The Binding of CTAB, a Cationic Surfactant, to the Rat Erythrocyte Membrane

Abstract

Absrract: The adsorption of CTAB (cetyltrimethylammonium bromide) to the rat erythrocyte membrane was studied by determining the electrophoretic mobility of erythrocytes treated with CTAB and by SDS polyacrylamide electrophoresis of membrane proteins from erythrocytes treated with IT-CTAB. At low concentrations of CTAB there was only a small reduction in the electrophoretic mobility of the erythrocytes. At lytic concentrations the electrophoretic mobility of the erythrocytes was markedly reduced. Alterations at the cell surface were found to be a more likely reason for the reduction in the electrophoretic mobility than interactions between the surfactant and charged groups at the cell surface. Very small amounts of radioactivity were found to be associated with the protein and sialoglycoprotein bands of the polyacrylamide gels. It is suggested that the adsorption of CTAB to the rat erythrocyte membrane does not involve electrostatic interactions between the surfactant and negatively charged groups of the sialoglycoproteins and that membrane proteins do not play a major role in the lytic events.

Interactions of Surface‐active Alkyltrimethylammonium Salts with the Plasma Membrane of Acanthamoeba castellanii

“…Because of their importance as antiseptic agents, the actions of surface-active alkyltrimethylammonium salts on cells have been subjected to many studies. Several authors have suggested that the principal point of attack of cationic surfactants is the lipid bilayer of the plasma membrane (Hooghwinkel et al 1965;Kondo & Tomizawa 1966;Reman et al 1969;Isomaa et al 1979). The surfactant molecules are assumed to penetrate into the lipid bilayer which they tend t o break up into localized micellar arrangements (Haydon & Taylor 1963;Seufert 1965).…”