Molecular interaction of lysozyme with therapeutic drug azithromycin: Effect of sodium dodecyl sulfate on binding profile

This paper describes an inclusive biophysical study elucidating the interaction of therapeutic drug azithromycin (Azith) with hen egg white lysozyme (HEWL). Spectroscopic and computational tools have been employed to study the interaction of Azith with HEWL at pH 7.4. The fluorescence quenching constant values (Ksv) exhibited a decrease with the increase in temperature which revealed the occurrence of static quenching mechanism between Azith and HEWL. The thermodynamic data demonstrated that hydrophobic interactions were predominantly involved in the Azith-HEWL interaction. The negative value of standard Gibbs free energy (ΔG°) stated that the Azith-HEWL complex formed via spontaneous molecular interactions. The effect of sodium dodecyl sulfate (SDS) surfactant monomers on the binding propensity of Azith with HEWL was insignificant at lower concentrations however the binding significantly decreased at increased concentrations of the former. Far-UV CD data revealed alteration in the secondary structure of HEWL in the presence of Azith and the overall HEWL conformation changed. Molecular docking results revealed that the binding of Azith with HEWL takes place through hydrophobic interactions and hydrogen bonds.