Ultrastructure of serum high density lipoproteins: facts and models.

The complexity of the structure of plasma high density lipoproteins (HDL) has invited numerous approaches which have been directed at the study of the intact particles, their apolipoproteins and reassembled complexes. Parameters such as flotation and sedimentation coefficients, size and molecular weight have been determined and in addition, through scattering techniques, an understanding has been obtained on the long range organization between core (cholesteryl esters and triglycerides) and surface components (unesterified cholesterol, phospholipids and apoproteins). In the case of the apolipoproteins, the knowledge of their primary structure has facilitated the study of their physicochemical properties in solution and at the air-water interface and has also permitted realistic predictions of the two dimensional organization, not only of their alpha-helical segments but also of the beta-pleated sheets, random coil and beta-turns, all of which have amphipathic properties. When all of the information from the physical and chemical studies is put together, the various HDL can be described as spherical structures having a liquid core of radius, r - 20.2 A, surrounded by a monolayer of cholesterol and phospholipids with closely packed hydrophobic ends on the surface of the core. The organization of the apoproteins at the lipoprotein interface is comparatively less understood. However, reasonable predictions can be made on secondary structure considerations and on their behavior at the air-water interface. The emerging overall structural information can be translated into a space-filling model that not only provides a useful representation of HDL, but, more importantly, a basis for planning future studies on the elucidation of the structure of these particles on a molecular level.