Evidence for the presence of a specific ganglioside GM1/valinomycin complex in mixed monolayers.
The effect of a negatively charged mono-sialoglyco-sphingolipid (GM1-ganglioside) on the molecular organization and on physiochemical properties of lipid/peptide (valinomycin) systems was investigated in monolayers at the air/water interface. At a high molar fraction of GM1, the surface pressure/area isotherms of the two-component films of the system GM1/valinomycin and the isotherm of the pure ganglioside monolayer are identical concerning the space requirement of the molecules and thereby the packing of the monolayer. Using space-filling molecular models, a simple calculation gives the theoretical amount of 4.5 ganglioside molecules associated with one molecule of the depsipeptide valinomycin. The average surface potential indicates, that valinomycin, interacting with the polar head group of GM1, becomes partly embedded within the lipid interface. For GM1/eicosanol and valinomycin/eicosanol mixtures, the agreement between theory and experimental data strongly supports the model of ideal mixing without any molecular interactions between the different components. The results suggest the formation of a ganglioside/valinomycin complex with simultaneous alteration of the surface potential and molecular structure of the single components.
Schifferer
F
F
Zoological Institute, Universität Stuttgart-Hohenheim, F.R.G.
Cordroch
W
W
Beitinger
H
H
Möbius
D
D
Rahmann
H
H
D000388:Air; D005677:G(M1) Ganglioside / Q000737:chemistry*; D008961:Models, Structural; D008968:Molecular Conformation; D011199:Potentiometry; D011312:Pressure; D011487:Protein Conformation; D013499:Surface Properties; D014634:Valinomycin / Q000737:chemistry*; D014867:Water
D014867:Water; D014634:Valinomycin; D005677:G(M1) Ganglioside