Physicochemical nature of sodium dodecyl sulfate interactions with bovine serum albumin revealed by interdisciplinary approaches
Introduction
Surfactants are the subject of interest to many research groups since it has been found that they can be utilized in several industrial and technical applications, including detergent industry, food chemistry, drug delivery, and cosmetic preparation as well as developments in life sciences [1], [2], [3], [4]. Much attention has been focused on studies of surfactant interactions with biologically relevant macromolecules such as proteins [5], [6], [7], [8], [9], [10], [11].
An excellent review on the protein - surfactant interactions provided by Otzen reveals the most important techniques for analysing these interactions and highlights the different issues related to this field, namely the impact of surfactant on protein denaturation, binding affinity and unfolding processes [12]. The macromolecule - surfactant interactions depend on many factors, including the topology of the investigated surfactant species (monomeric and micelle forms), a chemical structure of a surfactant (anionic, cationic, amphoteric or non-ionic) as well as experimental conditions (pH, temperature). A remarkable degree of specificity and high affinity of surfactants towards proteins results in changes in their physicochemical properties. Consequently the conformational changes and the saturation of the binding sites of a macromolecule affect its biological activity upon a complex formation.
The understanding of the thermodynamic and thermal stability of the binding process and the structural changes of a protein in the presence of ubiquitous surfactants may be helpful for an in-depth interpretation of a surfactant role underlying biologically relevant protein’s functions. Moreover, it is fundamental from the viewpoint of the surfactants application in environmental processes and the pharmaceutical industry [13]. In this paper, we report the influence of pH and temperature on the interactions of the sodium dodecyl sulfate (SDS), a common, anionic surfactant, with the protein bovine serum albumin (BSA). As far as we are concerned, there are few reports on the SDS – BSA interactions [14], [15], [16], [17], [18], [19]. However, in contrast to these previous studies, we have focused our attention on a low SDS to BSA molar ratio range. Furthermore, the experimental and in silico data related to the structural impact of pH and temperature on the potential binding sites and poses of BSA have been discussed.
Section snippets
Materials
Bovine serum albumin (BSA, lyophilized powder, ≥96%, Sigma-Aldrich, Poland), sodium dodecyl sulfate (SDS, BioUltra, for molecular biology, ≥99%, Sigma-Aldrich, Poland), sodium cacodylate trihydrate (Caco, ≥99%, Sigma-Aldrich, Poland) were used as obtained without further purification. Double-distilled water with conductivity not exceeding 0.18 μS cm−1 was used for preparations of aqueous solutions.
Conductometric analysis
A microtitration unit (Cerko Lab System, Poland) fitted with a 5 mL syringe (Hamilton, Poland) and
Critical micelle concentration (CMC) of SDS in cacodylate buffer
Surfactant molecules reveal tendency to self-association and formation of ordered structures (micelles). Thus, the investigations of systems in which surfactants are involved require determination of the critical micelle concentration (CMC) [31], [32]. The presence of monomeric surfactants (below the CMC) and micelles modifies solution properties as well as has a considerable impact on their interaction’s mode with various proteins [33], [34], [35]. The CMC value depends on many factors, among
Conclusions
In this study, we showed that a low concentration of SDS (0.009 mg/1 mg SDS/BSA) significantly affects the BSA structure, which may have an impact on its biological functions. It should be stressed that the binding constant and the stoichiometry of the resulting BSA complexes are so-called condition-dependent parameters as their values often depend on experimental conditions (pH and temperature). Furthermore, the determination of the binding properties of BSA is not always straightforward,
CRediT authorship contribution statement
Aleksandra Tesmar: Conceptualization, Data curation. Małgorzata M. Kogut: Methodology, Investigation. Krzysztof Żamojć: Methodology, Investigation. Ola Grabowska: Investigation, Resources. Katarzyna Chmur: Investigation, Resources. Sergey A. Samsonov: Methodology, Supervision. Joanna Makowska: Methodology, Investigation. Dariusz Wyrzykowski: Conceptualization, Project administration, Writing - review & editing. Lech Chmurzyński: Supervision, Writing - review & editing.
Declaration of Competing Interest
The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
Acknowledgements
This work was supported by the Polish National Science Centre under Grant No. 2016/23/D/ST4/01576. Theoretical research was funded by National Science Centre of Poland, grant number UMO-2018/30/E/ST4/00037. Computational resources were provided by the Polish Grid Infrastructure (PL-GRID, grants plgionsgpu, plggagstr2), ZIH at TU Dresden (grant p_gag) and the local cluster PIASEK at the Faculty of Chemistry, University of Gdansk.
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Authors contributed equally.