Lipid domains control myelin basic protein adsorption and membrane interactions between model myelin lipid bilayers

Dong Woog Lee, Xavier Banquy, Kai Kristiansen, Yair Kaufman, Joan M. Boggs, Jacob N. Israelachvili

Research output: Contribution to journalArticlepeer-review

54 Scopus citations

Abstract

The surface forces apparatus and atomic force microscope were used to study the effects of lipid composition and concentrations of myelin basic protein (MBP) on the structure of model lipid bilayers, as well as the interaction forces and adhesion between them. The lipid bilayers had a lipid composition characteristic of the cytoplasmic leaflets of myelin from "normal" (healthy) and "disease-like" [experimental allergic encephalomyelitis (EAE)] animals. They showed significant differences in the adsorption mechanism of MBP. MBP adsorbs on normal bilayers to form a compact film (3-4 nm) with strong intermembrane adhesion (∼0.36 mJ/m2), in contrast to its formation of thicker (7-8 nm) swelled films with weaker intermembrane adhesion (∼0.13 mJ/m2) on EAE bilayers. MBP preferentially adsorbs to liquid-disordered submicron domains within the lipid membranes, attributed to hydrophobic attractions. These results show a direct connection between the lipid composition of membranes and membrane-protein adsorption mechanisms that affects intermembrane spacing and adhesion and has direct implications for demyelinating diseases.

Original languageEnglish
Pages (from-to)E768-E775
JournalProceedings of the National Academy of Sciences of the United States of America
Volume111
Issue number8
DOIs
StatePublished - 25 Feb 2014
Externally publishedYes

Keywords

  • Biomembrane adhesion
  • Intrinsically unstructured proteins
  • Lipid raft
  • Multiple sclerosis
  • Myelin structure

ASJC Scopus subject areas

  • General

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