Delfi Bastos-González

Interaction of Monovalent Ions with Hydrophobic and Hydrophilic Colloids: Charge Inversion and Ionic Specificity

Here we study experimentally and by simulations the interaction of monovalent organic and inorganic anions with hydrophobic and hydrophilic colloids. In the case of hydrophobic colloids, our experiments show that charge inversion is induced by chaotropic inorganic monovalent ions but it is not induced by kosmotropic inorganic anions. For organic anions, giant charge inversion is observed at very low electrolyte concentrations. In addition, charge inversion disappears for both organic and inorganic ions when turning to hydrophilic colloids. These results provide an experimental evidence for the hydrophobic effect as the driving force for both ion specific effects and charge inversion. In the case of organic anions, our molecular dynamics (MD) simulations with full atomic detail show explicitly how the large adsorption free energies found for hydrophobic colloids are transformed into large repulsive barriers for hydrophilic colloids. Simulations confirm that solvation free energy (and hence the hydrophobic effect) is responsible for the build up of a Stern layer of adsorbed ions and charge inversion in hydrophobic colloids and it is also the mechanism preventing charge inversion in hydrophilic colloids. Overall, our experimental and simulation results suggest that the interaction of monovalent ions with interfaces is dominated by solvation thermodynamics, that is, the chaotropic/kosmotropic character of ions and the hydrophobic/hydrophilic character of surfaces.

A comparative study between the adsorption of IgY and IgG on latex particles.

The use of egg yolk antibodies (IgY) instead of IgG from mammalian species may present several advantages in the development of routine diagnostic immunoassays. On the one hand, the animal suffering is reduced, as antibodies are obtained directly from the egg. On the other hand, the use of IgY avoids the rheumatoid factor interference. The rheumatoid factor interacts with IgG molecules in many immunoassays causing false positive results. Despite these advantages, IgY antibodies are scarcely used. As part of an aim to develop a diagnostic test based on IgY-latex agglutination, a preliminary study on some characteristics of the IgY-latex complexes is carried out. In this work, protein adsorption and desorption, isoelectric point, electrokinetic mobility, and colloidal stability are analysed. Results are compared to those obtained by IgG. Interesting differences are observed (which mainly arise from the difference in molecular structure between IgY and IgG), suggesting that IgY is a more hydrophobic molecule than IgG. In addition, colloidal dispersions of IgY-covered latex particles are more stable (at pH 8) than those sensitized by IgG.

A review of factors affecting the performances of latex agglutination tests

The present review describes the different strategies followed to improve the performance of latex agglutination tests. The analysis is mainly focused on the diverse parameters that affect the final colloidal stability of the immunoprotein-latex system. These parameters include: the surface properties of polymer carriers; the different kind of antibodies usually employed; the use of BSA as stabilizer; the co-adsorption of various macromolecules (BSA, surfactants and lipids) and antibodies; recent approaches to colloidal stability at high ionic strengths due to hydration forces; and the covalent coupling of antibodies on functionalized latex particles. Special emphasis is given to the relation between electrophoretic mobility and the colloidal stability of the sensitized particles and how this knowledge can be utilized for a better understanding of the immunoagglutination kinetic.

Thermally sensitive reversible microgels formed by poly(N-Isopropylacrylamide) charged chains: A Hofmeister effect study

In this study, we present a new method to obtain anionic and cationic stable colloidal nanogels from PNIPAM charged chains. The stability of the particles formed by inter-chain aggregation stems from the charged chemical groups attached at the sides of PNIPAM polymer chains. The particle formation is fully reversible-that is, it is possible to change from stable polymer solutions to stable colloidal dispersions and vice versa simply by varying temperature. In addition, we also demonstrate that the polymer LCST (lower critical solution temperature), the final particle size and the electrokinetic behavior of the particles formed are highly dependent on the electrolyte nature and salt concentration. These latter results are related to Hofmeister effects. The analysis of these results provides more insights about the origin of this ionic specificity, confirming that the interaction of ions with interfaces is dominated by the chaotropic/kosmotropic character of the ions and the hydrophobic/hydrophilic character of the surface in solution.

