Abstract
The objective of this study was to examine the interactions between anionic surfactants, specifically 1-alkylsulfonates (KXS) and 1-alkylsulfates (SXS) ions, with human serum albumin (HSA). A combination of experimental techniques, including isothermal titration calorimetry (ITC), steady-state fluorescence spectroscopy (SF), and molecular dynamics-based approaches was employed to gain a comprehensive understanding of these processes. It has been demonstrated that the subtle variations in the charge distribution on the anionic surfactant headgroups have a significant impact on the number of binding sites, the stoichiometry of the resulting complexes, and the strength of the interactions between the surfactants and the protein. Additionally, we established that the affinity of the investigated ligands to specific regions on the protein surface is governed by both the charge of the surfactant headgroup and the length of the aliphatic hydrocarbon chain. In summary, the findings highlight the crucial role of charge distribution on surfactant functional groups in the binding mode and the thermodynamic stability of surfactant-protein complexes.