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ABSTRACT: Sodium cholate (NaC) was used as a representative bile salt in the process of cooperative binding to bovine serum albumin (BSA) in a mixture with sodium dodecyl sulfate (SDS). The experiments were performed in 0.02 M Tris-HCl buffer solution (pH 7.50), in the presence of 0.1% BSA and at 25 degrees C. The aim of this study is to provide information on the performance of the BSA in the promotion of cooperative binding of sodium cholate promoted by the presence of SDS. The method used to monitor the binding was based on the analysis of the effect of SDS and NaC concentrations and their mixtures upon the fluorescence intensity of the BSA tryptophan residues. Plots of the fluorescence emission bands in terms of the A0/A ratio vs surfactant concentrations, where A0 and A represent the areas of emission bands in the presence and absence of the surfactants, respectively, were drawn in order to investigate the surfactant interaction with the protein. An alternative methodology, the specific conductivity vs surfactant concentration plots, was used, which involves mixtures of SDS and NaC to investigate the association processes, through the determination of the critical aggregation concentration (cac, when in the presence of protein) and the critical micellar concentration (cmc). The results led to a general conclusion that as the mixed micellar aggregates become richer in the bile salt monomer, the tendency to lose the reactivity with the protein increases. According to our results, a clear evidence of the predomination of BSA-SDS-NaC complexes is found only for the SDS molar fraction above approximately 0.6, and below this fraction a tendency toward free mixed micelles starts to predominate.
Journal of Colloid and Interface Science 07/2006; 298(1):457-66. · 3.07 Impact Factor
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ABSTRACT: In this study sodium cholate (NaC) was used as a representative bile salt for the competitive binding between NaC and sodium dodecyl sulfate (SDS) in bovine serum albumin (BSA), in 0.02 M tris-HCl buffer solution at pH 7.50 and 25 °C. The NaC and SDS associations with BSA were monitored at low surfactant concentrations where only this specific binding process can develop. The applied method to monitor the binding was based on the analysis of the effect of SDS and NaC concentrations and their mixtures upon the fluorescence intensity of the BSA tryptophan residues. This consists of the measurement of the surfactant monomer partitioning between the dispersion medium and the microaggregates on the protein molecule where the binding is indicated by the quenching of the fluorescence chromophores. Experimentally, varying the protein concentration, the surfactant concentration needed to reach a given Io/I ratio (Io and I are the intensities with and without protein, respectively) was measured. The analyses, based on the average number of surfactant molecules bound on the protein, indicated that the SDS is a more efficient quencher than the bile salt. The need for 4–6 NaC bound molecules to give the same protein quenching efficiency by a single molecule of SDS was estimated. We concluded that the differences in the competitive binding on the protein are exclusively related to the quenching efficiency in the formation of the nonfluorescent fluorophore-quencher complex via a physical contact and static quenching process.
Macromolecular Symposia 11/2005; 229(1):208 - 216.
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ABSTRACT: Mixtures of ethyl(hydroxyethyl)cellulose (EHEC) and sodium dodecanoate (SDoD) were investigated using surface tension, conductivity and transmittance measurements. The parameters of the surfactant to polymer association processes such as the critical aggregation concentration (cac) and saturation of the polymer by SDoD (psp) were determined from the plots of surface tension and specific conductivity versus surfactant concentration. The transmittance versus [SDoD] profiles exhibited bands that, in conjunction with conductivity and surface tension data, gave support to the explanation of the behavior of EHEC–SDoD–water solutions. Transmittance bands determined in the presence of EHEC and surfactant are sensitive to the process of surfactant to polymer binding. In this process, a discontinuity point represented by a second broader peak in the transmittance plots was identified, implying a slight inhibition of the breakdown of the network process. This is explained as a kind of intermediate re-structural network of the complexes produced by the formation of regular SDoD micelles. It was demonstrated that the second conductivity breakpoint marks the polymer saturation by surfactant clusters, and the effect of the EHEC concentration on the process of binding can be described by a linear correlation when the psp breakpoint is plotted against the polymer concentration.
Colloids and Surfaces A Physicochemical and Engineering Aspects 256:171-180. · 2.24 Impact Factor
