Small Angle Neutron Scattering Study Research Articles

A library of benzimidazole based amide and urea derivatives as supramolecular gelators – A comparative study

We present a set of alkyl chain functionalized benzimidazole based compounds containing amide and urea functional groups which were screened for their gelation behaviour. Both the sets bear similar molecular scaffolds, making them an excellent tool for determining the role of the supramolecular interactions involved in the gelation process. All the compounds were characterised using physico-chemical techniques like NMR and FT-IR. The gels were subjected to small angle neutron scattering studies (SANS), rheological studies, SEM and FT-IR. In order to rationalize the gelation behaviour, solvent parameter studies were conducted. The results show a dependence on refractive index of solvent, polarizability and dispersion interactions. The respective orientation of amide and conformation in urea based compounds were explored and studied using computational calculations and their corresponding effect on the resulting supramolecular superstructures was scrutinized. The compounds were also explored to act as chemosensor for selective detection of mercuric ions with exceptionally low LOD (limit of detection) values.

Correlative Low-dose Cryogenic Electron Microscopy and Small Angle Neutron Scattering Studies Reveal Morphological Differences in Fluorinated vs Non-fluorinated Fire Suppressant Foams.

Correlative Low-dose Cryogenic Electron Microscopy and Small Angle Neutron Scattering Studies Reveal Morphological Differences in Fluorinated vs Non-fluorinated Fire Suppressant Foams.

A Small-Angle Neutron Scattering, Calorimetry and Densitometry Study to Detect Phase Boundaries and Nanoscale Domain Structure in a Binary Lipid Mixture

Techniques that can probe nanometer length scales, such as small-angle neutron scattering (SANS), have become increasingly popular to detect phase separation in membranes. But to extract the phase composition and domain structure from the SANS traces, complementary information is needed. Here, we present a SANS, calorimetry and densitometry study of a mixture of two saturated lipids that exhibits solidus-liquidus phase coexistence: 1,2-dipalmitoyl-d62-sn-glycero-3-phosphocholine (dDPPC, tail-deuterated DPPC) and 1,2-dilauroyl-sn-glycero-3-phosphocholine (DLPC). With calorimetry, we investigated the phase diagram for this system and found that the boundary traces for both multilamellar vesicles (MLVs) as well as 50 nm unilamellar vesicles overlap. Because the solidus boundary was mostly inaccessible by calorimetry, we investigated it by both SANS and molecular volume measurements for a 1:1 dDPPC:DLPC lipid mixture. From the temperature behavior of the molecular volume for the 1:1 dDPPC:DLPC mixture, as well as the individual molecular volume of each lipid species, we inferred that the liquidus phase consists of only fluid-state lipids while the solidus phase consists of lipids that are in gel-like states. Using this solidus-liquidus phase model, the SANS data were analyzed with an unrestricted shape model analysis software: MONSA. The resulting fits show irregular domains with dendrite-like features as those previously observed on giant unilamellar vesicles (GUVs). The surface pair correlation function describes a characteristic domain size for the minority phase that decreases with temperature, a behavior found to be consistent with a concomitant decrease in membrane mismatch between the liquidus and solidus phases.

Protein-Surfactant and Protein-Protein Interactions During Freeze and Thaw: A Small-Angle Neutron Scattering Study of Lysozyme Solutions with Polysorbate and Poloxamer

Protein structural changes during freezing and subsequent thawing are of great importance to a variety of biopharmaceutical applications. In this work, we studied the influence of non-ionic surfactants (polysorbate 20 and poloxamer 188) on protein structural changes during freeze and thaw using lysozyme as a model protein. Small-angle neutron scattering was employed to characterize protein structures in both liquid and frozen solution states. The results show minimal impact of polysorbate 20 on lysozyme structures during freeze and thaw using practically relevant concentrations. Polysorbate 20 used at 0.04% (w/w) completely prevents freeze-induced aggregation of lysozyme. Poloxamer 188 seems to interact with lysozyme; when applied at high concentrations (10% w/w), such interaction prevents protein crowding or close packing typically associated with freeze concentration. Despite such interactions, lysozyme aggregation is observed with 10% (w/w) of poloxamer 188 during freezing, although the aggregation is reversed upon thawing.

SANS Studies of the Gallium-Indium Alloy Structure within Regular Nanopores.

Potential applications of nanolattices often require filling their empty space with eutectic metallic alloys. Due to confinement to nanolattices, the structure of phase segregates in eutectic alloys can differ from that in bulk. These problems are poorly understood now. We have used small angle neutron scattering (SANS) to study the segregation in the Ga-In alloy confined to an opal template with the regular pore network, created by a strict regularity of opal constituents in close similarity with nanolattices. We showed that SANS is a powerful tool to reveal the configuration of segregated phases within nanotemplates. The In-rich segregates were found to have specific structural features as small sizes and ordered arrangement.

