Surface Structure of Lipid Membrane Modulates Apolipoprotein A-I Binding and Its Conformational Change

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  • Tanaka Masafumi
    Department of Biophysical Chemistry, Kobe Pharmaceutical University

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  • 脂質膜構造により制御されるアポリポ蛋白質A-Iの結合性と構造変化
  • シシツマク コウゾウ ニ ヨリ セイギョサレル アポリポ タンパクシツ A I ノ ケツゴウセイ ト コウゾウ ヘンカ

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Abstract

Interaction of apolipoproteins with lipid surfaces plays crucial roles in lipoprotein metabolism and cholesterolhomeostasis. It has been accepted that apolipoprotein (apo)A-I, the major protein constituent of high-density lipopro-tein (HDL), is inversely related to risk of cardiovascular disease in humans. ApoA-I binding to lipid surfaces dependson membrane structure. In this study, to elucidate the detailed mechanism by which apoA-I associates with plasmamembrane and lipoprotein particles, the effects of lipid composition and surface curvature on the lipid-apoA-I interac-tions were examined.In the initial step of the HDL formation, apoA-I produces discoidal particles. The membrane structure in discoidalparticles is thought to be distinct from that in lipid vesicles although both contain lipid bilayer structure.The possi-bilities of lipid nanodisks for application to drug delivery systems will be discussed.

Journal

  • MEMBRANE

    MEMBRANE 33 (4), 147-152, 2008

    THE MEMBRANE SOCIETY OF JAPAN

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