The interactions between bovine serum albumin (BSA) and two cleavable anionic surfactants, sodium 3-[(2-nonyl-1,3-dioxolan-4-yl)methoxy]propane-1-sulfonate (SNPS) and sodium 3,3′-(2-nonyl-1,3-dioxane-5,5-diyl)bis(methylene)bis(oxy)dipropane-1-sulfonate (SNDPS), have been studied by means of fluorescence spectroscopy and thermodynamic analysis. The fluorescence of BSA is quenched via a static quenching mechanism with the addition of the surfactants. The binding constants of the surfactants and proteins have been measured, with (SNPS) = M？1 and (SNDPS) = 7.08？×？104？M？1, respectively. The interaction between surfactants and BSA is mainly of hydrophobic nature, based on the number of binding sites, n[n(SNPS) = 1.57, n(SNDPS) = 1.47], and the thermodynamic relationship. These results suggest that SNPS and SNDPS could be effective protein denaturants for protein separation and analysis. 1. Introduction Protein is an integral part of life in organisms and can bind a wide variety of ligands such as surfactants, drugs, toxicants, and heavy metal ions [1–6]. Studies on the interactions between surfactants and proteins would be beneficial for understanding the occurence of surfactants acting as solubilizing or denaturing agents for proteins [7, 8]. For example, serum albumins are the most abundant proteins in blood plasma and are the major soluble protein in the circulatory system [9]. They play an important role in the transport of endogenous and exogenous ligands in blood. Studying the interaction between surfactants and serum albumins would have a significant impact on the development of protein separation and analysis methods as well as our understanding of the metabolism of endogenous and exogenous ligands [10]. Traditionally, the single-chain surfactants, like cetyltrimethyl ammonium bromide (CTAB) and sodium dodecyl sulfate (SDS), have been widely used in proteomic research, such as protein separation and analysis [11–14]. However, the applications are sometimes complicated due to the formation of foams and emulsions. This also encourages the interest in researching the synthesis of simple and practical surfactants and developing desirable methods in proteomic research. Recently, protein-gemini surfactants interactions have been developed because these surfactants have a low critical micelle concentration (CMC), a low Krafft temperature, a strong hydrophobic microdomain, and a superior viscous behavior in comparison to the conventional single-chain surfactants [15–18]. However, the complex synthesis and purification procedures associated with these
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