Interaction among bovine serum albumin (BSA) molecules in the presence of anions: a small-angle neutron scattering study.

Protein-protein interaction in solution strongly depends on dissolved ions and solution pH. Interaction among globular protein (bovine serum albumin, BSA), above and below of its isoelectric point (pI ≈ 4.8), is studied in the presence of anions (Cl-, Br-, I-, F-, SO42-) using small-angle neutron scattering (SANS) technique. The SANS study reveals that the short-range attraction among BSA molecules remains nearly unchanged in the presence of anions, whereas the intermediate-range repulsive interaction increases following the Hofmeister series of anions. Although the interaction strength modifies below and above the pI of BSA, it nearly follows the series.

Monitoring food structure in plant protein gels during digestion: Rheometry and Small Angle Neutron Scattering studies

We studied rheology and nanostructures (by Small Angle Neutron Scattering) of heat-set canola seed protein gels, containing cruciferin and napin, prepared at pH 8 and pH 11. We focused on gastric and intestinal digestion of 10 mm pieces, mimicking human gastro-intestinal tract. Stronger gels, prepared at pH 11 (above the isoelectric points (IEP), of both proteins), retained local folded and compact conformations, close to native ones. Preparation at pH 8 (below napin's IEP but above cruciferin's one), could destabilize conformations due to charge differences of the proteins. For preparation pH 8, proteins were almost unfolded, and the gel softer. In gastric digestion, modulus decreased for pH 8 gels, but surprisingly, increased for pH 11. We propose a competition between unfolding, increasing local interactions (hence the modulus), and enzymatic scission. Scission could be less efficient for pH 11 gels, with less unfolded proteins and higher crosslink density, hindering enzymatic diffusion. Additional interactions could result from crossing one or two IEPs, towards gastric pH 2. For intestinal digestion, the two gels behave similar (proteins re-compaction and modulus decrease). Beyond loss of submicronic connectivity, external erosion of the gel for largest times is observed, but less on SANS, which involves the center of the piece. • Following SANS, we can prepare gels of different structures, with proteins either compact (pH 11) or unfolded (pH 8). • Gastric digestion provoked different protein evolutions for the two gels: unfolding (pH 11) or local aggregation (pH 8). • Opposed rheological behaviors in gastric step for the two pH : increase of G’ for pH 11 gel linked to unfolding. • For both pH gels, intestinal digestion results in protein re-compaction, together with rapid and progressive loss of moduli. • Stronger resistance of pH 11 gel is associated to hindering of enzymatic scission: folded proteins and denser network.

Small-Angle Neutron Scattering Study of the Structural Relaxation of Elongationally Oriented, Moderately Stretched Three-Arm Star Polymers.

We present structural relaxation studies of a polystyrene star polymer after cessation of high-rate extensional flow. During the steady-state flow, the scattering pattern shows two sets of independent correlations peaks, reflecting the structure of a polymer confined in a fully oriented three-armed tube. Upon cessation of flow, the relaxation constitutes three distinct regimes. In a first regime, the perpendicular correlation peaks disappear, signifying disruption of the virtual tube. In a second regime, broad scattering arcs emerge, reflecting relaxation from highly aligned chains to more relaxed, still anisotropic form. New entanglements dominate the last relaxation regime where the scattering pattern evolves to a successively elliptical and circular pattern, reflecting relaxation via reptation.

Small-Angle Neutron Scattering Study of Graphene-Nanodiamond Composites for Biosensor and Electronic Applications

Small-Angle Neutron Scattering Study of Graphene-Nanodiamond Composites for Biosensor and Electronic Applications

Structural Insights into Polymethacrylamide-Based LCST Polymers in Solution: A Small-Angle Neutron Scattering Study

Structural Insights into Polymethacrylamide-Based LCST Polymers in Solution: A Small-Angle Neutron Scattering Study

Structure and Interactions in Perfluorooctanoate Micellar Solutions Revealed by Small-Angle Neutron Scattering and Molecular Dynamics Simulations Studies: Effect of Urea.

