Tween-80 on Water/Oil Interface: Structure and Interfacial Tension by Molecular Dynamics Simulations.

Surfactants are used in many fields of the chemical industry in a wide range of applications. Generally, surfactants on water/oil interfaces reduce interfacial tension, enabling the formation of emulsions or providing greater stability to the emulsion formed. Although molecular dynamics has been extensively used and has achieved remarkable success in describing thermodynamic and molecular properties of systems with surface-active compounds, the traditional molecular simulation force fields considerably constrain the system size and the time scale of simulations. Here, we propose a coarse-grained model of polysorbate 80, a nonionic surfactant commercially known as Tween-80. Based on the proposed coarse-grained model, we evaluate the influence of the more internal ethylene oxide chain on the properties of the water/Tween-80/decane system. We verify with the simulation results that the model can reproduce the expected decrease in interfacial tension as the surfactant quantity increases in the simulations. Furthermore, we observe changes in the surfactant orientation as their quantity in the interface increases, indicating a preferential orientation for these molecules in the adsorption layer. We also assessed the partition coefficient of the surfactant between the two bulk phases by performing free energy calculations, which showed a higher affinity of Tween-80 surfactants with the water phase.

Pollution caused by nanoplastics: adverse effects and mechanisms of interaction via molecular simulation.

The continuous increase in the production of synthetic plastics for decades and the inadequate disposal of plastic waste have resulted in a considerable increase of these materials in aquatic environments, which has developed into a major environmental concern. In addition to conventional parameters, the relevance of the environmental monitoring of microplastics (MPs) and nanoplastics (NPs) has been highlighted by the scientific community due to the potential adverse effects these materials pose to the ecosystem as well as to human health. The literature has registered an increasing interest in understanding the mechanisms, at the molecular level, of the interaction between NPs and other compounds using molecular simulation techniques. The present review aims to: (i) summarize the force fields conventionally used to describe NPs by molecular simulations; (ii) discuss the effects of NPs in the structural and dynamical properties of biological membranes; (iii) evaluate how NPs affect the folding of proteins; (iv) discuss the mechanisms by which NPs adsorb contaminants from the environment. NPs can affect the secondary structure of proteins and change the lateral organization and diffusion of lipid membranes. As a result, they may alter the lipid digestion in the gastrointestinal system representing a risk to the assimilation of the nutrients by humans. The adsorption of contaminants on MPs and NPs can potentiate their harmful effects on human health, due to a possible synergism. Therefore, understanding the mechanisms involved in these interactions is crucial to predict dangerous combinations and outline action strategies that reduce negative impacts on ecosystems and human health. Depending on the chemical properties of contaminants and NPs, electrostatic and/or van der Waals interactions can be more relevant in explaining the adsorption process. Finally, we conclude by highlighting gaps in the literature and the critical aspects for future investigations.

A modified Poisson-Boltzmann equation applied to protein adsorption.

Ion-exchange chromatography has been widely used as a standard process in purification and analysis of protein, based on the electrostatic interaction between the protein and the stationary phase. Through the years, several approaches are used to improve the thermodynamic description of colloidal particle-surface interaction systems, however there are still a lot of gaps specifically when describing the behavior of protein adsorption. Here, we present an improved methodology for predicting the adsorption equilibrium constant by solving the modified Poisson-Boltzmann (PB) equation in bispherical coordinates. By including dispersion interactions between ions and protein, and between ions and surface, the modified PB equation used can describe the Hofmeister effects. We solve the modified Poisson-Boltzmann equation to calculate the protein-surface potential of mean force, treated as spherical colloid-plate system, as a function of process variables. From the potential of mean force, the Henry constants of adsorption, for different proteins and surfaces, are calculated as a function of pH, salt concentration, salt type, and temperature. The obtained Henry constants are compared with experimental data for several isotherms showing excellent agreement. We have also performed a sensitivity analysis to verify the behavior of different kind of salts and the Hofmeister effects.