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Sökning: WFRF:(Porcar Lionel)

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2.
  • Berts, Ida, 1984-, et al. (författare)
  • Controlling adsorption of albumin with hyaluronan on silica surfaces and sulfonated latex particles
  • 2017
  • Ingår i: Journal of Colloid and Interface Science. - : Elsevier BV. - 0021-9797 .- 1095-7103. ; 504, s. 315-324
  • Tidskriftsartikel (refereegranskat)abstract
    • Polysaccharides are known to modify binding of proteins at interfaces and this paper describes studies of these interactions and how they are modified by pH. Specifically, the adsorption of human serum albumin on to polystyrene latex and to silica is described, focusing on how this is affected by hyaluronan. Experiments were designed to test how such binding might be modified under relevant physiological conditions. Changes in adsorption of albumin alone and the co-adsorption of albumin and hyaluronan are driven by electrostatic interactions. Multilayer binding is found to be regulated by the pH of the solution and the molecular mass and concentration of hyaluronan. Highest adsorption was observed at pH below 4.8 and for low molecular mass hyaluronan (<= 150 kDa) at concentrations above 2 mg ml(-1). On silica with grafted hyaluronan, albumin absorption is reversed by changes in solvent pH due to their strong electrostatic attraction. Albumin physisorbed on silica surfaces is also rinsed away with dilute hyaluronan solution at pH 4.8. The results demonstrate that the protein adsorption can be controlled both by changes of pH and by interaction with other biological macromolecules.
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4.
  • Dicko, Cedric, et al. (författare)
  • NUrF-Optimization of in situ UV-vis and fluorescence and autonomous characterization techniques with small-angle neutron scattering instrumentation
  • 2020
  • Ingår i: Review of Scientific Instruments. - : AMER INST PHYSICS. - 0034-6748 .- 1089-7623. ; 91:7
  • Tidskriftsartikel (refereegranskat)abstract
    • We have designed, built, and validated a (quasi)-simultaneous measurement platform called NUrF, which consists of neutron small-angle scattering, UV-visible, fluorescence, and densitometry techniques. In this contribution, we illustrate the concept and benefits of the NUrF setup combined with high-performance liquid chromatography pumps to automate the preparation and measurement of a mixture series of Brij35 nonionic surfactants with perfluorononanoic acid in the presence of a reporter fluorophore (pyrene).
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5.
  • Galvagnion, Celine, et al. (författare)
  • Structural characterisation of α-synuclein-membrane interactions and the resulting aggregation using small angle scattering
  • 2024
  • Ingår i: Physical Chemistry, Chemical Physics - PCCP. - : Royal Society of Chemistry. - 1463-9076 .- 1463-9084. ; 26:14, s. 10998-11013
  • Tidskriftsartikel (refereegranskat)abstract
    • The presence of amyloid fibrils is a hallmark of several neurodegenerative diseases. Some amyloidogenic proteins, such as alpha-synuclein and amyloid beta, interact with lipids, and this interaction can strongly favour the formation of amyloid fibrils. In particular the primary nucleation step, i.e. the de novo formation of amyloid fibrils, has been shown to be accelerated by lipids. However, the exact mechanism of this acceleration is still mostly unclear. Here we use a range of scattering methods, such as dynamic light scattering (DLS) and small angle X-ray and neutron scattering (SAXS and SANS) to obtain structural information on the binding of alpha-synuclein to model membranes formed from negatively charged lipids and their co-assembly into amyloid fibrils. We find that the model membranes take an active role in the reaction. The binding of alpha synuclein to the model membranes immediately induces a major structural change in the lipid assembly, which leads to a break-up into small and mostly disc- or rod-like lipid-protein particles. This transition can be reversed by temperature changes or proteolytic protein removal. Incubation of the small lipid-alpha-synuclein particles for several hours, however, leads to amyloid fibril formation, whereby the lipids are incorporated into the amyloid fibrils. alpha S binding to DLPS and DMPS leads to a ms fast reversible deformation into disks and rods. Upon further incubation, lipid rods elongate within the same time scale as that of amyloid formation confirming lipids co-assembly with alpha S into fibrils.
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6.
  • Galvagnion, Céline, et al. (författare)
  • Structural characterisation of α-synuclein-membrane interactions and the resulting aggregation using small angle scattering
  • 2024
  • Ingår i: Physical Chemistry Chemical Physics. - : Royal Society of Chemistry. - 1463-9076 .- 1463-9084. ; 26:14, s. 10998-11013
  • Tidskriftsartikel (refereegranskat)abstract
    • The presence of amyloid fibrils is a hallmark of several neurodegenerative diseases. Some amyloidogenic proteins, such as α-synuclein and amyloid β, interact with lipids, and this interaction can strongly favour the formation of amyloid fibrils. In particular the primary nucleation step, i.e. the de novo formation of amyloid fibrils, has been shown to be accelerated by lipids. However, the exact mechanism of this acceleration is still mostly unclear. Here we use a range of scattering methods, such as dynamic light scattering (DLS) and small angle X-ray and neutron scattering (SAXS and SANS) to obtain structural information on the binding of α-synuclein to model membranes formed from negatively charged lipids and their co-assembly into amyloid fibrils. We find that the model membranes take an active role in the reaction. The binding of α synuclein to the model membranes immediately induces a major structural change in the lipid assembly, which leads to a break-up into small and mostly disc- or rod-like lipid-protein particles. This transition can be reversed by temperature changes or proteolytic protein removal. Incubation of the small lipid-α-synuclein particles for several hours, however, leads to amyloid fibril formation, whereby the lipids are incorporated into the amyloid fibrils.
