Kinetic and Structural Study of the Interaction of Myelin Basic Protein with Dipalmitoylphosphatidylglycerol Layers

AbstractThe interaction of myelin basic protein (MBP) with dipalmitoylphosphatidylglycerol films has been investigated by means of a microgravimetric gauge sensitive to the changes in load and structural modifications of the layer deposited onto its surface. Fourier transform infrared spectroscopy, circular dichroism, and x-ray diffraction have confirmed protein uptake by the lipid phase along with a global disordering effect onto the lipid alkyl chains and have shown a temporal evolution of the structure of water penetrating the lipid phase together with the protein. These effects are clearly related to the temporal variation of the microgravimetric gauge signal. Finally, measurements carried out on pre-annealed samples point out the role of mesoscopic morphology in determining the pathways through which MBP penetrates the lipid multilayer. The results obtained in our model system could be useful in clarifying the mechanisms of the myelinating and demyelinating processes that take place in the natural membrane