Comparative study of myelin proteolipid apoprotein solvation by multilayer membranes of synthetic DPPC and biological lipid extract from bovine brain. An FT-IR investigation

Abstract

The interaction between the aqueous form of the myelin proteolipid apoprotein (PLA) and model membranes prepared with either synthetic dipalmitoylphosphatidyl choline (DPPC) or biological lipids extracted from bovine brain (BE) has been investigated by Fourier-Transform IR spectroscopy. IR spectra obtained with lyophilized samples of PLA demonstrated 2 main peaks (amide I and amide II) culminating at 1656 cm −1 and 1545 cm −1, which we assigned to helical conformation. When PLA was solvated in DPPC or BE membranes, both the amide I and amide II features remained located at 1655 cm −1 and 1545 cm −1, although their half-width significantly decreased, demonstrating that the lipid environment favoured α helix structures. However differences between both mixtures were detected by measuring the amide I and amide II half-widths as a function of the L:P molar ratio. Moreover, analysis of the 1545/1515 peak intensity ratio brought evidence of different localization and/or molecular arrangement of the protein segments containing tyrosine residues, depending on the lipid composition of the membrane. According to previously published models, these data suggest that recombinants prepared with PLA and BE multilayers better mimic the biological membrane than do DPPC-PLA mixtures.