Bovine serum albumin (BSA) plays a role in the size of SDS micelle-like aggregates at the saturation binding: the ionic strength effect

Shweitzer, Bianca; Zanette, Dino; Itri, Rosângela

doi:10.1016/j.jcis.2004.04.059

Cited by 54 publications

(58 citation statements)

References 26 publications

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“…In this context, SDS exhibits both effects: at low concentrations it induces only a decrease in the protein emission band but, at higher concentrations, this effect is concomitant with a blue shift. [6,10,15] Differently to the well-known SDS effects on the fluorescent emission spectra of BSA, for the BSA concentrations studied here, we found that the effect of sodium cholate produces only the decrease in intensity with a maximum emission at 240 AE 1 nm without displacement of the band up to %2.0 mM NaC. Moreover, above this [NaC], the spectra are not sensitive to an additional amount of NaC (data not shown).…”

Section: Resultssupporting

confidence: 46%

Competitive Process of Binding Between the Anionic Surfactants Sodium Dodecyl Sulfate and Sodium Cholate in Bovine Serum Albumin

Schweitzer

Felippe

Dal-Bó

et al. 2005

Macromolecular Symposia

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Summary: 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 8C. 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 I o /I ratio (I o 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 fluorophorequencher complex via a physical contact and static quenching process.

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Section: Resultssupporting

confidence: 46%

Competitive Process of Binding Between the Anionic Surfactants Sodium Dodecyl Sulfate and Sodium Cholate in Bovine Serum Albumin

Schweitzer

Felippe

Dal-Bó

et al. 2005

Macromolecular Symposia

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“…These results demonstrated the presence of mixed micelles containing SDS and BSA, in agreement with previously published results. [48][49][50] Similar AUC-SV experiments were conducted using darbepoetin alfa (5. showed that the presence of darbepoetin alfa did not affect the sedimentation profiles of the polysorbates. The PS-20 and PS-80 micelle s-values were 1.7 and 2.1s, respectively.…”

Section: Monitoring Darbepoetin Alfa-polysorbate Interactions By Sedimentioning

confidence: 99%

Physical and biophysical effects of polysorbate 20 and 80 on darbepoetin alfa

Deechongkit

Wen

Narhi

et al. 2009

Journal of Pharmaceutical Sciences

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“…Thus the CAC value is lower than the CMC of the surfactant in the absence of protein, a behaviour that has been described in the literature for ionic surfactants and globular proteins [23,28,48,49]. Formation of the surfactant-protein complex hinders the micellization process and thus the surfactant self-assembles to form free micelles in solution at higher concentrations than the CMC of pure surfactant solution.…”

Section: Surface Tension Datamentioning

confidence: 77%

“…Formation of the surfactant-protein complex hinders the micellization process and thus the surfactant self-assembles to form free micelles in solution at higher concentrations than the CMC of pure surfactant solution. As a consequence, interfacial saturation of the interaction profile, corresponding to CMC, occurs at a higher surfactant concentration compared to the dilution profile, an indication of effective interaction between (C 12 Cys) 2 and BSA [23,28,48,49].…”

Section: Surface Tension Datamentioning

confidence: 99%