Anomalous and anisotropic nanoscale diffusion of hydration water molecules in fluid lipid membranes

Toppozini, Laura; Roosen-Runge, Felix; Bewley, Robert; Dalgliesh, Robert M.; Perring, T. G.; Seydel, Tilo; Glyde, H. R.; Sakai, Victoria García; Rheinstädter, Maikel C.

doi:10.1039/c5sm01713k

Cited by 37 publications

(30 citation statements)

References 70 publications

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“…There exists an analytical form of the Fourier transform of Eq. (53) ( Kneller and Hinsen, 2004) (without resolution function term), but practically its calculation is often performed numerically (Toppozini et al, 2015;Ameseder et al, 2018b). To describe non-exponential relaxations, also the fractional Brownian dynamics (FBD) model can be employed.…”

Section: Localized Internal Dynamicsmentioning

confidence: 99%

Dynamics of proteins in solution

Grimaldo

Roosen-Runge

Zhang

et al. 2019

Quart. Rev. Biophys.

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164

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The dynamics of proteins in solution includes a variety of processes, such as backbone and side-chain fluctuations, interdomain motions, as well as global rotational and translational (i.e. center of mass) diffusion. Since protein dynamics is related to protein function and essential transport processes, a detailed mechanistic understanding and monitoring of protein dynamics in solution is highly desirable. The hierarchical character of protein dynamics requires experimental tools addressing a broad range of time- and length scales. We discuss how different techniques contribute to a comprehensive picture of protein dynamics, and focus in particular on results from neutron spectroscopy. We outline the underlying principles and review available instrumentation as well as related analysis frameworks.

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Section: Localized Internal Dynamicsmentioning

confidence: 99%

Dynamics of proteins in solution

Grimaldo

Roosen-Runge

Zhang

et al. 2019

Quart. Rev. Biophys.

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164

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“…Due to interactions with the bilayer, membrane hydration water has distinct properties as compared to bulk water, such as structure, freezing temperature, and dynamics. 38,39 The distance between lipid chains can be determined from the position of the acyl chain correlation peak while the width of the peak is related to the packing density in the hydrocarbon core. Values for a T , Da T , as well as the area and the volume per lipid acyl chain are given in Table 2.…”

Section: X-ray Diffractionmentioning

confidence: 99%

Amyloid-β_25–35peptides aggregate into cross-β sheets in unsaturated anionic lipid membranes at high peptide concentrations

et al. 2016

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One of the hallmarks of Alzheimer's disease is the formation of protein plaques in the brain, which mainly consist of amyloid-β peptides of different lengths. While the role of these plaques in the pathology of the disease is not clear, the mechanism behind peptide aggregation is a topic of intense research and discussion. Because of their simplicity, synthetic membranes are promising model systems to identify the elementary processes involved. We prepared unsaturated zwitterionic/anionic lipid membranes made of 1-palmitoyl-2-oleoyl-sn-glycero-phosphocholine (POPC) and 1,2-dimyristoyl-sn-glycero-3-phospho-l-serine (DMPS) at concentrations of POPC/3 mol% DMPS containing 0 mol%, 3 mol%, 10 mol%, and 20 mol% amyloid-β25-35 peptides. Membrane-embedded peptide clusters were observed at peptide concentrations of 10 and 20 mol% with a typical cluster size of ∼11 μm. Cluster density increased with peptide concentration from 59 (±3) clusters per mm(2) to 920 (±64) clusters per mm(2), respectively. While monomeric peptides take an α-helical state when embedded in lipid bilayers at low peptide concentrations, the peptides in peptide clusters were found to form cross-β sheets and showed the characteristic pattern in X-ray experiments. The presence of the peptides was accompanied by an elastic distortion of the bilayers, which can induce a long range interaction between the peptides. The experimentally observed cluster patterns agree well with Monte Carlo simulations of long-range interacting peptides. This interaction may be the fundamental process behind cross-β sheet formation in membranes and these sheets may serve as seeds for further growth into amyloid fibrils.

