoxin. A recently developed extension of SPS offering enhanced sensitivity and specificity, surface plasmon fluorescence spectroscopy (SPFS), was then used to monitor subsequent binding of the monoclonal WF6 and polyclonal antibody, respectively. The latter was fluorescence labeled with Cy5. The different binding assays indicate the successful incorporation of the receptor in the lipid bilayer.
year | journal | country | edition | language |
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1998-11-26 | Biosensors and Bioelectronics |