Osmotic shrinkage in star/linear polymer mixtures.

Multiarm star polymers were used as model grafted colloidal particles with long hairs, to study their size variation due to osmotic forces arising from added linear homopolymers of smaller size. This is the origin of the depletion phenomenon that has been exploited in the past as a means to melt soft colloidal glasses by adding linear chains and analyzed using dynamic light scattering experiments and an effective interactions analysis yielding the depletion potential. Shrinkage is a generic phenomenon for hairy particles, which affects macroscopic properties and state transitions at high concentrations. In this work we present a small-angle neutron scattering study of star/linear polymer mixtures with different size ratios (varying the linear polymer molar mass) and confirm the depletion picture, i.e., osmotic star shrinkage. Moreover, we find that as the linear/star polymer size ratio increases for the same effective linear volume fraction (c/c* with c* the overlapping concentration), the star shrinkage is reduced whereas the onset of shrinkage appears to take place at higher linear polymer volume fractions. A theoretical description of the force balance on a star polymer in solution, accounting for the classic Flory contributions, i.e. elastic and excluded volume, as well as the osmotic force due to the linear chains, accurately predicts the experimental findings of reduced star size as a function of linear polymer concentration. This is done in a parameter-free fashion, in which the size of the cavity created by the star, and from which the chains are excluded, is related to the radius of the former from first principles.

Structural changes of poly(N-isopropylacrylamide)-based microgels induced by hydrostatic pressure and temperature studied by small angle neutron scattering.

We study the structural properties of microgels made of poly(N-isopropylacrylamide) and acrylic acid as a function of hydrostatic pressure and temperature using small angle neutron scattering. Hydrostatic pressure induces particle deswelling by changing the mixing of the microgel with the solvent, similar to temperature. We extend this analogy to the structural properties of the particles and show that the form factor at a certain temperature is equal to the form factor at a certain hydrostatic pressure. We fit the results with an existent model for the microgel structure and carefully analyze the fitting procedure in order to obtain physically meaningful values of the free parameters in the model.

Small-angle neutron scattering study of protein unfolding and refolding.

Small-angle neutron scattering has been used to study protein unfolding and refolding in protein bovine serum albumin (BSA) due to perturbation in its native structure as induced by three different protein denaturating agents: urea, surfactant, and pressure. The BSA protein unfolds for urea concentrations greater than 4 M and is observed to be independent of the protein concentration. The addition of surfactant unfolds the protein by the formation of micellelike aggregates of surfactants along the unfolded polypeptide chains of the protein and depends on the ratio of surfactant to protein concentration. We make use of the dilution method to show the refolding of unfolded proteins in the presence of urea and surfactant. BSA does not show any protein unfolding up to the pressure of 450 MPa. The presence of urea and surfactant (for concentrations prior to inducing their own unfolding) has been used to examine pressure-induced unfolding of the protein at lower pressures. The protein unfolds at 200 MPa pressure in the presence of urea; however, no unfolding is observed with surfactant. The protein unfolding is shown to be reversible in all the above denaturating methods.

Small-angle neutron scattering study of structure and kinetics of temperature-induced protein gelation.

The phase diagram, structural evolution, and kinetics of temperature-induced protein gelation of protein Bovine Serum Albumin (BSA) have been studied as a function of solution pH and protein concentration. The protein gelation temperature represents the onset of turbidity in the protein solution, which increases significantly with increasing pH beyond the isoelectric pH of the protein molecule. On the other hand, the gelation temperature decreases with an increase in protein concentration only in the low-protein-concentration regime and shows a small increasing trend at higher protein concentrations. The structural evolution and kinetics of protein gelation have been studied using small-angle neutron scattering. The structure of the protein molecule remains stable up to temperatures very close to the gelation temperature. On increasing the temperature above the gelation temperature, the protein solution exhibits a fractal structure, an indication of gel formation due to aggregation. The fractal dimension of the gel increases with increasing temperature, suggesting an increase in branching between the aggregates, which leads to stronger gels. The increase in both solution pH and protein concentration is found to delay the growth in the fractal structure and its saturation. The kinetics of gelation has been studied using the temperature-jump process of heating. It is found that the structure of the protein gels remains invariant after the heating time ( approximately 1 min), indicating a rapid formation of gel structure within this time. The protein gels prepared through gradual and temperature-jump heating routes do not always show the same structure. In particular, at higher temperatures (e.g., 85 degrees C ), while gradual heating shows a fractal structure, there is collapse of such fractal structure during temperature-jump heating.

