Authors: S. Iyer, A. Dattelbaum, J. Majewski, A. Shreve
Affilation: Los Alamos National Laboratory, United States
Pages: 480 - 483
Keywords: myelin, lipid, bilayers, self-assembly
The myelin sheath is among nature’s most fascinating nanoscale assemblies. In spite of its critical role in physiology, several questions on the structure-function relationship of myelin and its components remain unanswered. This is chiefly due to the fact that interactions between the constituents of myelin are particularly difficult to study in intact tissue. The compact, multi- lamellar structure of myelin inhibits or limits access to the interacting membrane surfaces. In addition, characterizing the interaction of purified myelin components has provided only limited information on such things as compositional and environmental effects on myelin structure. Thus, there is a tremendous need to develop novel biomimetic systems that can act as experimental models to help understand this critical component of complex neural systems. Our long-term goal is to create an assembly that closely mimics structural and functional aspects of natural myelin. Here we present data demonstrating the assembly of protein linked multi-bilayers. We also present data supporting the applicabilty of approaches such as spectroscopic ellipsometry, AFM and neutron reflectivity to analyze the structural integrity of the assemblies. Finally, we will present results of experiments where we altered specific propoerties of the binding proteins to ascertain their effect on structure.
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