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Sökning: WFRF:(Rennie Adrian. R)

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  • Ericsson, A., et al. (författare)
  • Crystallization of a Zr-based metallic glass produced by laser powder bed fusion and suction casting
  • 2021
  • Ingår i: Journal of Non-Crystalline Solids. - : Elsevier. - 0022-3093 .- 1873-4812. ; 571
  • Tidskriftsartikel (refereegranskat)abstract
    • The crystallization behaviour during low temperature annealing of samples of the Zr59.3Cu28.8Al10.4Nb1.5 (at%) bulk metallic glass produced by suction casting and the laser powder bed fusion (LPBF) process were studied with small angle neutron scattering (SANS), X-ray diffraction and scanning electron microscopy. The in-situ SANS measurements during isothermal annealing reveals that the phase separation in the LPBF processed material proceeds at a smaller characteristic length-scale than the cast material. Quantitative analysis of the SANS data shows that, while the crystallization process in both materials proceed through rapid nucleation followed by diffusion limited growth, the LPBF processed material crystallizes with a smaller cluster size and at a higher rate. The smaller cluster size is attributed to the elevated oxygen content in the LPBF processed material which reduces the nucleation barrier and thus the thermal stability.
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4.
  • Hemming, Joanna M., et al. (författare)
  • Environmental Pollutant Ozone Causes Damage to Lung Surfactant Protein B (SP-B)
  • 2015
  • Ingår i: Biochemistry. - : American Chemical Society (ACS). - 0006-2960 .- 1520-4995. ; 54:33, s. 5185-5197
  • Tidskriftsartikel (refereegranskat)abstract
    • Lung surfactant protein B (SP-B) is an essential protein found in the surfactant fluid at the air water interface of the lung. Exposure to the air pollutant ozone could potentially damage SP-B and lead to respiratory distress. We have studied two peptides, one consisting of the N-terminus of SP-B [SP-B(1-25)] and the other a construct of the N- and C-termini of SP-B [SP-B-(1-25,B-63-78)], called SMB. Exposure to dilute levels of ozone (similar to 2 ppm) of monolayers of each peptide at the air water interface leads to a rapid reaction, which is evident from an increase in the surface tension. Fluorescence experiments revealed that this increase in surface tension is accompanied by a loss of fluorescence from the tryptophan residue at the interface. Neutron and X-ray reflectivity experiments show that, in contrast to suggestions in the literature, the peptides are not solubilized upon oxidation but rather remain at the interface with little change in their hydration. Analysis of the product material reveals that no cleavage of the peptides occurs, but a more hydrophobic product is slowly formed together with an increased level of oligomerization. We attributed this to partial unfolding of the peptides. Experiments conducted in the presence of phospholipids reveal that the presence of the lipids does not prevent oxidation of the peptides. Our results strongly suggest that exposure to low levels of ozone gas will damage SP-B, leading to a change in its structure. The implication is that the oxidized protein will be impaired in its ability to interact at the air water interface with negatively charged phosphoglycerol lipids, thus compromising what is thought to be its main biological function.
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5.
  • Larsen, Simon R., et al. (författare)
  • Sample cell for studying liquid interfaces with an in situ electric field using X-ray reflectivity and application to clay particles at oil–oil interfaces
  • 2018
  • Ingår i: Journal of Synchrotron Radiation. - 0909-0495 .- 1600-5775. ; 25:Part: 3, s. 915-917
  • Tidskriftsartikel (refereegranskat)abstract
    • Commissioning results of a liquid sample cell for X-ray reflectivity studies with an in situ applied electrical field are presented. The cell consists of a Plexiglas container with lateral Kapton windows for air-liquid and liquid-liquid interface studies, and was constructed with grooves to accept plate electrodes on the walls parallel to the direction of the beam. Both copper and ITO plate electrodes have been used, the latter being useful for simultaneous optical studies. Commissioning tests were made at the I07 beamline of the Diamond Light Source.
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6.
  • Thompson, Katherine C., et al. (författare)
  • Degradation and Rearrangement of a Lung Surfactant Lipid at the Air-Water Interface during Exposure to the Pollutant Gas Ozone
  • 2013
  • Ingår i: Langmuir. - : American Chemical Society (ACS). - 0743-7463 .- 1520-5827. ; 29:14, s. 4594-4602
  • Tidskriftsartikel (refereegranskat)abstract
    • The presence of unsaturated lipids in lung surfactant is important for proper respiratory function. In this work, we have used neutron reflection and surface pressure measurements to study the reaction of the ubiquitous pollutant gas-phase ozone, 03, with pure and mixed phospholipid monolayers at the air-water interface. The results reveal that the reaction of the unsaturated lipid 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine, POPC, with ozone leads to the rapid loss of the terminal C9 portion of the oleoyl strand of POPC from the air-water interface. The loss of the C9 portion from the interface is accompanied by an increase in the surface pressure (decrease in surface tension) of the film at the air-water interface. The results suggest that the portion of the oxidized oleoyl strand that is still attached to the lipid headgroup rapidly reverses its orientation and penetrates the air-water interface alongside the original headgroup, thus increasing the surface pressure. The reaction of POPC with ozone also leads to a loss of material from the palmitoyl strand, but the loss of palmitoyl material occurs after the loss of the terminal C9 portion from the oleoyl strand of the molecule, suggesting that the palmitoyl material is lost in a secondary reaction step. Further experiments studying the reaction of mixed monolayers composed of unsaturated lipid POPC and saturated lipid dipalmitoyl-sn-glycero-3-phosphocholine, DPPC, revealed that no loss of DPPC from the air-water interface occurs, eliminating the possibility that a reactive species such as an OH radical is formed and is able to attack nearby lipid chains. The reaction of ozone with the mixed films does cause a significant change in the surface pressure of the air-water interface. Thus, the reaction of unsaturated lipids in lung surfactant changes and impairs the physical properties of the film at the air-water interface.
