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A novel methodology to study nanoporous alumina by small-angle neutron scattering.

ABSTRACT: Nanoporous anodic aluminium oxide (AAO) membranes are promising host systems for confinement of condensed matter. Characterizing their structure and composition is thus of primary importance for studying the behavior of confined objects. Here a novel methodology to extract quantitative information on the structure and composition of well defined AAO membranes by combining small-angle neutron scattering (SANS) measurements and scanning electron microscopy (SEM) imaging is reported. In particular, (i) information about the pore hexagonal arrangement is extracted from SEM analysis, (ii) the best SANS experimental conditions to perform reliable measurements are determined and (iii) a detailed fitting method is proposed, in which the probed length in the fitting model is a critical parameter related to the longitudinal pore ordering. Finally, to validate this strategy, it is applied to characterize AAOs prepared under different conditions and it is shown that the experimental SANS data can be fully reproduced by a core/shell model, indicating the existence of a contaminated shell. This original approach, based on a detailed and complete description of the SANS data, can be applied to a variety of confining media and will allow the further investigation of condensed matter under confinement.

SUBMITTER: Christoulaki A

PROVIDER: S-EPMC6662990 | biostudies-literature |

REPOSITORIES: biostudies-literature

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Microfluidic devices for small-angle neutron scattering.

Project description:A comparative examination is presented of materials and approaches for the fabrication of microfluidic devices for small-angle neutron scattering (SANS). Representative inorganic glasses, metals, and polymer materials and devices are evaluated under typical SANS configurations. Performance criteria include neutron absorption, scattering background and activation, as well as spatial resolution, chemical compatibility and pressure resistance, and also cost, durability and manufacturability. Closed-face polymer photolithography between boron-free glass (or quartz) plates emerges as an attractive approach for rapidly prototyped microfluidic SANS devices, with transmissions up to ∼98% and background similar to a standard liquid cell (I ≃ 10-3 cm-1). For applications requiring higher durability and/or chemical, thermal and pressure resistance, sintered or etched boron-free glass and silicon devices offer superior performance, at the expense of various fabrication requirements, and are increasingly available commercially.

| S-EPMC5988002 | biostudies-literature

Small-angle neutron scattering from CuCrZr coupons and components.

Project description:Small-angle neutron scattering (SANS) is performed to analyse the microstructural state of a reference CuCrZr material with carefully controlled heat treatments, small-scale manufacturing mock-ups of assemblies and high-heat-flux-exposed mock-ups for fusion reactor components. The information derived from the SANS data corresponds well to existing literature data based on microscopic-scale techniques, but is obtained at millimetre scale with minimal surface preparation. The manufacturing method and high-heat-flux testing conditions are confirmed to have little impact on the microstructural properties, demonstrating the validity of these treatments for scaled-up reactor components.

| S-EPMC8493624 | biostudies-literature

Confinement Facilitated Protein Stabilization As Investigated by Small-Angle Neutron Scattering.

Project description:While mesoporous silicas have been shown to be a compelling candidate for drug delivery and the implementation of biotechnological applications requiring protein confinement and immobilization, the understanding of protein behavior upon physical adsorption into silica pores is limited. Many indirect methods are available to assess general adsorbed protein stability, such as Fourier-transform infrared spectroscopy and activity assays. However, the limitation of these methods is that spatial protein arrangement within the pores cannot be assessed. Mesoporous silicas pose a distinct challenge to direct methods, such as transmission electron microscopy, which lacks the contrast and resolution required to adequately observe immobilized protein structure, and nuclear magnetic resonance, which is computationally intensive and requires knowledge of the primary structure a priori. Small-angle neutron scattering can surmount these limitations and observe spatial protein arrangement within pores. Hereby, we observe the stabilization of fluid-like protein arrangement, facilitated by geometry-dependent crowding effects in cylindrical pores of ordered mesoporous silica, SBA-15. Stabilization is induced from a fluid-like structure factor, which is observed for samples at maximum protein loading in SBA-15 with pore diameters of 6.4 and 8.1 nm. Application of this effect for prevention of irreversible aggregation in high concentration environments is proposed.

| S-EPMC6187370 | biostudies-literature

Sub-millisecond time-resolved small-angle neutron scattering measurements at NIST.

Project description:Instrumentation for time-resolved small-angle neutron scattering measurements with sub-millisecond time resolution, based on Gähler's TISANE (time-involved small-angle neutron experiments) concept, is in operation at NIST's Center for Neutron Research. This implementation of the technique includes novel electronics for synchronizing the neutron pulses from high-speed counter-rotating choppers with a periodic stimulus applied to a sample. Instrumentation details are described along with measurements demonstrating the utility of the technique for elucidating the reorientation dynamics of anisometric magnetic particles.

| S-EPMC7312138 | biostudies-literature

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| S-EPMC5541351 | biostudies-literature

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Project description:Magnetic small-angle neutron scattering (SANS) is a powerful technique for investigating magnetic nanoparticle assemblies in nonmagnetic matrices. For such microstructures, the standard theory of magnetic SANS assumes uniformly magnetized nanoparticles (macrospin model). However, there exist many experimental and theoretical studies which suggest that this assumption is violated: deviations from ellipsoidal particle shape, crystalline defects, or the interplay between various magnetic interactions (exchange, magnetic anisotropy, magnetostatics, external field) may lead to nonuniform spin structures. Therefore, a theoretical framework of magnetic SANS of nanoparticles needs to be developed. Here, we report numerical micromagnetic simulations of the static spin structure and related unpolarized magnetic SANS of a single cobalt nanorod. While in the saturated state the magnetic SANS cross section is (as expected) determined by the particle form factor, significant deviations appear for nonsaturated states; specifically, at remanence, domain-wall and vortex states emerge which result in a magnetic SANS signal that is composed of all three magnetization Fourier components, giving rise to a complex angular anisotropy on a two-dimensional detector. The strength of the micromagnetic simulation methodology is the possibility to decompose the cross section into the individual Fourier components, which allows one to draw important conclusions regarding the fundamentals of magnetic SANS.

| S-EPMC5638870 | biostudies-other

Characterization of colloidal structures during intestinal lipolysis using small-angle neutron scattering.

