Alzheimer's disease amyloid-β peptide analogue alters the ps-dynamics of phospholipid membranes

Buchsteiner, A.; Hauβ, Thomas; Dante, Silvia; Dencher, Norbert A.

doi:10.1016/j.bbamem.2010.06.024

Cited by 42 publications

(43 citation statements)

References 43 publications

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“…Figure 9 shows 1 and 2 together with quasielastic energy broadening data previously published for DMPC in its fluid phase, at = 303 K [8]. Only one diffusion process was observed in the experiment by Armstrong et al The data quality resulting from this experiment did not allow for the unambiguous assignment of more than one process; however, the diffusion constant obtained from this analysis was in good agreement with coefficients quoted in the literature for similar systems [1,4,11,12,28]. The fit in Figure 9 corresponds to a diffusion coefficient of 64 × 10 −12 m 2 /s.…”

Section: Discussionsupporting

confidence: 78%

Incoherent Neutron Spin-Echo Spectroscopy as an Option to Study Long-Range Lipid Diffusion

et al. 2013

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Diffusion is the fundamental mechanism for lipids and other molecules to move in a membrane. It is an important process to consider in modelling the formation of membrane structures, such as rafts. Lipid diffusion is mainly studied by two different techniques: incoherent neutron scattering and fluorescence microscopy. Both techniques access distinctly different length scales. While neutron scattering measures diffusion over about 3 lipid diameters, microscopic techniques access motions of lipids over micrometer distances. The diffusion constants which are determined by these two methods often differ by about an order of magnitude, with the neutrons usually seeing a faster lipid diffusion. Different theories are used to describe lipid diffusion in the two experiments. In order to close the "gap" between these two techniques, we propose to study lipid diffusion at mesoscopic length scales using a neutron spin-echo (NSE) spectrometer. We have conducted an experiment in highly oriented, solid supported lipid bilayers to prove the feasibility of performing incoherent NSE on biological samples. Lateral lipid diffusion was measured in a fluid phase model membrane system at a length scale of 12Å. Using the high-energy resolution of the NSE technique, we find evidence for two dynamic processes.

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Section: Discussionsupporting

confidence: 78%

Incoherent Neutron Spin-Echo Spectroscopy as an Option to Study Long-Range Lipid Diffusion

et al. 2013

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“…In the presence of Ab42 at 323 K, however, we find a small increase in the lateral diffusion coefficients for the 30%/70% and 40%/60% exo/cyto cholesterol distributions, consistent with previous quasielastic neutron scattering data on Ab25-35 in DMPC/DMPS membranes (44) that showed an increase in lipid mobility caused by the interaction between the bilayer and the Ab peptide itself. In fact comparing our results to that study (44), which measured lateral lipid diffusion coefficients of 50-180 10 À12 m 2 /s over a range of 290-320 K for membranes without cholesterol, our determined values of 7-90 Â 10 À12 m 2 /s over the same temperature range and with cholesterol, and given that the MARTINI CG model dynamics are usually faster, appear reasonable. The one exception is that the lipid lateral diffusion coefficient decreased in the presence of the Ab peptide for the 50%/ 50% exo/cyto, in good agreement with an atomistic MD study (45) that simulated the Ab42 monomer embedded in a bilayer composed of only POPC with symmetrically distributed cholesterol at a 40% concentration.…”

Section: Membrane Thickness and Diffusionsupporting

confidence: 65%

Embedding Aβ42 in Heterogeneous Membranes Depends on Cholesterol Asymmetries

Liguori

Nerenberg

Head‐Gordon

2013

Biophysical Journal

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Using a coarse-grained lipid and peptide model, we show that the free energy stabilization of amyloid-β in heterogeneous lipid membranes is predicted to have a dependence on asymmetric distributions of cholesterol compositions across the membrane leaflets. We find that a highly asymmetric cholesterol distribution that is depleted on the exofacial leaflet but enhanced on the cytofacial leaflet of the model lipid membrane thermodynamically favors membrane retention of a fully embedded Aβ peptide. However, in the case of cholesterol redistribution that increases concentration of cholesterol on the exofacial layer, typical of aging or Alzheimer's disease, the free energy favors peptide extrusion of the highly reactive N-terminus into the extracellular space that may be vulnerable to aggregation, oligomerization, or deleterious oxidative reactivity.

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“…It is also possible that the translocation of Hsp70 into the lipid bilayer may be related to the flipping/flopping of PS across the membrane (De Maio 2011). In this regard, amyloid β peptides have been shown to alter the mobility of PS during interaction with membranes (Buchsteiner et al 2010).…”

Section: Discussionmentioning

confidence: 99%

Interaction of heat shock protein 70 with membranes depends on the lipid environment

Armijo

Okerblom

Cauvi³

et al. 2014

Cell Stress and Chaperones

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Heat shock proteins (hsp) are well recognized for their protein folding activity. Additionally, hsp expression is enhanced during stress conditions to preserve cellular homeostasis. Hsp are also detected outside cells, released by an active mechanism independent of cell death. Extracellular hsp appear to act as signaling molecules as part of a systemic response to stress. Extracellular hsp do not contain a consensus signal for their secretion via the classical ER-Golgi compartment. Therefore, they are likely exported by an alternative mechanism requiring translocation across the plasma membrane. Since Hsp70, the major inducible hsp, has been detected on surface of stressed cells, we propose that membrane interaction is the first step in the export process. The question that emerges is how does this charged cytosolic protein interact with lipid membranes? Prior studies have shown that Hsp70 formed ion conductance pathways within artificial lipid bilayers. These early observations have been extended herewith using a liposome insertion assay. We showed that Hsp70 selectively interacted with negatively charged phospholipids, particularly phosphatidyl serine (PS), within liposomes, which was followed by insertion into the lipid bilayer, forming high-molecular weight oligomers. Hsp70 displayed a preference for less fluid lipid environments and the region embedded into the lipid membrane was mapped toward the Cterminus end of the molecule. The results from our studies provide evidence of an unexpected ability of a large, charged protein to become inserted into a lipid membrane. This observation provides a new paradigm for the interaction of proteins with lipid environments. In addition, it may explain the export mechanism of an increasing number of proteins that lack the consensus secretory signals.

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Alzheimer's disease amyloid-β peptide analogue alters the ps-dynamics of phospholipid membranes

Cited by 42 publications

References 43 publications

Incoherent Neutron Spin-Echo Spectroscopy as an Option to Study Long-Range Lipid Diffusion

Incoherent Neutron Spin-Echo Spectroscopy as an Option to Study Long-Range Lipid Diffusion

Embedding Aβ42 in Heterogeneous Membranes Depends on Cholesterol Asymmetries

Interaction of heat shock protein 70 with membranes depends on the lipid environment

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