Indresh Yadav

Structure and Interaction in the pH-Dependent Phase Behavior of Nanoparticle–Protein Systems

The pH-dependent structure and interaction of anionic silica nanoparticles (diameter 18 nm) with two globular model proteins, lysozyme and bovine serum albumin (BSA), have been studied. Cationic lysozyme adsorbs strongly on the nanoparticles, and the adsorption follows exponential growth as a function of lysozyme concentration, where the saturation value increases as pH approaches the isoelectric point (IEP) of lysozyme. By contrast, irrespective of pH, anionic BSA does not show any adsorption. Despite having a different nature of interactions, both proteins render a similar phase behavior where nanoparticle-protein systems transform from being one-phase (clear) to two-phase (turbid) above a critical protein concentration (CPC). The measurements have been carried out for a fixed concentration of silica nanoparticles (1 wt %) with varying protein concentrations (0-5 wt %). The CPC is found to be much higher for BSA than for lysozyme and increases for lysozyme but decreases for BSA as pH approaches their respective IEPs. The structure and interaction in these systems have been examined using dynamic light scattering (DLS) and small-angle neutron scattering (SANS). The effective hydrodynamic size of the nanoparticles measured using DLS increases with protein concentration and is related to the aggregation of the nanoparticles above the CPC. The propensity of the nanoparticles to aggregate is suppressed for lysozyme and enhanced for BSA as pH approached their respective IEPs. This behavior is understood from SANS data through the interaction potential determined by the interplay of electrostatic repulsion with a short-range attraction for lysozyme and long-range attraction for BSA. The nanoparticle aggregation is caused by charge neutralization by the oppositely charged lysozyme and through depletion for similarly charged BSA. Lysozyme-mediated attractive interaction decreases as pH approaches the IEP because of a decrease in the charge on the protein. In the case of BSA, a decrease in the BSA-BSA repulsion enhances the depletion attraction between the nanoparticles as pH is shifted toward the IEP. The morphology of the nanoparticle aggregates is found to be mass fractal.

Enhancement in Elastic Bending Rigidity of Polymer Loaded Reverse Microemulsions

Elastic bending rigidity of the surfactant shell is a crucial parameter which determines the phase behavior and stability of microemulsion droplets. For water-in-oil reverse microemulsions stabilized by AOT (sodium 1,4-bis(2-ethylhexoxy)-1,4-dioxobutane-2-sulfonate) surfactant, the elastic bending rigidity is close to thermal energy at room temperature (kBT) and can be modified by the presence of hydrophilic polymers. Here, we explore the influence of two polymers polyethylene glycol (PEG) and polyvinylpyrrolidone (PVP), both having nearly same size (radius of gyration, Rg) but different dipole moment, on elastic bending rigidity of water-AOT-n-decane reverse microemulsions via estimating the percolation temperatures (TP) and droplet radii using dielectric relaxation spectroscopy (DRS) and small-angle neutron scattering (SANS) techniques. Notably, an increase in TP is observed on introducing PEG and PVP polymers and is attributed to the adsorption of polymer chains onto the surfactant monolayer. The stability of the droplet phase of microemulsion after the incorporation of PEG and PVP polymers is confirmed by contrast matching SANS experiments. An enhancement in elastic bending rigidity of AOT surfactant shell amounting to ∼46% is observed upon incorporation of PVP into the droplet core, whereas for PEG addition, a smaller increase of about 17% is recorded. We conjecture that the considerable increase in elastic bending rigidity of the surfactant monolayer upon introducing PVP is because of the strong ion-dipole interaction between anionic AOT and dipoles present along the PVP polymer chains. Scaling exponents extracted from the temperature dependent electrical conductivity measurements and the frequency dependent scaling of conductivity at percolation indicate the dynamic nature of percolation for both pure and polymer loaded reverse microemulsions. The decrease in activation energy of percolation upon incorporating PEG and PVP polymer molecules also reflects the increased stability of microemulsion droplets against thermal fluctuations.