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7.
  • Gentile, Luigi, et al. (författare)
  • Multilamellar Vesicle Formation from a Planar Lamellar Phase under Shear Flow
  • 2014
  • Ingår i: Langmuir. - : American Chemical Society (ACS). - 0743-7463 .- 1520-5827. ; 30:28, s. 8316-8325
  • Tidskriftsartikel (refereegranskat)abstract
    • The formation of multilamellar vesicles (MLVs) from the lamellar phase of nonionic surfactant system C12E5/D2O under shear flow is studied by time-resolved small angle neutron and light scattering during shear flow. A novel small angle neutron scattering sample environment enables the tracking of the lamellae alignment in the velocity-velocity gradient (1-2) plane during MLV formation, which was tracked independently using flow small angle light scattering commensurate with rheology. During the lamellar-to-multilamellar vesicle transition, the primary Bragg peak from the lamellar ordering was observed to tilt, and this gradually increased with time, leading to an anisotropic pattern with a primary axis oriented at similar to 25 degrees relative to the flow direction. This distorted pattern persists under flow after MLV formation. A critical strain and critical capillary number based on the MLV viscosity are demonstrated for MLV formation, which is shown to be robust for other systems as well. These novel measurements provide fundamentally new information about the flow orientation of lamellae in the plane of flow that cannot be anticipated from the large body of previous literature showing nearly isotropic orientation in the 2,3 and 1,3 planes of flow. These observations are consistent with models for buckling-induced MLV formation but suggest that the instability is three-dimensional, thereby identifying the mechanism of MLV formation in simple shear flow.
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8.
  • Hellsing, Maja S., et al. (författare)
  • Crystalline order of polymer nanoparticles over large areas at solid/liquid interfaces
  • 2012
  • Ingår i: Applied Physics Letters. - : AIP Publishing. - 0003-6951 .- 1077-3118. ; 100:22, s. 221601-
  • Tidskriftsartikel (refereegranskat)abstract
    • We report on the formation of large two-dimensional domains (about 20 cm2) of oriented and ordered structures of polystyrene particles dispersed in water at a solid/liquid interface.  Gentle flow of the dispersed sample into the holder at a shear strain rate of about 0.1 s−1 caused particles at the air/latex meniscus to self-assemble in a regular structure on both solid silica or alumina surfaces.  Scattering experiments show that the particle separation at the surface was the same as in the bulk and determined by repulsion arising from the charges on the particles.  Close-packed planes formed parallel to the interface.
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9.
  • Hellsing, Maja S., et al. (författare)
  • Scattering from Dilute and Lamellar Phase Solutions of Aerosol-OT Simultaneous Probe of Surface Structures and Bulk
  • 2011
  • Ingår i: Trends in colloid andinterface science XXIV. - Berlin, Heidelberg : Springer Berlin Heidelberg. - 9783642190377 ; , s. 139-142
  • Konferensbidrag (refereegranskat)abstract
    • The benefits of simultaneous studies of adsorbed layers and bulk structures are shown for solutions of the surfactant Aerosol-OT. Above the critical micelle concentration, Aerosol-OT forms an aligned lamellar phase at the sapphire/solution interface which is in equilibrium with a bulk phase that consists of coexisting micellar solution and dispersed lamellar phase. Measurements of the aligned surface layers and the bulk scattering from a 2% wt solution by grazing incidence and small-angle neutron scattering show that the bulk consist of lamellar structures with the same d-spacing as seen at the surface but without the surface induced alignment. The surface lamellar structure corresponds to a 10% volume fraction for a 2% wt bulk which implies that there must be coexistence of regions of different concentration. Scattering patterns measured in grazing incidence geometry clearly show the relative contributions from small-angle scattering and specular reflectivity.
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10.
  • Hellsing, Maja S., et al. (författare)
  • Structure of flocs of latex particles formed by addition of protein from Moringa seeds
  • 2014
  • Ingår i: Colloids and Surfaces A: Physicochemical and Engineering Aspects. - : Elsevier BV. - 0927-7757 .- 1873-4359. ; 460, s. 460-467
  • Tidskriftsartikel (refereegranskat)abstract
    • Proteins extracted from the seeds of Moringa trees are effective flocculents for particles dispersed in water and are attractive as a natural and sustainable product for use in water purification. Studies with a model system consisting of polystyrene latex particles have shown that the protein adsorbs to the surface and causes flocculation as unusually dense aggregates. Small-angle neutron scattering that exploits contrast matching of deuterated latex particles dispersed in D2O to highlight bound protein has shown that the adsorbed amount reaches about 3 mg m(-2). The particles form very compact flocs that are characterized by fractal dimensions that approach the theoretical maximum of 3. Ultra small-angle neutron scattering allows these flocs to be characterized for a range of particle and protein concentrations. Proteins from two species of Moringa trees were investigated. The protein from Moringa stenopetala seeds gave rise to slightly lower fractal dimensions compared to Moringa oleifera, but still much larger than values observed for conventional ionic or polymeric flocculents that are in the range 1.75-2.3. Compact flocs are desirable for efficient separation of impurities and dewatering of sludge as well as other applications. A trend of increasing fractal dimension with particle concentration was observed when M. stenopetala seed protein was used and this resembles the behaviour predicted in Brownian dynamics simulation of flocculation. (C) 2013 The Authors. Published by Elsevier B.V. All rights reserved.
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