The self-assembly of surfactants in aqueous solution can be modulated by the presence of additives including urea, which is a well-known protein denaturant and also present in physiological fluids and agricultural runoff. This study addresses the effects of urea on the structure of micelles formed in water by the fluorinated surfactant perfluoro-n-octanoic acid ammonium salt (PFOA). Analysis of small-angle neutron scattering (SANS) experiments and atomistic molecular dynamics (MD) simulations provide consensus strong evidence for the direct mechanism of urea action on micellization: urea helps solvate the hydrophobic micelle core by localizing at the surface of the core in the place of some water molecules. Consequently, urea decreases electrostatic interactions at the micelle shell, changes the micelle shape from prolate ellipsoid to sphere, and decreases the number of surfactant molecules associating in a micelle. These findings inform the interactions and behavior of surface active per- and polyfluoroalkyl substances (PFAS) released in the aqueous environment and biota.

Nanoscale Domain Structure in a Binary Lipid Mixture: A Small Angle Neutron Scattering and Calorimetry Study

In biological membranes the lipid composition is extraordinarily complex and this complexity provides proteins with the optimal lipid micro environment for physiological activity. The complexity of lipid composition and the consequences for biological systems has attracted significant interest in the past four decades. Here, however, we chose to revisit a simple binary mixture of lipids (DPPC and DLPC) which is still relevant since some biological systems can be relatively simple, composed of only a few different lipid species which form nanodomain when the temperature is decreased.

Small-Angle X-Ray Scattering (Saxs) and Small-Angle Neutron Scattering (Sans) Study on the Structure of Sodium Caseinate in Dispersions and at the Oil-Water Interface: Effect of Calcium Ions

Small-Angle X-Ray Scattering (Saxs) and Small-Angle Neutron Scattering (Sans) Study on the Structure of Sodium Caseinate in Dispersions and at the Oil-Water Interface: Effect of Calcium Ions

Designing sub-20 nm self-assembled nanocarriers for small molecule delivery: Interplay among structural geometry, assembly energetics, and cargo release kinetics

Biological constraints in diseased tissues have motivated the need for small nanocarriers (10–30 nm) to achieve sufficient vascular extravasation and pervasive tumor penetration. This particle size limit is only an order of magnitude larger than small molecules, such that cargo loading is better described by co-assembly processes rather than simple encapsulation. Understanding the structural, kinetic, and energetic contributions of carrier-cargo co-assembly is thus critical to achieve molecular-level control towards predictable in vivo behavior. These interconnected set of properties were systematically examined using sub-20 nm self-assembled nanocarriers known as three-helix micelles (3HM). Both hydrophobicity and the “geometric packing parameter” dictate small molecule compatibility with 3HM's alkyl tail core. Planar obelisk-like apomorphine and doxorubicin (DOX) molecules intercalated well within the 3HM core and near the core-shell interface, forming an integral component to the co-assembly, as corroborated by small-angle X-ray and neutron-scattering structural studies. DOX promoted crystalline alkyl tail ordering, which significantly increased (+63%) the activation energy of 3HM subunit exchange. Subsequently, 3HM-DOX displayed slow-release kinetics (t1/2 = 40 h) at physiological temperatures, with ~50× greater cargo preference for the micelle core as described by two drug partitioning coefficients (micellar core/shell Kp1 ~ 24, and shell/bulk solvent Kp2 ~ 2). The geometric and energetic insights between nanocarrier and their small molecule cargos developed here will aid in broader efforts to deconvolute the interconnected properties of carrier-drug co-assemblies. Adding this knowledge to pharmacological and immunological explorations will expand our understanding of nanomedicine behavior throughout all the physical and in vivo processes they are intended to encounter.

Structural Change of Apoferritin as the Effect of pH Change: DLS and SANS Study

Apoferritin is a complex protein potential for drug delivery application. The advantage of apoferritin lies in its core-shell structure, its nano size, and its pH-sensitivity. This study was aimed to characterize the structure of apoferritin due to the pH alteration effect in a solution using dynamic light scattering (DLS) and small-angle neutron scattering (SANS). Both DLS and SANS can observe protein size in solution near its physiological condition. The results show that apoferritin possesses a core-shell structure with a diameter of around 12–13 nm at pH 7. The dissociation of apoferritin occurs at pH 1.9. The SANS data shows the apoferritin at pH 1.9 was dissociated into the smaller oligomer. The structure of this smaller oligomer has a different configuration than the configuration of apoferritin subunits at pH 7. It can cause the failure of reassembly of apoferritin if the apoferritin is neutralized back to pH 7 after dissociation from pH 1.9.

