Properties of human plasma lipid transfer protein in aqueous solution and at interfaces.

Abstract

Human plasma lipid transfer protein (cholesteryl ester transfer protein) has been characterized for its solution and surface properties. The protein is monomeric in aqueous solution up to 0.62 g/L (11.7 microM) as demonstrated by sedimentation equilibrium. It binds to the surface of a lipid microemulsion having an average diameter of 26 nm made from triolein and egg yolk phosphatidylcholine, with an estimated dissociation constant 1.2 x 10(-8) M, and the maximum saturation binding level is 8 protein molecules per particle regardless of the presence of apolipoprotein A-I. Circular dichroism measurement indicated that the protein in solution is predominantly in the beta-sheet/beta-turn conformation with some alpha-helix, and this profile does not undergo drastic change by its binding to the lipid surface. The analysis of the behavior of the protein in its monomolecular layer at the air-buffer interface indicated that it is also monomeric at the interface. LTP molecules occupied the same area per amino acid as other apolipoproteins in the monolayer but had a higher collapse pressure of its monolayer (18 dyn/cm), and the protein stayed at the interface even after the overcompressing monolayer far beyond the collapsing pressure up to 40 dyn/cm.