FTIR study of the monosialoganglioside GM1 in perdeuterated dimyristoylglycerophosphocholine (DMPCd54) multilamellar bilayers: spectroscopic evidence of a significant interaction between Ca2+ ions and the sialic acid moiety of GM1.

Fourier transform infrared (FTIR) spectroscopy was employed to study bovine brain GM1 and perdeuterated dimyristoylglycerophosphocholine (DMPCd54) multilamellar dispersions (mole fractions of GM1 in DMPCd54: 0.12, 0.15, 0.19, 0.26, 0.34, 0.41, and 0.58), in the absence and presence of 10 mM CaCl2. GM1 micelles did not display a thermal phase transition in the temperature range 5-60 degrees C. Moreover, the ceramide moiety of GM1 inserted into the hydrophobic core of DMPCd54 bilayers and was capable of undergoing a single, cooperative phase transition (Tm = 22-28 degrees C, depending on GM1 content) in a bilayer system. This suggested that the mixed bilayers consisted of a homogeneous mixture and that GM1 was uniformly dispersed in the bilayer plane rather than segregated into regions of relative enrichment. The coexistence of GM1 and DMPCd54 in a bilayer environment induced a rearrangement of the interfacial hydrogen bonding network of the amide I and ester C=O groups, relative to GM1 micelles and DMPCd54 bilayers, respectively. The modifications induced by GM1 might ultimately modulate surface events such as lipid-lipid and/or lipid-protein interactions. The spectroscopic results also suggested that the glycolipid's headgroup surface location and conformation in bilayers allow GM1 to act as a receptor for Ca2+ via its sialic acid moiety.