The molecular interactions between two single-chain lysosomotropic surfactants DMM-11 (2-Dodecanoyloxyethyl)trimethylammonium bromide) and DMPM-11 (2-Dodecanoyloxypropyl)trimethylammonium bromide) with a small heme-protein (cytochrome c (cyt-c)) in Hepes buffer (pH = 7.4) were extensively investigated by surface tension, dynamic light scattering (DLS), circular dichroism (CD) and fluorescence spectroscopy in combination with molecular dynamic simulation techniques. The results demonstrated that surfactants can destroy the hydrophobic cavity of cyt-c, make the α-helical become loose and convert it into the β-sheet structure. The interactions between surfactants and cyt-c are mainly hydrophobic. Molecular modelling approaches were also used to gather a deeper insight on the binding of lysosomotropic surfactants with cyt-c and the in silico results were found to be in good agreement with the experimental ones. This study provides a molecular basis for the applications of protein-surfactant complexes in biological, food, pharmaceutical, industrial and cosmetic systems.
Keywords: Circular dichroism; Cytochrome c; Fluorescence quenching; Lysosomotropic surfactant; Molecular dynamic simulations.
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