Elasticity, Strength, and Water Permeability of Bilayers that Contain Raft Microdomain-Forming Lipids

Rawicz, W.; Smith, Benjamin; McIntosh, Thomas J.; Simon, Sidney A.; Evans, EA

doi:10.1529/biophysj.107.121731

Cited by 218 publications

(227 citation statements)

References 60 publications

(136 reference statements)

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“…These inhomogeneities can dramatically amplify the effect of even small changes in the lipid composition or protein isoform (20), resulting in large changes in bilayer adhesion (7,15) that may cause the myelin sheath to unravel. Lipid domains within lipid bilayers are known to be correlated with bilayer-bilayer interactions (46) and may play important roles in adhesion (47), intermembrane spacing (48), and permeability (49). Lipid domains also are thought to act as platforms on which proteins can adsorb selectively (50).…”

Section: Discussionmentioning

confidence: 99%

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

Lee

Banquy

Kristiansen

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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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/m 2 ), in contrast to its formation of thicker (7-8 nm) swelled films with weaker intermembrane adhesion (∼0.13 mJ/m 2 ) 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.lipid raft | biomembrane adhesion | myelin structure | multiple sclerosis | intrinsically unstructured proteins M yelin is an asymmetric multilamellar membrane wrapped around the axons of the central nervous system (CNS) and consists of alternating extracellular and cytoplasmic leaflets (1-3). The bilayer-associated proteins, mainly myelin basic protein (MBP) and proteolipid protein, play an essential role in stabilizing and maintaining the myelin structure. The bilayers are in close contact (∼3 nm separation between lipid headgroupwater interfaces), providing a low dielectric constant through the compact bilayers, which is essential for efficient and fast saltatory propagation of nerve impulses. Any structural changes of the myelin sheath in the CNS, including lesion formation, loss of adhesion, swelling of the water gaps, vacuolization, vesiculation, and complete delamination (demyelination) of the myelin sheath (4-6), are signatures of several inflammatory neurological disorders. These types of disorders are characterized by a broad spectrum of neurological symptoms, such as physical and cognitive disabilities, with multiple sclerosis (MS) being one of the most common demyelinating diseases (2).The primary cause of structural changes in the myelin is still under debate; however, morphological changes of the myelin structure due to diseases such as MS are well known. A wellstudied and accepted animal model for MS is the experimental allergic encephalomyelitis (EAE) of the marmoset (2, 6). Using this model, recent studies conducted with the surface forces apparatus (SFA) have shown that a loss of adhesion force (7) and structural changes of model membranes with lipid composition characteristic of myelin accompanied compositional alterations of the lipid species (8), as well as an electric charge imbalance between lipid molecules and MBP (9). These alterations also change the lateral distribution a...

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Section: Discussionmentioning

confidence: 99%

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

Lee

Banquy

Kristiansen

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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“…1C). From AFM measurements (Yuan et al 2002;Lawrence et al 2003;Connell and Smith 2006), it has been shown that L o membranes are thicker than L d membranes, and therefore stiffer, as has been measured by tube pulling experiments Roux et al 2005) and pipette aspiration (Rawicz et al 2008). Typical values of k of ternary vesicles in the L o phase are 50 -60 kT, whereas in the L d phase, typically 20 -30 kT.…”

Section: Box 1 Energy Of a Two-component Membranementioning

confidence: 90%

Curvature-Driven Lipid Sorting in Biomembranes

Callan-Jones¹,

Sorre²,

Bassereau³

2011

Cold Spring Harbor Perspectives in Biology

128

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It has often been suggested that the high curvature of transport intermediates in cells may be a sufficient means to segregate different lipid populations based on the relative energy costs of forming bent membranes. In this review, we present in vitro experiments that highlight the essential physics of lipid sorting at thermal equilibrium: It is driven by a trade-off between bending energy, mixing entropy, and interactions between species. We collect evidence that lipid sorting depends strongly on lipid -lipid and protein-lipid interactions, and hence on the underlying composition of the membrane and on the presence of bound proteins.

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“…A plethora of studies have looked at the function of cholesterol in cell membranes and the effect of the addition of cholesterol in altering the intermolecular interactions in biomimetic 1 membrane systems. 3,15,16 For example, phase diagrams of binary and ternary lipid mixtures containing cholesterol are well-documented 17,18 , and studies have also looked at the alteration of membrane mechanical properties due to preferential segregation of cholesterol 2,8 . In terms of high resolution structural characterization, Mills et al 19 quantified changes in the lamellar repeat distance in multilamellar DPPC vesicles with cholesterol using wide angle x-ray scattering.…”

Section: Introductionmentioning

confidence: 99%

Characterization of Solid-Supported Dipalmitoylphosphatidylcholine Membranes Containing Cholesterol

Kurniawan

Kuhl

2015

Langmuir

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The incorporation of cholesterol into dipalmitoylphosphatidylcholine (DPPC) membranes, even in small amounts, has been shown to significantly alter the properties of the membrane. In this work, force–distance interaction profiles of DPPC membranes containing 8 mol % cholesterol obtained using the surface force apparatus are analyzed in the context of high-resolution structural characterization by atomic force microscopy and neutron reflectometry. The adhesion between the mixed membranes was greater than that for pure DPPC and was variabledepending on the number of defects in the outer membrane leaflets. These defects were only detectable by atomic force microscopy and had an average size of 230 ± 30 nm and 1–5% surface density in the outer leaflet. The adhesion between the membranes monotonically increased as the thickness of the membrane decreasedin direct correlation with the number of defects present (exposed hydrophobic groups) in the membrane contact region. Because of the low diffusion rate of gel-phase membranes, the interaction force profiles were stable and no membrane restructuring was observed.

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Elasticity, Strength, and Water Permeability of Bilayers that Contain Raft Microdomain-Forming Lipids

Cited by 218 publications

References 60 publications

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

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

Curvature-Driven Lipid Sorting in Biomembranes

Characterization of Solid-Supported Dipalmitoylphosphatidylcholine Membranes Containing Cholesterol

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