Solubilization and insertion into reverse micelles of the major myelin transmembrane proteolipid.

The Folch-Pi proteolipid has been isolated from bovine white matter and characterized with respect to phospholipid and glycolipid composition. The protein-lipid complex has been solubilized in aqueous reverse micelles of di(2-ethylhexyl) sodium sulfosuccinate and isooctane. Solubilization of this otherwise water-insoluble proteolipid requires small amounts of water, the percent of solubility being maximum for a low molar ratio of water to surfactant (Wo = 5.6). Unlike hydrophilic proteins, the extent of incorporation into the micellar system is negligible at 50 mM surfactant and reaches 90Vo only at 300 mM. However, the conformation of the proteolipid in reverse micelles as studied by fluorescence emission spectroscopy and circular dichroism was not affected by variations of the surfactant concentration. These results are consistent with the peculiar properties of the aqueous environment of the proteolipid within the reverse micelles and may reflect the membrane-like character of these bio-assemblies.