Selectivity of lipid-protein interaction with myelin proteolipids PLP and DM-20. A fluorescence anisotropy study.

摘要: Abstract The two main myelin proteolipids, PLP (30 kDa) and DM-20 (25 kDa), differ by an internal deletion in DM-20. deleted fragment, of 35 amino acids (116–150), corresponds to the major hydrophilic domain PLP. Fluorescence anisotropy experiments using diphenylhexatriene as a fluorescent probe were performed detect phase separation induced these proteolipids multilamellar vesicles binary composition. We found that composed 30% l -α-PS 70% DPPC, boundary layer contained about 18 motionally restricted phospholipids, almost exclusively -α-PS. On contrary, only 14 15 with composition no different from bulk vesicle. In mixtures DMPG selectivity for acidic phospholipid was maintained, but lower than observed assume this stems mainly electrostatic interactions between charged residues 116–150 DM-20, phospholipids. These results suggest fragment may play specific role interaction lipid bilayer membrane.