Interaction forces and adhesion of supported myelin lipid bilayers modulated by myelin basic protein

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 106; no. 9; pp. 3154 - 3159
• Main Authors: Min, Younjin, Kristiansen, Kai, Boggs, Joan M, Husted, Cynthia, Zasadzinski, Joseph A, Israelachvili, Jacob
• Format: Journal Article
• Language: English
• Published: United States National Academy of Sciences 03.03.2009; National Acad Sciences
• Subjects: Adhesion; Adhesiveness; Biological Sciences; Cell adhesion & migration; Cells; Chemical composition; Electrostatics; Fatty acids; Lipid bilayers; Lipid Bilayers - chemistry; Lipids; Molecular Structure; Molecules; Myelin; Myelin Basic Protein - chemistry; Myelin basic proteins; Myelin sheath; Myelin Sheath - chemistry; Proteins; Surface Properties; Swelling
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.0813110106

Force-distance measurements between supported lipid bilayers mimicking the cytoplasmic surface of myelin at various surface coverages of myelin basic protein (MBP) indicate that maximum adhesion and minimum cytoplasmic spacing occur when each negative lipid in the membrane can bind to a positive arginine or lysine group on MBP. At the optimal lipid/protein ratio, additional attractive forces are provided by hydrophobic, van der Waals, and weak dipolar interactions between zwitterionic groups on the lipids and MBP. When MBP is depleted, the adhesion decreases and the cytoplasmic space swells; when MBP is in excess, the bilayers swell even more. Excess MBP forms a weak gel between the surfaces, which collapses on compression. The organization and proper functioning of myelin can be understood in terms of physical noncovalent forces that are optimized at a particular combination of both the amounts of and ratio between the charged lipids and MBP. Thus loss of adhesion, possibly contributing to demyelination, can be brought about by either an excess or deficit of MBP or anionic lipids.