Studies on the hydrogen belts of membranes: III. Glycerol permeability of dihydrosphingomyelin-cholesterol membranes

Abstract

The permeability of an N-oleoyldihydrosphingomyelin bilayer against glycerol was similar to that of a bilayer of phosphatidylcholine with identical effective hydrophobic chain length. Cholesterol at 1:1 molar ratio reduced the permeability, and also reduced the energy of activation of glycerol penetration, an effect not found for diesterphosphatidylcholine with cholesterol. The higher level of the ground state of the entropy of activation for permeability can be interpreted in terms of a hydrogen belt model which postulates lipid-lipid hydrogen bonding in membranes and explains the effect found as a disturbance of the hydrogen belt structure. Dihydrosphingomyelin can be considered to function as an "extender" in the hydrogen belt network.