Structure and phase diagram of an adhesive colloidal dispersion under high pressure: a small angle neutron scattering, diffusing wave spectroscopy, and light scattering study.

We have applied small angle neutron scattering (SANS), diffusing wave spectroscopy (DWS), and dynamic light scattering (DLS) to investigate the phase diagram of a sterically stabilized colloidal system consisting of octadecyl grafted silica particles dispersed in toluene. This system is known to exhibit gas-liquid phase separation and percolation, depending on temperature T, pressure P, and concentration phi. We have determined by DLS the pressure dependence of the coexistence temperature and the spinodal temperature to be dP/dT=77 bar/K. The gel line or percolation limit was measured by DWS under high pressure using the condition that the system became nonergodic when crossing it and we determined the coexistence line at higher volume fractions from the DWS limit of turbid samples. From SANS measurements we determined the stickiness parameter tau(B)(P,T,phi) of the Baxter model, characterizing a polydisperse adhesive hard sphere, using a global fit routine on all curves in the homogenous regime at various temperatures, pressures, and concentrations. The phase coexistence and percolation line as predicted from tau(B)(P,T,phi) correspond with the determinations by DWS and were used to construct an experimental phase diagram for a polydisperse sticky hard sphere model system. A comparison with theory shows good agreement especially concerning the predictions for the percolation threshold. From the analysis of the forward scattering we find a critical scaling law for the susceptibility corresponding to mean field behavior. This finding is also supported by the critical scaling properties of the collective diffusion.

Structural study of coacervation in protein-polyelectrolyte complexes.

Coacervation is a dense liquid-liquid phase separation and herein we report coacervation of protein bovine serum albumin (BSA) in the presence of polyelectrolyte sodium polystyrene sulfonate (NaPSS) under varying solution conditions. Small-angle neutron scattering (SANS) measurements have been performed on above protein-polyelectrolyte complexes to study the structural evolution of the process that leads to coacervation and the phase separated coacervate as a function of solution pH , protein-polyelectrolyte ratio and ionic strength. SANS study prior to phase separation on the BSA-NaPSS complex shows a fractal structure representing a necklace model of protein macromolecules randomly distributed along the polystyrene sulfonate chain. The fractal dimension of the complex decreases as pH is shifted away from the isoelectric point ( approximately 4.7) of BSA protein, which indicates the decrease in the compactness of the complex structure due to increase in the charge repulsion between the protein macromolecules bound to the polyelectrolyte. Concentration-dependence studies of the polyelectrolyte in the complex suggest coexistence of two populations of polyelectrolytes, first one fully saturated with proteins and another one free from proteins. Coacervation phase has been obtained through the turbidity measurement by varying pH of the aqueous solution containing protein and polyelectrolyte from neutral to acidic regime to get them to where the two components are oppositely charged. The spontaneous formation of coacervates is observed for pH values less than 4. SANS study on coacervates shows two length scales related to complex aggregations (mesh size and overall extent of the complex) hierarchically branched to form a larger network. The mesh size represents the distance between cross-linked points in the primary complex, which decreases with increase in ionic strength and remains the same on varying the protein-polyelectrolyte ratio. On the other hand, the overall extent of the complex shows a similar structure irrespective of varying ionic strength and protein-polyelectrolyte ratio. A large fraction ( approximately 50%) of protein-polyelectrolyte complexes is also found to be free in the supernatant after the coacervation.

Structural evolution during protein denaturation as induced by different methods.

