title: The influence of size, structure and hydrophilicity of model surfactants on the adsorption of lysozyme to oil-water interface--interfacial shear measurements.
abstract: The flexibility and aggregation of proteins can cause adsorption to oil-water interfaces and thereby create challenges during formulation and processing. Protein adsorption is a complex process and the presence of surfactants further complicates the system, in which additional parameters need to be considered. The purpose of this study is to scrutinize the influence of surfactants on protein adsorption to interfaces, using lysozyme as a model protein and sorbitan monooleate 80 (S80), polysorbate 80 (T80), polyethylene-block-poly(ethylene glycol) (PE-PEG) and polyglycerol polyricinoleate (PG-PR) as model surfactants. Rheological properties, measured using a TA AR-G2 rheometer equipped with a double wall ring (DWR) geometry, were used to compare the efficacy of the surfactant in hindering lysozyme adsorption. The system consists of a ring and a Delrin® trough with a circular channel (interfacial area=1882.6 mm(2)). Oscillatory shear measurements were conducted at a constant frequency of 0.1 Hz, a temperature of 25°C, and with strain set to 1%. The adsorption of lysozyme to the oil-water interface results in the formation of a viscoelastic film. This can be prevented by addition of surfactants, in a manner depending on the concentration and the type of surfactant. The more hydrophilic surfactants are more effective in hindering lysozyme adsorption to oil-water interfaces. Additionally, the larger surfactants are more persistent in preventing film formation, whereas the smaller ones eventually give space for the lysozyme on the interface. The addition of a mixture of two different surfactants was only beneficial when the two hydrophilic surfactants were mixed, in which case a delay in the multilayer formation was detected. The method is able to detect the interfacial adsorption of lysozyme and thus the hindering of film formation by model surfactants. It can therefore aid in processing of any delivery systems for proteins in which the protein is introduced to oil-water interfaces.
authors.affiliation: Department of Pharmaceutics and Analytical Chemistry, Faculty of Pharmaceutical Sciences, University of Copenhagen, Copenhagen, Denmark. sba@farma.ku.dk
authors.forename: Stefania G
authors.initials: SG
authors.lastname: Baldursdottir
authors.forename: Lene
authors.initials: L
authors.lastname: Jorgensen
mesh_terms: D000327:Adsorption; D000818:Animals; D002645:Chickens; D055119:Elastic Modulus; D057927:Hydrophobic and Hydrophilic Interactions; D008956:Models, Chemical; D009113:Muramidase / Q000737:chemistry*; D009821:Oils / Q000737:chemistry*; D010316:Particle Size; D033081:Shear Strength; D013501:Surface-Active Agents / Q000737:chemistry*; D013997:Time Factors; D014783:Viscosity; D014867:Water / Q000737:chemistry*
chemical_list: D009821:Oils; D013501:Surface-Active Agents; D014867:Water; D009113:Muramidase