Interaction of Myoglobin with Cationic Gemini Surfactants in Phosphate Buffer at pH 7.4

Abstract

AbstractThe interactions between myoglobin, a monomeric water soluble heme protein, and cationic gemini surfactants 14‐3‐14, 14‐4‐14, 14‐5‐14 have been studied in phosphate buffer at pH 7.4 using different techniques such as surface tension, UV–visible spectroscopy, fluorescence spectroscopy and circular dichroism. Myoglobin is a surface active protein and it is bound with surfactant molecules. The spin states of the heme group of myoglobin change depending on the concentration of surfactant. The unfolding process of protein in the presence of surfactant is observed from fluorescence spectra. With increasing surfactant concentration, α‐helicity of myoglobin decreases with the appearance of β‐sheet and random coil. The extent of interaction of myoglobin with gemini surfactant increases with increasing spacer length.