Adsorption of Membrane-Associated Proteins to Lipid Bilayers Studied with an Atomic Force Microscope:  Myelin Basic Protein and Cytochrome <i>c</i>

Mueller, Henning; Butt, Hans‐Jürgen; Bamberg, Ernst

doi:10.1021/jp9940856

Cited by 77 publications

(80 citation statements)

References 78 publications

(88 reference statements)

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“…4A further indicates that the adhesion force can be enhanced by repeated approach-separation cycles and also by increasing the equilibrium contact time between the 2 surfaces. This enhancement shows that the lipids and proteins are laterally mobile and ''adaptable'' and can diffuse and rearrange to find their optimum configuration (14,25). It should be noted that the adhesive force in run 3 shows a noticeable deviation from the linear relationship shown by the straight line in Fig.…”

Section: Table 1 Lipid Compositions Of Healthy and Diseased Bilayersmentioning

confidence: 89%

“…Finally, the MBP undergoes conformational changes when it adsorbs to the lipid bilayer (25). In the presence of excess MBP, a phase transition is observed across highly swollen bilayers, suggesting the formation of a weak, dilute, but extended gel-like structure of MBP rather than a simple electrostatic repulsion (26,27).…”

Section: Table 1 Lipid Compositions Of Healthy and Diseased Bilayersmentioning

confidence: 99%

See 1 more Smart Citation

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

Min

Kristiansen

Boggs

et al. 2009

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

145

159

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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.biomembrane adhesion ͉ lipid-protein interactions ͉ multiple sclerosis ͉ myelin membrane structure ͉ experimental allergic encephalomyelitis T he myelin sheath is a multilamellar membrane surrounding the axons of neurons in both the central nervous system (CNS) and peripheral nervous system (PNS) (1) as shown in Fig. 1 A and B. The myelin sheath consists of repeating units of double bilayers separated by 3-to 4-nm-thick aqueous layers that alternate between the cytoplasmic and extracellular faces of cell membranes (2) (Fig. 1C). Dehydrated myelin is unusual in that it is composed of 75-80% lipid and 20-25% protein by weight, compared with Ϸ50% of most other cell membranes (3) (Fig. 1 C and D). Multiple lipids make up the myelin sheath (Table 1), and each sheath, with its own distinct physical properties, contributes to the structure, adhesive stability, and possibly the pathogenesis of the myelin membrane. The asymmetric distribution of lipid composition on the cytoplasmic and extracellular faces likely also plays an important role (4). Myelin basic protein (MBP) constitutes 20-30% of total protein by weight and is located only between the 2 cytoplasmic faces, where it acts as an intermembrane adhesion protein.The myelin sheath acts as an electrical insulator, forming a capacitor surrounding the axon, which allows for faster and more efficient conduction of nerve impulses than unmyelinated nerves (5). According to cable theory, the time to transmit a signal over a distance x is ϭ 1 ⁄2RC myelin x 2 , where R is the resistance per unit length, and C myelin is the capacitance between the axon and its surroundings, which is given by (5) C myelin ϭ 2 0 myelin log͑R O /R I ͒ per unit length,where R O and R I are the outer and inner radii (Fig. 1B), 0 is the permittivity of free space, and the mean dielectric constant of the myelin sheath iswhere (Fig. 1C). Low capacitance necessitates a low value of myelin , which is promoted by the much l...

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Section: Table 1 Lipid Compositions Of Healthy and Diseased Bilayersmentioning

confidence: 89%

Section: Table 1 Lipid Compositions Of Healthy and Diseased Bilayersmentioning

confidence: 99%

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

Min

Kristiansen

Boggs

et al. 2009

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

145

159

View full text Add to dashboard Cite

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“…In this section we also discuss force curves measured on solid supported lipid bilayers [728][729][730][731], surfactant layers [732][733][734][735][736][737] and adsorbed layers on solid surfaces. Lipids or surfactants can form adsorbed layers at the solid surface.…”

Section: Overviewmentioning

confidence: 99%

Force measurements with the atomic force microscope: Technique, interpretation and applications

Butt

Cappella

Kappl

2005

Surface Science Reports

Self Cite

3,135

2,907

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“…The intrinsic disorder of MBP when it is not associated to lipids is deemed essential to its biological function, but apart from this little is known about the actual microscopic mechanisms of the roles of MBP in normal and pathological cases. In particular, the relative weight of noncovalent interactions, mainly electrostatic and hydrophobic, and their roles in determining the morphology and mechanical properties of the myelin membrane have been the subject of extensive studies, which indicate the active presence of both (Mueller et al 1999(Mueller et al , 2000Boggs et al 1981a). Experimental evidence suggests that MBP plays an important role in linking two opposing cytoplasmic faces of myelin membranes, as it is shown by the dilation of the coding gene in shiverer mutant mice (Roach et al 1985), but does not seem to be so crucial in keeping together the extracellular faces of two compact membranes (Kirschner and Ganser 1980).…”

Section: Introductionmentioning

confidence: 99%

Microstructural analysis of the effects of incorporation of myelin basic protein in phospholipid layers

et al. 2005

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We report an X-ray reflectivity study on the effects of adsorption of myelin basic protein (MBP) on Langmuir monolayers and on deposited LangmuirSchaefer multilayers of the phospholipid dipalmitoyl phosphatidylglycerol (DPPG). We provide for the first time, direct microscopic evidence on the destructuring effects of MBP leading to plasticity of the DPPG layers supporting commonly accepted models of the stabilizing role of MBP in the myelin membrane. We also show how protein adsorption onto the layer is determined both by electrostatic and nonspecific hydrophobic interactions.

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Adsorption of Membrane-Associated Proteins to Lipid Bilayers Studied with an Atomic Force Microscope: Myelin Basic Protein and Cytochrome c

Cited by 77 publications

References 78 publications

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

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

Force measurements with the atomic force microscope: Technique, interpretation and applications

Microstructural analysis of the effects of incorporation of myelin basic protein in phospholipid layers

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