Fluorescence studies of the nicotinic acetylcholine receptor in its membrane environment.
Since the discovery of the fraction of immobilized lipid in contact with the nicotinic acetylcholine receptor (AChR), the lipid-belt region around this protein has become the focus of a variety of biophysical studies aimed at defining its properties. Here we summarize recent spectroscopic studies from our laboratory using Laurdan fluorescence to characterize distinct sites for lipids and to describe their effect on the AChR microenvironment.
Barrantes
F J
FJ
Instituto de Investigaciones Bioquímicas de Bahía Blanca, Universidad Nac. del Sur, Argentina. rtfjbl@criba.edu.ar
Antollini
S
S
Massol
R
R
D015081:2-Naphthylamine / Q000031:analogs & derivatives; D002462:Cell Membrane / Q000737:chemistry*; D005456:Fluorescent Dyes; D007848:Laurates; D008563:Membrane Lipids / Q000737:chemistry; D011978:Receptors, Nicotinic / Q000737:chemistry*; D013050:Spectrometry, Fluorescence
D005456:Fluorescent Dyes; D007848:Laurates; D008563:Membrane Lipids; D011978:Receptors, Nicotinic; D015081:2-Naphthylamine; C065580:laurdan