Project description:Bile micelles are thought to mediate intestinal absorption, in part by providing a phase into which compounds can partition. Solubilizing capacity of bile micelles is enhanced during the digestion of fat rich food. We hypothesized that the intestinal digestion of triglycerides causes an increase in volume of micelles that can be quantitatively monitored over the course of digestion using small-angle neutron scattering (SANS), and that SANS can enable evaluation of the contribution of each of the components present during digestion to the size of micelles.SANS was used to characterize the size and shape of micelles present prior to and during the in vitro simulated intestinal digestion of a model food-associated lipid, triolein.Pre-lipolysis mixtures of a bile salt and phospholipid simulating bile concentrations in fed conditions were organized in micelles with an average volume of 40 nm3. During lipolysis, the micelle volume increased 2.5-fold over a 2-h digestion period due to growth in one direction as a result of insertion of monoglycerides and fatty acids. These efforts represent a basis for quantitative mechanistic understanding of changes in solubilizing capacity of the intestinal milieu upon ingestion of a fat-rich meal.

| S-EPMC5627765 | biostudies-literature

Solution Structure of an Intramembrane Aspartyl Protease via Small Angle Neutron Scattering.

Project description:Intramembrane aspartyl proteases (IAPs) comprise one of four families of integral membrane proteases that hydrolyze substrates within the hydrophobic lipid bilayer. IAPs include signal peptide peptidase, which processes remnant signal peptides from nascent polypeptides in the endoplasmic reticulum, and presenilin, the catalytic component of the ?-secretase complex that processes Notch and amyloid precursor protein. Despite their broad biomedical reach, basic structure-function relationships of IAPs remain active areas of research. Characterization of membrane-bound proteins is notoriously challenging due to their inherently hydrophobic character. For IAPs, oligomerization state in solution is one outstanding question, with previous proposals for monomer, dimer, tetramer, and octamer. Here we used small angle neutron scattering (SANS) to characterize n-dodecyl-?-D-maltopyranoside (DDM) detergent solutions containing and absent a microbial IAP ortholog. A unique feature of SANS is the ability to modulate the solvent composition to mask all but the enzyme of interest. The signal from the IAP was enhanced by deuteration and, uniquely, scattering from DDM and buffers were matched by the use of both tail-deuterated DDM and D2O. The radius of gyration calculated for IAP and the corresponding ab initio consensus model are consistent with a monomer. The model is slightly smaller than the crystallographic IAP monomer, suggesting a more compact protein in solution compared with the crystal lattice. Our study provides direct insight into the oligomeric state of purified IAP in surfactant solution, and demonstrates the utility of fully contrast-matching the detergent in SANS to characterize other intramembrane proteases and their membrane-bound substrates.

| S-EPMC5985038 | biostudies-literature

Monomeric Amyloid Beta Peptide in Hexafluoroisopropanol Detected by Small Angle Neutron Scattering.

Project description:Small proteins like amyloid beta (A?) monomers are related to neurodegenerative disorders by aggregation to insoluble fibrils. Small angle neutron scattering (SANS) is a nondestructive method to observe the aggregation process in solution. We show that SANS is able to resolve monomers of small molecular weight like A? for aggregation studies. We examine A? monomers after prolonged storing in d-hexafluoroisopropanol (dHFIP) by using SANS and dynamic light scattering (DLS). We determined the radius of gyration from SANS as 1.0±0.1 nm for A?1-40 and 1.6±0.1 nm for A?1-42 in agreement with 3D NMR structures in similar solvents suggesting a solvent surface layer with 5% increased density. After initial dissolution in dHFIP A? aggregates sediment with a major component of pure monomers showing a hydrodynamic radius of 1.8±0.3 nm for A?1-40 and 3.2±0.4 nm for A?1-42 including a surface layer of dHFIP solvent molecules.

| S-EPMC4769228 | biostudies-literature

Small-angle neutron scattering studies suggest the mechanism of BinAB protein internalization.

Project description:Small-angle neutron scattering (SANS) is one of the most widely used neutron-based approaches to study the solution structure of biological macromolecular systems. The selective deuterium labelling of different protein components of a complex provides a means to probe conformational changes in multiprotein complexes. The Lysinibacillus sphaericus mosquito-larvicidal BinAB proteins exert toxicity through interaction with the receptor Cqm1 protein; however, the nature of the complex is not known. Rationally engineered deuterated BinB (dBinB) protein from the L. sphaericus ISPC-8 species was synthesized using an Escherichia coli-based protein-expression system in M9 medium in D2O for 'contrast-matched' SANS experiments. SANS data were independently analysed by ab initio indirect Fourier transform-based modelling and using crystal structures. These studies confirm the dimeric status of Cqm1 in 100% D2O with a longest intramolecular vector (D max) of ∼94 Å and a radius of gyration (R g) of ∼31 Å. Notably, BinB binds to Cqm1, forming a heterodimeric complex (D max of ∼129 Å and R g of ∼40 Å) and alters its oligomeric status from a dimer to a monomer, as confirmed by matched-out Cqm1-dBinB (D max of ∼70 Å and R g of ∼22 Å). The present study thus provides the first insight into the events involved in the internalization of larvicidal proteins, likely by raft-dependent endocytosis.

| S-EPMC7055391 | biostudies-literature

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