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

doi:10.1073/pnas.1401165111

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 journal › Article › peer-review

50 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 language	English
Pages (from-to)	E768-E775
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	111
Issue number	8
DOIs	https://doi.org/10.1073/pnas.1401165111
State	Published - 25 Feb 2014
Externally published	Yes

Keywords

Biomembrane adhesion
Intrinsically unstructured proteins
Lipid raft
Multiple sclerosis
Myelin structure

ASJC Scopus subject areas

General

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10.1073/pnas.1401165111

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title = "Lipid domains control myelin basic protein adsorption and membrane interactions between model myelin lipid bilayers",

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.",

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Lipid domains control myelin basic protein adsorption and membrane interactions between model myelin lipid bilayers. / Lee, Dong Woog; Banquy, Xavier; Kristiansen, Kai et al.
In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 111, No. 8, 25.02.2014, p. E768-E775.

Research output: Contribution to journal › Article › peer-review

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T1 - Lipid domains control myelin basic protein adsorption and membrane interactions between model myelin lipid bilayers

AU - Lee, Dong Woog

AU - Banquy, Xavier

AU - Kristiansen, Kai

AU - Kaufman, Yair

AU - Boggs, Joan M.

AU - Israelachvili, Jacob N.

PY - 2014/2/25

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N2 - 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.

AB - 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.

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

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