Ion-induced reversibility in the aggregation of hydrophobic colloids

Experimental evidence of a fully reversible aggregation process due to ionic specificity is presented for the first time. The results indicate the existence of repulsive structural forces between particles coming from the specific accumulation of poorly hydrated ions around hydrophobic surfaces. This result emphasizes the key role that ion-water structure near interfaces plays in Hofmeister effects, as recently suggested by molecular dynamics simulations.

Adsorption of Milk Proteins (β-Casein and β-Lactoglobulin) and BSA onto Hydrophobic Surfaces

Here, we study films of proteins over planar surfaces and protein-coated microspheres obtained from the adsorption of three different proteins (β-casein, β-lactoglobulin and bovine serum albumin (BSA)). The investigation of protein films in planar surfaces is performed by combining quartz crystal microbalance (QCM) and atomic force microscopy (AFM) measurements with all-atomic molecular dynamics (MD) simulations. We found that BSA and β-lactoglobulin form compact monolayers, almost without interstices between the proteins. However, β-casein adsorbs forming multilayers. The study of the electrokinetic mobility of protein-coated latex microspheres shows substantial condensation of ions from the buffer over the complexes, as predicted from ion condensation theories. The electrokinetic behavior of the latex-protein complexes is dominated by the charge of the proteins and the phenomenon of ion condensation, whereas the charge of the latex colloids plays only a minor role.

Ions-induced nanostructuration: effect of specific ionic adsorption on hydrophobic polymer surfaces.

The effect of surface charges on the ionic distribution in close proximity to an interface has been extensively studied. On the contrary, the influence of ions (from dissolved salts) on deformable interfaces has been barely investigated. Ions can adsorb from aqueous solutions on hydrophobic surfaces, generating forces that can induce long-lasting deformation of glassy polymer films, a process called ion-induced polymer nanostructuration, IPN. We have found that this process is ion-specific; larger surface modifications are observed in the presence of water ions and hydrophobic and amphiphilic ions. Surface structuration is also observed in the presence of certain salts of lithium. We have used streaming potential and atomic force microscopy to study the effect of dissolved ions on the surface properties of polystyrene films, finding a good correlation between ionic adsorption and IPN. Our results also suggest that the presence of strongly hydrated lithium promotes the interaction of anions with polystyrene surfaces and more generally with hydrophobic polymer surfaces, triggering then the IPN process.

Effect of organic and inorganic ions on the lower critical solution transition and aggregation of PNIPAM

We have studied the effect of different ions belonging to the extended Hofmeister series on the thermosensitive polymer poly(N-isopropylacrylamide) (PNIPAM), by combining Differential Scanning Calorimetry (DSC) and Dynamic Light Scattering (DLS). The variations in the lower critical solution temperature (TLCS) and enthalpy change during PNIPAM phase separation evidence the importance of considering both hydration and hydrophobicity to explain the interaction of ions with interfaces. The results obtained in the presence of inorganic ions can be explained by the tendency of water molecules to preferentially hydrate the PNIPAM chains or the ions, depending on the kosmotropic (highly hydrated) or chaotropic (poorly hydrated) character of the ions. On the contrary, tetraphenyl organic ions (Ph4B- and Ph4As+) interact with the hydrophobic moieties of PNIPAM chains, inducing a significant reduction of the TLCS. DLS results show that the aggregation state of PNIPAM above the TLCS is also strongly influenced by the presence of ions. While macroscopic phase separation (formation of a polymer-rich phase insoluble in water) was apparent in the presence of inorganic ions, we observed the formation of submicron PNIPAM aggregates at temperatures above the TLCS in the presence of the hydrophobic ions. Kinetically arrested monodisperse PNIPAM nanoparticles were formed in the presence of the Ph4B- anion, while a rather polydisperse distribution of particle sizes was observed in the presence of Ph4As+. These results show that ionic specificity influences both the static (thermodynamic) and dynamic (kinetically controlled aggregation) states of PNIPAM in an aqueous environment.