Interaction of myelin basic protein with single bilayers on a solid support: an NMR, DSC and polarized infrared ATR study.

The interaction of myelin basic protein (MBP) with single bilayers on a solid support (planar and spherical support) is studied by deuterium nuclear magnetic resonance (2H-NMR), differential scanning calorimetry (DSC) and polarized attenuated total reflection infrared spectroscopy (ATR-IR). The single bilayer consisted of either DMPC or of a binary mixture of DMPC with 10-20 mol% of an acidic phospholipid (DMPG, DMPS or DMPA). All methods applied indicate that MBP strongly interacts with the binary lipid systems but not with the pure DMPC bilayers. The interaction is predominantly electrostatic in nature and does not depend on the choice of a particular acidic lipid (for the binary systems). In particular, the results give no indication for a hydrophobic interaction of MBP with the membrane. Our data provide evidence that, in contrast to previous findings, no demixing and/or domain formation in the binary systems is induced due to the MBP coupling. The infrared order parameter was determined for both lipid components of the binary systems and shows a remarkable change for both lipids due to the interaction with MBP while the NMR order parameter remained essentially unchanged. This is discussed in terms of the different timescales characteristic for both methods. The single supported bilayer responds to the MBP coupling as a whole although only 50% of the bilayer surface is accessible to the protein, indicating a strong coupling between the two bilayer leaflets via the hydrophobic chain region. Moreover, the asymmetric coupling of MBP to the single supported bilayer does not result in a significant redistribution of lipids between the two bilayer leaflets. NMR relaxation time measurements in the headgroup and chain region of DMPG and DMPC suggest that the lateral diffusion coefficient of the acidic lipid decreases significantly due to the coupling with MBP while the zwitterionic DMPC is not affected.