Small Angle Neutron Scattering Study of Nanoscale Structure of Low-Carbon Steel After Rolling with Shear Followed by Cold Drawing

Small angle neutron scattering was applied to steel produced by rolling with shear (RS) technology and compared to samples produced by standard technology (ST). Based on small angle neutron scattering measurements the morphology of the grains and pores of RS steels were compared to those of the ST steels. The scattering in small scattering vector region showed anisotropy, attributed to the elongation of the pores; the pearlite lamellae distances along and perpendicular to the rolling directions differed by a factor of 1.5. The results of the Small angle neutron scattering measurements were in accordance with the electrical characteristics of the specimens. They showed smaller and less anisotropic average sizes of the cracks and nanopores for the RS samples than for the ST rods. This confirms the dynamic healing of the nanosized defects during the cold drawing of the RS rods. This fundamental result shows that during severe plastic deformation a cyclic process of nucleation and healing of the nanovoids took place. However, during the standard deformation process only nucleation of the nanovoids is present.

Small-Angle Neutron Scattering Study of High Fat Fish Oil-In-Water Emulsion Stabilized with Sodium Caseinate and Phosphatidylcholine.

We report on small-angle neutron scattering (SANS) investigations of separate phase domains in high fat (70%) oil-in-water emulsions emulsified with the combination of sodium caseinate (CAS) and phosphatidylcholine (PC). The emulsion as a whole was studied by contrast variation to identify scattering components dominated by individual emulsifiers. The emulsion was subsequently separated into the aqueous phase and the oil-rich droplet phase, which were characterized separately. Emulsions produced with 1.05% (w/w) CAS and PC fraction which varies between 1.75% (w/w) and 0.35% (w/w) provided droplets between 10 and 19 μm in surface weighted mean in 70% fish oil-in-water emulsions. At least two-third of the overall CAS is associated with the interface, while the rest remains with the aqueous phase. Six percent of PC formed a monolayer in the interface, while the rest of the PC remains in the droplet phase in the form of multilayers. When the separated components were resuspended, the resuspended emulsion showed similar characteristics compared to the original emulsion in terms of droplet size distribution and neutron scattering. Instead, CAS in the aqueous phase separated from the emulsion shows aggregation not present in the corresponding CAS-in-D2O system.

Impact of 1,8-diiodooctane on the morphology of organic photovoltaic (OPV) devices – A Small Angle Neutron Scattering (SANS) study

The impact of the additive 1,8-diiodooctane on the morphology of bulk-heterojunction solar cells based on the systems P3HT:PC71BM, PTB7:PC71BM and PTB7-Th:PC71BM is studied using a combination of Small Angle Neutron Scattering (SANS) and Atomic Force Microscopy (AFM). The results clearly show that while in the P3HT:PC71BM system, the additive DIO promotes a slight coarsening of the phase domains (type I additive), in the systems PTB7:PC71BM and PTB7-Th:PC71BM, DIO promotes a large decrease in the size of the phase domains (type II additive). SANS is demonstrated as being particularly useful at detecting the minor morphological changes observed in the P3HT:PC71BM system, which can be hardly seen in AFM. This work illustrates how SANS complements AFM and both techniques when used together provide a deeper insight into the nanoscale structure in thin organic photovoltaic (OPV) device films.

Small-angle Neutron Scattering Study of Micelle Structure and Hydration Behavior of Oleic Acid-based Gemini Surfactant

Herein, we characterized the micelle structure and hydration behavior of oleic acid-based gemini surfactants by small-angle neutron scattering. A larger counterion size (Li+ < Na+ < K+ < Cs+) resul...

Small-Angle Neutron Scattering Study of Temperature-Induced Structural Changes in Liposomes.

Liposomes of specific artificial phospholipids, such as Pad-PC-Pad and Rad-PC-Rad, are mechanically responsive. They can release encapsulated therapeutics via physical stimuli, as naturally present in blood flow of constricted vessel segments. The question is how these synthetic liposomes change their structure in the medically relevant temperature range from 22 to 42 °C. In the present study, small-angle neutron scattering (SANS) was employed to evaluate the temperature-induced structural changes of selected artificial liposomes. For Rad-PC-Rad, Pad-Pad-PC, Sur-PC-Sur, and Sad-PC-Sad liposomes, the SANS data have remained constant because the phase transition temperatures are above 42 °C. For Pad-PC-Pad and Pes-PC-Pes liposomes, whose phase transitions are below 42 °C, the q-plots have revealed temperature-dependent structural changes. The average diameter of Pad-PC-Pad liposomes remained almost constant, whereas the eccentricity decreased by an order of magnitude. Related measurements using transmission electron microscopy at cryogenic temperatures, as well as dynamic light scattering before and after the heating cycles, underpin the fact that the non-spherical liposomes flatten out. The SANS data further indicated that, as a consequence of the thermal loop, the mean bilayer thickness increased by 20%, associated with the loss of lipid membrane interdigitation. Therefore, Pad-PC-Pad liposomes are unsuitable for local drug delivery in the atherosclerotic human blood vessel system. In contrast, Rad-PC-Rad liposomes are thermally stable for applications within the human body.