Interaction of Bovine Serum Albumin with Cationic Imidazolium Surfactants Containing a Methoxyphenyl Fragment

Complexation ability of the imidazolium surfactants with a methoxyphenyl fragment towards a model protein, bovine serum albumin, has been investigated by means of physico-chemical methods (tensiometry, fluorescence spectroscopy, and dynamic as well as electrophoretic light scattering). The addition of bovine serum albumin has led to a decrease in the aggregation threshold of surfactants by 1.5–2 times. The imidazolium surfactants have formed stable complexes with the protein. The components binding has occurred primarily via the tyrosine amino acid fragments, involving hydrogen bonding and van der Waals interactions. Additional contribution of electrostatic forces and hydrophobic effect in the surfactant–albumin system has been revealed by means of dynamic and electrophoretic light scattering.