Structure and Interaction of Nanoparticle–Protein Complexes

The integration of nanoparticles with proteins is of high scientific interest due to the amazing potential displayed by their complexes, combining the nanoscale properties of nanoparticles with the specific architectures and functions of the protein molecules. The nanoparticle-protein complexes, in particular, are useful in the emerging field of nanobiotechnology (nanomedicine, drug delivery, and biosensors) as the nanoparticles having sizes comparable to that of living cells can access and operate within the cell. The understanding of nanoparticle interaction with different protein molecules is a prerequisite for such applications. The interaction of the two components has been shown to result in conformational changes in proteins and to affect the surface properties and colloidal stability of the nanoparticles. In this feature article, our recent studies exploring the driving interactions in nanoparticle-protein systems and resultant structures are presented. The anionic colloidal silica nanoparticles and two globular charged proteins [lysozyme and bovine serum albumin (BSA)] have been investigated as model systems. The adsorption behavior of the two proteins on nanoparticles is found to be completely different, but they both give rise to similar phase transformation from one phase to two phase in respective nanoparticle-protein systems. The presence of protein induces the short-range and long-range attraction between the nanoparticles with lysozyme and BSA, respectively. The observed phase behavior and its dependence on various physiochemical parameters (e.g., nanoparticle size, ionic strength, and solution pH) have been explained in terms of underlying interactions.

Interactions in reentrant phase behavior of a charged nanoparticle solution by multivalent ions

The interactions following a reentrant phase transition of charged silica nanoparticles from one phase to two phases and back to one phase by varying the concentration of multivalent counterions have been examined. The observations are far beyond the framework of Debye-Hückel or even nonlinear Poisson-Boltzmann equations and demonstrate the universal behavior of multivalent counterion-driven charge inversion. We show that the interplay of multivalent counterion-induced short-range attraction and long-range electrostatic repulsion between nanoparticles results in reentrant phase behavior.

Kinetics of aggregation in charged nanoparticle solutions driven by different mechanisms

The structure and kinetics during aggregation of anionic silica nanoparticles as induced through different mechanisms have been studied by dynamic light scattering (DLS) and small-angle neutron scattering (SANS). Three different additives, namely an electrolyte (NaCl), cationic protein (lysozyme) and non-ionic surfactant (C12E10) were used to initiate nanoparticle aggregation. Electrolyte induced aggregation can be explained by DLVO interaction, whereas depletion interaction (non-DLVO interaction) is found responsible for nanoparticle aggregation in case of non-ionic surfactant. Unlike these two cases, strong electrostatic attraction between nanoparticle and oppositely charged protein results into protein-mediated nanoparticle aggregation. The electrolyte induced aggregation show quite slow aggregation rate whereas protein mediated as well as surfactant induced aggregation takes place almost instantaneously. The significant differences observed in the kinetics are explained based on range of interactions ...

Modifications in nanoparticle-protein interactions by varying the protein conformation

Small-angle neutron scattering has been used to study the interaction of silica nanoparticle with Bovine Serum Albumin (BSA) protein without and with a protein denaturing agent urea. The measurements have been carried out at pH 7 where both the components (nanoparticle and protein) are similarly charged. We show that the interactions in nanoparticle-protein system can be modified by changing the conformation of protein through the presence of urea. In the absence of urea, the strong electrostatic repulsion between the nanoparticle and protein prevents protein adsorption on nanoparticle surface. This non-adsorption, in turn gives rise to depletion attraction between nanoparticles. However, with addition of urea the depletion attraction is completely suppressed. Urea driven denaturation of protein is utilized to expose the positively charged patched of the BSA molecules which eventually leads to adsorption of BSA on nanoparticles eliminating the depletion interaction.

Position-momentum uncertainty products

We point out two interesting features of position-momentum uncertainty product: U = ΔxΔp. We show that two special (non-differentiable) eigenstates of the Schrodinger operator with the Dirac delta potential [V(x) = −V0δ(x)], V0 > 0, also satisfy Heisenberg’s uncertainty principle by yielding \frac{\hbar }{2}

Small-angle neutron scattering study of differences in phase behavior of silica nanoparticles in the presence of lysozyme and bovine serum albumin proteins.

SRC=http://ej.iop.org/images/0143-0807/35/4/045015/ejp494730ieqn1.gif/>. One of these eigenstates is a zero-energy and zero-curvature bound state.