Effects of Tween 20 on the desorption of proteins from polymer surfaces

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Abstract
The effects of Tween 20 on the desorption of proteins from polyethylene and polyurethane were studied, using single protein solutions of the human proteins fibrinogen (Fb), immunoglobulin G (IgG), serum albumin (HSA), high density lipoproteins (HDL), and plasma. The surfactant may partly or even completely desorb the proteins, depending on the type of polymer and protein. About 40% of adsorbed HSA and 80% of adsorbed HDL from the corresponding single protein solutions were desorbed by Tween 20 from polyethylene, whereas Tween 20 had a small effect on the desorption of adsorbed Fb and IgG under the same conditions. However, the desorption of Fb and IgG by Tween 20 was much higher in the case of a diluted plasma solution compared to a pure protein solution. These findings may be explained by the differences of the interaction strengths between polymers and the adsorbed proteins. The displacement of HSA from polyethylene by Tween 20 occurred in the first few minutes and did not increase in time. It was also observed that preadsorbed Tween 20 was able to prevent in a large extent the adsorption of HSA onto polyethylene. Thus, the effect of Tween 20 on the desorption of protein is due to either the displacement of protein or prevention of protein adsorption onto the surfaces.