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“…For over 25 years, QENS has provided an important complement to other techniques such as NMR by probing the water dynamics at time scales in the 10 9 -10 13 s range. [1][2][3][4][5][6][7] For example, the wave vector (Q) dependence of QENS inaccessible to NMR can be used to infer the length scale of the water motion and to distinguish between different types of translational and rotational motion.…”

Section: Introductionmentioning

confidence: 99%

“…[1][2][3][4][5][6][7] Unfortunately, the complexity of these samples renders them difficult to model by molecular dynamics (MD) simulations and to characterize by Atomic Force Microscopy (AFM). The sheer number of membranes, the interactions between the membranes in a stack, and the presence of unknown amounts of water between the membranes render modeling of their water dynamics by computer simulation virtually impossible.…”

Section: Introductionmentioning

confidence: 99%

On the structure and dynamics of water associated with single-supported zwitterionic and anionic membranes

Miskowiec

Buck

Hansen

et al. 2017

The Journal of Chemical Physics

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We have used high-resolution quasielastic neutron scattering (QENS) to investigate the dynamics of water molecules (time scale of motion ∼10-10 s) in proximity to single-supported bilayers of the zwitterioniclipid DMPC (1,2-dimyristoyl-sn-glycero-3-phosphorylcholine) and the anionic lipid DMPG (1,2-dimyristoyl-sn-glycero-3-phosphoglycerol) in the temperature range 160-295 K. For both membranes, the temperature dependence of the intensity of neutronsscattered elastically and incoherently from these samples indicates a series of freezing/melting transitions of the membrane-associated water, which have not been observed in previous studies of multilayer membranes. We interpret these successive phase transitions as evidence of different types of water that are common to the two membranes and which are defined by their local environment: bulk-like water located furthest from the membrane and two types of confined water in closer proximity to the lipids. Specifically, we propose a water type termed "confined 2" located within and just above the lipid head groups of the membrane and confined 1 water that lies between the bulk-like and confined 2 water. Confined 1 water is only present at temperatures below the freezing point of bulk-like water. We then go on to determine the temperature dependence of the translational diffusion coefficient of the water associated with single-supported DMPG membranes containing two different amounts of water as we have previously done for DMPC. To our knowledge, there have been no previous studies comparing the dynamics of water in proximity to zwitterionic and anionic membranes. Our analysis of the water dynamics of the DMPG and DMPC membranes supports the classification of water types that we have inferred from their freezing/melting behavior. However, just as we observe large differences in the freezing/melting behavior between these model membranes for the same water type, our measurements demonstrate variation between these membranes in the dynamics of their associated water over a wide temperature range. In particular, there are differences in the diffusive motion of water closest to the lipid head groups. Previously, QENS spectra of the DMPC membranes have revealed the motion of water bound to the lipid head groups. For the DMPG membrane, we have found some evidence of such bound water molecules; but the signal is too weak for a quantitative analysis. However, we observe confined 2 water in the DMPG membrane to undergo slow translational diffusion in the head group region, which was unobserved for DMPC. The weak temperature dependence of its translational diffusion coefficient allows extrapolation to physiological temperatures for comparison with molecular dynamics simulations.

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Anomalous and anisotropic nanoscale diffusion of hydration water molecules in fluid lipid membranes

Cited by 37 publications

References 70 publications

Dynamics of proteins in solution

Dynamics of proteins in solution

Amyloid-β_25–35peptides aggregate into cross-β sheets in unsaturated anionic lipid membranes at high peptide concentrations

On the structure and dynamics of water associated with single-supported zwitterionic and anionic membranes

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Anomalous and anisotropic nanoscale diffusion of hydration water molecules in fluid lipid membranes

Cited by 37 publications

References 70 publications

Dynamics of proteins in solution

Dynamics of proteins in solution

Amyloid-β25–35peptides aggregate into cross-β sheets in unsaturated anionic lipid membranes at high peptide concentrations

On the structure and dynamics of water associated with single-supported zwitterionic and anionic membranes

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Product

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Amyloid-β_25–35peptides aggregate into cross-β sheets in unsaturated anionic lipid membranes at high peptide concentrations