Small-angle neutron scattering (SANS) and dynamic light scattering (DLS) have been used to study conformational changes in protein bovine serum albumin (BSA) due to perturbation in its native structure as induced by varying temperature and pressure, and in presence of protein denaturating agents urea and surfactant. BSA has prolate ellipsoidal shape at ambient temperature and we observe no effect of temperature on its structure up to a temperature of about 60 degrees C . At temperatures beyond 60 degrees C , protein denaturation leads to aggregation. The protein solution exhibits a fractal structure at temperatures above 64 degrees C , and its fractal dimension increases with temperature. This is an indication of aggregation followed by gelation that evolves with increasing temperature. It is known for some of the proteins (e.g., Staphylococcal Nuclease) that pressure of 200 MPa can unfold the protein, whereas BSA does not show any protein unfolding even up to the pressure of 450 MPa . In presence of urea, the BSA protein unfolds for urea concentrations greater than 4M and acquires a random coil configuration. We make use of the dilution method to show the reversibility of protein unfolding with urea. The addition of surfactant denaturates the protein by the formation of micellelike aggregates of surfactants along the unfolded polypeptide chains of the protein. We show such structure of the protein-surfactant complex can be stabilized at higher temperatures, which is not the case for pure protein.

A high pressure cell for small angle neutron scattering up to 500 MPa in combination with light scattering to investigate liquid samples.

We report on a high pressure cell to use with small angle neutron scattering (SANS) in a pressure range up to 500 MPa. The cell offers the new possibility to investigate liquid samples by a specially designed sample chamber, which allows changing of samples relatively easily. Since the cell construction uses sapphire as window material, also light scattering investigations can be performed simultaneously to the SANS measurements. In this article we describe the construction of a high pressure cell and we demonstrate the applicability of the construction for SANS in combination with dynamic light scattering showing data on the biological molecule lysozyme.

Particle dynamics in concentrated colloidal suspensions.

We have studied the dynamical and structural properties of dense charge stabilized colloidal suspensions by a combination of small-angle neutron scattering (SANS), 3D dynamic light scattering (3DDLS) and diffusing wave spectroscopy (DWS). SANS and 3DDLS extend static and dynamic light scattering techniques to the regime of opaque samples while DWS additionally provides information on short length scales, typically from 1-50 nm. This offers an increased range of accessible length and time scales perfectly suited for the (non-invasive) investigation of highly concentrated suspensions. Different systems have been examined ranging from hard sphere like suspensions over strongly repulsive charged spheres to colloidal gels. We furthermore present an extended theoretical frame for DWS to characterize the internal dynamics of turbid gels made from nanosized colloidal particles.

[Properties of plasma low density lipoproteins in patients with hypertriglyceridemia and ischemic heart disease]. / Svoistva plazmennykh lipoproteinov nizkoi plotnosti u patsientov s gipertriglitseridemiei i ishemicheskoi bolezn'iu serdtsa.

It has been shown that low-density plasma lipoproteins in patients with ischemic heart disease and hypertriglyceridemia are heavier in density, smaller in size, more negatively charged and more inclined to peroxide modification and aggregation than in healthy persons. The protein in the composition of such lipoproteins deviates towards the water phase, which may result in the masking of the domen, recognized by the BE-receptor and may lead to hyperlipidemia of a retaining character.

[Acceptance of cholesterol by high density lipoproteins in people with dys-alpha-lipoproteinemia and the possible role of apoprotein E in this process]. / Aktseptsiia kholesterina lipoproteinami vysokoi plotnosti u lits s dis-alpha-lipoproteinemiei i vozmozhnaia rol' v étom protesse apoproteina E.

Both subfraction "2" of high density lipoproteins (HDL2) from patients with hypo-alpha-lipoproteinemia and subfraction HDL3 from persons with normal content of cholesterol were shown to accept the erythrocyte membranes cholesterol in vitro. Under these conditions HDL3 subfraction was transformed into HDL2-like particles, where content of unesterified cholesterol and its esters was increased simultaneously with enlargement of the particles size. The HDL subfraction, isolated from persons with high content of cholesterol, did not accept cholesterol under the experimental conditions. Apoprotein E, containing in the HDL subfractions, was not responsible for the particles cholesterol-accepting properties. Apoprotein E itself was capable of cholesterol elimination from erythrocytes as well as of cholesterol esters from HDL3 and HDL2-like particles with formation of a specific complex.