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7.
  • Thompson, Katherine C., et al. (författare)
  • Reaction of a Phospholipid Monolayer with Gas-Phase Ozone at the Air-Water Interface : Measurement of Surface Excess and Surface Pressure in Real Time
  • 2010
  • Ingår i: Langmuir. - : American Chemical Society (ACS). - 0743-7463 .- 1520-5827. ; 26:22, s. 17295-17303
  • Tidskriftsartikel (refereegranskat)abstract
    • The reaction between gas-phase ozone and monolayers of the unsaturated lipid 1-palmitoy1-2-oleoyl-sn-glycero-3-phosphocholine, POPC, on aqueous solutions has been studied in real time using neutron reflection and surface pressure measurements. The reaction between ozone and lung surfactant, which contains POPC, leads to decreased pulmonary function, but little is known shout the changes that occur to the interfacial material as a result of oxidation. The results reveal that the initial reaction of ozone with POPC leads to a rapid increase in surface pressure followed by a slow decrease to very low values. The neutron reflection measurements, performed on an isotopologue of POPC with a selectively deuterated palmitoyl strand, reveal that the reaction leads to loss of this strand from the air-water interface. suggesting either solubilization of the product lipid or degradation of the palmitoyl strand by a reactive species. Reactions of H-1-POPC on D2O reveal that the headgroup region of the lipids in aqueous solution is not dramatically perturbed by the reaction of POPC monolayers with ozone supporting degradation of the palmitoyl strand rather than solubilization. The results are consistent with the reaction of ozone with the oleoyl strand of POPC at the air water interface leading to the formation of OH radicals. the highly reactive OH radicals produced can then go on to react with the saturated palmitoyl strands leading to the formation or oxidized lipids with shorter alkyl tails.
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8.
  • Ainalem, Marie-Louise, et al. (författare)
  • On the Ability of PAMAM Dendrimers and Dendrimer/DNA Aggregates To Penetrate POPC Model Biomembranes
  • 2010
  • Ingår i: Journal of Physical Chemistry B. - : American Chemical Society (ACS). - 1520-6106 .- 1520-5207. ; 114:21, s. 7229-7244
  • Tidskriftsartikel (refereegranskat)abstract
    • Poly(amido amine) (PAMAM) dendrimers have previously been shown, as cationic condensing agents of DNA, to have high potential for nonviral gene delivery. This study addresses two key issues for gene delivery: the interaction of the biomembrane with (i) the condensing agent (the cationic PAMAM dendrimer) and (ii) the corresponding dendrimer/DNA aggregate. Using in situ null ellipsometry and neutron reflection, parallel experiments were carried out involving dendrimers or generations 2 (G2), 4 (G4), and 6 (G6). The study demonstrates that free dendrimers of all three generations were able to traverse supported palmitoyloleoylphosphatidylcholine (POPC) bilayers deposited on silica surfaces. The model biomembranes were elevated front the solid surfaces upon dendrimer penetration, which offers a promising new way to generate more realistic model biomembranes where the contact with the supporting surface is reduced and where aqueous cavities are present beneath the bilayer. The largest dendrimer (GO) induced partial bilayer destruction directly upon penetration, whereas the smaller dendrimers (G2 and G4) leave the bilayer intact, so we propose that lower generation dendrimers have greater potential as transfection mediators. In addition to the experimental observations, coarse-grained simulations on the interaction between generation 3 (03) dendrimers and POPC bilayers were performed in the absence and presence of a bilayer-supporting negatively charged surface that emulates the support. The simulations demonstrate that G3 is transported across free-standing POPC bilayers by direct penetration and not by endocytosis. The penetrability was, however, reduced in the presence of a surface, indicating that the membrane transport observed experimentally was not driven solely by the surface. The experimental reflection techniques were also applied to dendrimer/DNA aggregates of charge ratio = 0.5, and while G2/DNA and G4/DNA aggregates interact with POPC bilayers. G6/DNA displays no such interaction. These results indicate that, in contrast to free dendrimer molecules, dendrimer/DNA aggregates of low charge ratios are not able to traverse a membrane by direct penetration.
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  • 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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