268389 Effects of Myelin Basic Protein (MBP) On the Interaction Forces and the Rheology Between Myelin Bilayers Using Surface Forces Apparatus (SFA)

Wednesday, October 31, 2012: 1:15 PM
413 (Convention Center )
Dong woog Lee1, Xavier Banquy2, Kai Kristiansen1, Joan Boggs3 and Jacob Israelachvili1, (1)Chemical Engineering, University of California, Santa Barbara, Santa Barbara, CA, (2)Chemistry, University of Montreal, Montreal, QC, Canada, (3)The Hospital for Sick Children, Molecular Structure and Function, Toronto, Canada

Myelin Basic Protein (MBP) plays an important role in myelin structure, strongly holding the cytoplasmic membrane sides together mainly by electrostatic and hydrophobic interactions [1]. MBP is also known to affect lipid domains, increasing their size by lowering the line tension [2]. In this work, the rheological properties of MBPs between model myelin lipid bilayers and the effect of MBP on interaction forces are studied using the Surface Force Apparatus (SFA) technique. Results show that above a certain critical bulk concentration, Ccrit, MBP adsorbs abruptly on lipid membranes, forming a 3 nm - thick layer in which the viscosity is 2 to 3 times higher than the bulk MBP solution. Also, above this Ccrit, normal myelin membranes show higher adhesion and less repulsion compared to EAE (a model for multiple sclerosis) myelin lipid bilayers while below Ccrit, there was no evidence of MBP adsorption and no significant difference between the force profiles of normal (healthy) and EAE (diseased) myelin bilayers. These results suggest that MBP adsorbs “cooperatively” in clusters/domains to myelin bilayers, and provide new insights in to how lipid-protein domains affect inter-membrane interactions.

References:

[1] Min, Y., et al., Interaction forces and adhesion of supported myelin lipid bilayers modulated by myelin basic protein. PNAS, 2009. 106(9): p. 3154-3159.

[2] Y. Min, et al., Critical and Off-Critical Mixing-Demixing Transitions in Model Extracellular and Cytoplasmic Myelin Lipid Monolayers. Biophys. J. (2011) 100 1490-1498.


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