Physicochemical and molecular docking studies of tween 20 in the presence of NaX salts and hydrotropes in aqueous media

Abstract

An investigation has been conducted on the interaction between the plasma protein bovine serum albumin (BSA) and the surfactant T20 using various hydrotropes of sodium salt (NaX, where X is Sal and Benz). The acquired results provide a practical and efficient means to comprehend the binding process of the micellar system T20 to BSA. The predominant forces involved are hydrophobic forces and hydrogen bonding. The further study intends to investigate the impact of NaX (here, X represents Cl, Br, NO3, Sal, and Benz), on the T20 solution using various techniques including density (ρ), viscosity (η), sound velocity (U), dynamic light scattering (Dh), FT-IR spectroscopy, and molecular docking at varying temperatures. The values of ρ, η, and U increase as the concentration of Na salt increases. Conversely, when the temperature increases, the values of ρ and η fall, while the value of U increases. NaSal exhibits higher viscosity compared to other substances. The phase separation model was employed to calculate the standard Gibbs free energy ( Δ G CP 0 ), enthalpy ( Δ H CP 0 ), and entropy ( Δ S CP 0 ). The NaBenz exhibits the highest values of sound velocity while examining at different temperatures. The structural identification was performed using FT-IR data, which revealed good agreement with the available literature.