A study of chemoreception based on membrane fluidity and circular dichroism of a membrane assembly model--role of protein penetrating into the lipid bilayer.
We attempted to reconstitute a chemical sensing assembly by mimicking the natural constituents of cell membranes. This liposomal arrangement is able to recognize chemical stimulants by detecting perturbation of the ordered lipid bilayer due to penetration by protein molecules. It was ascertained by measuring membrane fluidity using ESR that this assembly may be able to detect individually added chemical stimulants such as short-chain-bearing odorants (isovaleric acid, isovaleraldehyde, and isoamyl alcohol etc) at a concentration of 3 x 10(-4) parts to 1 part water. This recognition mechanism may clarify both the affinity of chemical stimulants for the liposomal arrangement and the trigger action of conformational changes in poly-L-lysine (PLL) due to the penetration of the bilayer of the PLL and sodium octylsulfate complex.
Ishigami
Y
Y
National Chemical Laboratory for Industry, Ibaraki, Japan.
Gama
Y
Y
Someno
K
K
Kaise
M
M
Ishizuka
Y
Y
Ishii
F
F
D001692:Biological Transport; D002942:Circular Dichroism; D004578:Electron Spin Resonance Spectroscopy; D008051:Lipid Bilayers / Q000493:pharmacokinetics; D008081:Liposomes; D008560:Membrane Fluidity; D008954:Models, Biological; D008968:Molecular Conformation; D011107:Polylysine / Q000494:pharmacology; D011506:Proteins / Q000493:pharmacokinetics; D013113:Spin Labels
D008051:Lipid Bilayers; D008081:Liposomes; D011506:Proteins; D013113:Spin Labels; D011107:Polylysine