Abstract

The interactions of proteins with fluorinated/hydrogenated surfactants were investigated by circular dichroism and turbidity measurement. Pairs of fluorinated and hydrogenated surfactants with similar critical micelle concentrations (cmc), including sodium perfluorooctanoate/sodium decylsulfate and lithium perfluorononanoate/sodium dodecylsulfate were compared in view of their interactions with proteins including BSA, lysozyme, β-lactoglobulin and ubiquitin. It was found that fluorinated surfactants exhibited stronger interactions with proteins than hydrogenated ones, which, however, depended on the structures of both proteins and surfactant molecules. If the proteins are very stable, or the surfactant–protein interactions are very strong, such differences between the two kinds of surfactants might be indistinguishable.

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