Proteins are among the macromolecules that are now being extensively studied for possible therapeutic purposes. For most applications, the therapeutic proteins are accompanied or encapsulated in surfactants or polymers which act as engineered vehicles for drug delivery applications. The aim of this work is to investigate how a model protein interacts with drug delivery enhancers, including either surfactants or polymers. One way to determine these interactions is to measure surface tension and develop a model to predict the interactions. To achieve this aim, the surface properties of aqueous systems of Bovine Serum Albumin (BSA), polylisine, polyethylene glycol and two different surfactants are studied. The pendant drop method is used to measure the static and dynamic surface tensions. Dynamic surface tension is used to indicate the rate of the interfacial adsorption of the protein. Furthermore, the equilibrium surface tensions can show the overall driving force of the protein to migrate to the surfaces and the interaction between the protein and the surfactant/polymer. The equilibrium surface tensions are modelled by the equality of surface and bulk chemical potentials of the components. The molar surface area and surface to solution distributions for each aqueous solution of protein, polymer, and surfactant are obtained. These parameters are utilized to predict the surface properties of protein-polymer and protein-surfactant systems. Furthermore, the dynamic surface tensions for these systems are modeled using non-equilibrium thermodynamics and the chemical affinity model. This model is used to quantify the kinetic parameters of the interfacial adsorption. Results of this study will help researchers design better micro or nanoparticles that can carry therapeutic proteins.

Bovine serum albumin protein surface properties in the presence of polymers or surfactants

256th National Meeting (2018)

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