RESUMO
Understanding nonionic surfactant-protein interactions is fundamental from both technological and scientific points of view. However, there is a complete absence of kinetic data for such interactions. We employed surface plasmon resonance (SPR) to determine the kinetic and thermodynamic parameters of bovine lactoferrin-Brij58 interactions at various temperatures under physiological conditions (pH 7.4). The adsorption process was accelerated with increasing temperature, while the desorption rate decreased, resulting in a more thermodynamically stable complex. The kinetic energetic parameters obtained for the formation of the activated complex, [bLF-Brij58], indicated that the potential energy barrier for [bLF-Brij58] formation arises primarily from the reduction in system entropy. [bLF-Brij58]â formation was entropically driven, indicating that hydrophobic interactions play a fundamental role in bLF interactions with Brij58.
