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

• 田中 将史

  神戸薬科大学　薬品物理化学研究室

書誌事項

タイトル別名

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

抄録

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.

収録刊行物

• 膜

  膜 33 (4), 147-152, 2008

  日本膜学会

キーワード

• apolipoprotein A-I
• lipid emulsions
• interpenetration
• lipid nanodisks

詳細情報

• CRID: 1390282681400385152
• NII論文ID: 10026876281
• NII書誌ID: AN0023215X
• DOI: 10.5360/membrane.33.147
• ISSN: 18846440
• ISSN: 03851036
• NDL書誌ID: 9595191
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I9595191
• Web Site: https://www.jstage.jst.go.jp/article/membrane/33/4/33_147/_pdf
• Web Site: https://search.jamas.or.jp/link/ui/2008301530
• 本文言語コード: ja
• データソース種別:
  • JaLC
  • NDL
  • Crossref
  • CiNii Articles
• 抄録ライセンスフラグ: 使用不可