Mechanism of Time-Dependent Adsorption for Phosphatidylcholine onto a Clean Air-Water Interface from a Dispersion of Vesicles: Effect of Temperature and Acyl Chain Length.

Dynamic surface tension measurements were used to track adsorption kinetics for dilauroylphosphatidylcholine (DLPC) or dimyristoylphosphatidylcholine (DMPC) from monodisperse vesicle dispersions to an air-water interface at elevated temperatures ≥30 °C. Effects of vesicle concentration, aqueous solubility of the lipids, and temperature T on the adsorption kinetics were determined, and the controlling transport pathway was identified. Adsorption dynamics were tracked for 0.1-10 mM DLPC at 30 and 38 °C and for 1-10 mM DMPC at 30, 50, and 58 °C. Experimental results were compared to theoretical predictions for a reaction-enhanced, molecular transport mechanism, which was previously shown to effectively predict DLPC adsorption kinetics at 22 °C. At higher temperatures, for DLPC concentrations ≥0.25 mM or DMPC concentrations ≥1 mM, a weak dependence of adsorption time on concentration was observed, again consistent with the reaction-enhanced molecular pathway. Molecular release rates from vesicles increased with increasing temperature or decreasing acyl chain length. At equivalent ratios T/Tm of the dispersion temperature to the lipid chain phase transition temperature Tm, measured adsorption times for DLPC were approximately 10-fold shorter than those for DMPC, suggesting that the fluidity of the acyl tails is not the only lipid property determining adsorption rates. Despite the significant difference in aqueous solubility and chain phase transition temperature between DLPC and DMPC, the results provide further evidence for an adsorption mechanism that is well described by diffusion of molecular lipid, with rates of molecular diffusion near the interface enhanced by release from nearby vesicles.

Mechanism of Time-Dependent Adsorption for Dilauroyl Phosphatidylcholine onto a Clean Air-Water Interface from a Dispersion of Vesicles.

This study focused on mechanisms of adsorption for dilauroyl phosphatidylcholine (DLPC) from a dispersion of large, unilamellar vesicles (LUVs) onto a clean air-water interface. The adsorption kinetics were tracked using dynamic surface tension measurements for 0.01-10 mM concentrations of DLPC, contained within monodisperse LUVs with mean diameters between 100 and 300 nm. Any lipid in excess of the solubility limit, determined to be 1.1(±0.7) × 10-5 mM (1.1 × 10-8 M), was assumed to be in vesicle form. The adsorption rate was found to increase with increasing lipid concentration and decreasing vesicle diameter, indicating a clear mechanistic role for the vesicles. An induction regime was observed, during which lipid adsorption occurred without significantly changing the surface tension. Pressure-area isotherm data suggested that the surface concentration at the end of this induction period was ∼50% of the concentration at saturation, with the latter estimated as 4.2(±0.7) × 10-6 mol/m2. Convection was also introduced into these experiments to probe the importance of bulk transport mechanisms to the overall kinetics. Theoretical expressions for possible contributing mechanisms and pathways, via molecular and/or vesicle transport, were developed and used to predict associated transport time scales for different scenarios. These theoretical time scales were compared to experimentally measured characteristic times for a variety of DLPC concentrations, vesicle diameters, and convection rates. For DLPC concentrations ≥0.25 mM, our results were consistent with the monolayer formation arising from a molecular transport mechanism that is enhanced by vesicle-to-monomer exchange beneath the interface. At lower concentrations, experimental rates of adsorption increased with increasing convection, and a strong effect of lipid concentration was also observed. For DLPC ≤0.25 mM, transport controlled by direct interfacial vesicle adsorption reasonably captured the observed effect of lipid concentration; however, neither monomer nor vesicle pathway mechanisms captured the influence of convection. Understanding the adsorption kinetics for such nearly insoluble surfactant systems is important in several areas, including food emulsification, foam or microbubble formulation, spray drying techniques, and therapeutics.

Assessing the thermodynamic signatures of hydrophobic hydration for several common water models.

Following the conclusions of an information theory analysis that hydrophobic hydration is dictated by the equation of state of liquid water, we perform simulations of ten different water models to examine the correlation between the fidelity of each model to the experimental density of liquid water and the accuracy of its description of methane hydration. We find that the three- and five-point water models provide an inferior description of both the liquid density and methane solubility compared to the four-point water models. Of the four-point water models, TIP4P/2005 provides the best description of both the aqueous equation-of-state and methane hydration thermodynamics. When the optimized potentials for liquid simulation united-atom description for methane is used, we find that while the entropy and heat capacity of methane hydration are in excellent agreement with experiment, the chemical potential and enthalpy are systematically shifted upwards. We subsequently reoptimize the methane interaction to accurately reproduce the experimental solubilities as a function of temperature by accounting for missing attractive interactions.

Temperature-induced protein release from water-in-oil-in-water double emulsions.

A model water-in-oil-in-water (W1/O/W2) double emulsion was prepared by a two-step emulsification procedure and subsequently subjected to temperature changes that caused the oil phase to freeze and thaw while the two aqueous phases remained liquid. Our previous work on individual double-emulsion globules1 demonstrated that crystallizing the oil phase (O) preserves stability, while subsequent thawing triggers coalescence of the droplets of the internal aqueous phase (W1) with the external aqueous phase (W2), termed external coalescence. Activation of this instability mechanism led to instant release of fluorescently tagged bovine serum albumin (fluorescein isothiocyanate (FITC)-BSA) from the W 1 droplets and into W2. These results motivated us to apply the proposed temperature-induced globule-breakage mechanism to bulk double emulsions. As expected, no phase separation of the emulsion occurred if stored at temperatures below 18 degrees C (freezing point of the model oil n-hexadecane), whereas oil thawing readily caused instability. Crucial variables were identified during experimentation, and found to greatly influence the behavior of bulk double emulsions following freeze-thaw cycling. Adjustment of these variables accounted for a more efficient release of the encapsulated protein.