脂質膜相互作用を基盤としたアポリポタンパク質の構造機能研究

抄録

Exchangeable apolipoproteins such as apoA–I and apoE function in lipid transport as structural components of lipoprotein particles, cofactors for enzyme, and ligands for cell–surface receptors. Both apoA–I and apoE contain amphipathic α– helical repeats that can adopt a helix bundle conformation in the N–terminal domain, with the separate C–terminal domain being primarily responsible for lipid binding. Interaction with lipid membranes induces changes in the conformation of the N–terminal domain in apoA–I and apoE, providing molecular insights into how these apolipoproteins interact with lipids on cell surfaces and lipoprotein particles. A hereditary amyloidogenic mutation in apoA–I destabilizes the N–terminal helix bundle structure and facilitates amyloid fibril formation by the N–terminal fragment of apoA–I in solution as well as on lipid membranes. Here, I briefly review my research on the structure and function of apolipoproteins based on lipid–apolipoprotein interaction.