Interactions in the hydrogen belts of membranes: cholesterol leaving phosphatidylcholine bilayers

Cholesterol transfer from sonicated liposomes of phosphatidylcholine containing 10 or 30 mole percent cholesterol was measured with erythrocytes as acceptor. The activation energies of the (rate-limiting) bilayer-cholesterol dissociation were determined. In parallel experiments, phosphatidylcholine was replaced by an analog lacking the carbonyl oxygens, diether-phosphatidylcholine. The activation energies for dissociation of cholesterol from this phospholipid were three Cal/mole smaller than those for cholesterol-phosphatidylcholine dissociation, at both concentrations of cholesterol. These results demonstrate the involvement of the carbonyl oxygen in cholesterol-phospholipid bonding and support the hypothesis of lipid-lipid hydrogen bonding in the hydrogen belts of membranes.