Abstract
The interactions between cetyltrimethylammonium bromide (CTAB) and hen egg white lysozymes (HEWL) was carried out to investigate protein-swfactant interaction mechanisms while both exist in the overall same charged state. The interactions between CTAB and the HEWL were examined with circular dichroism (CD), dynamic light scattering (DLS), fluorescence spectroscopy, and computational docking at a pH 9.0 at room temperature. The far-UV CD and fluorescence results revealed that CTAB at concentrations from 0.15 to 10.0 mM influenced the secondary as well as the tertiary structure of HEWL The secondary structure of the HEWL was retained, while the tertiary structure of the HEWL was disrupted in the CTAB-treated samples at pH 9.0. The hydrodynamic radii of the HEWL were also expanded in the presence of CTAB. Molecular docking studies showed that (TAB formed one electrostatic and four hydrophobic interactions, as well as one carbon hydrogen bond with HEWL The data obtained from spectroscopic and computational studies demonstrated that the positively charged head and 18-carbon alkyl chain of the CTAB interacted through weak electrostatic and strong hydrophobic interactions. (C) 2019 Elsevier B.V. All rights reserved.