脂質膜環境におけるアポリポタンパク質の凝集・ アミロイド線維化機構

DOI Web Site Web Site オープンアクセス

書誌事項

タイトル別名
  • Mechanisms of Aggregation and Amyloid Fibril Formation of Apolipoproteins on Lipid Membranes
  • シシツマク カンキョウ ニ オケル アポリポタンパクシツ ノ ギョウシュウ ・ アミロイド センイカ キコウ

この論文をさがす

抄録

Lipid membranes are known to influence the folding, aggregation, and fibril formation of a variety of amyloidogenic proteins. In some natively unstructured amylodogenic proteins such as α– synuclein and islet amyloid peptide, the formation of partially α– helical conformations upon membrane binding promotes the aggregation of proteins through exposure of highly amyloidogenic regions. We recently demonstrated that a G26R mutation, the first amyloidogenic mutation found in apolipoprotein A–I (apoA–I), facilitates aggregation and fibril formation of the N–terminal 1–83 fragment of apoA–I on lipid membranes through a partial destabilization of α– helical conformation. Here, we have reviewed the molecular mechanism of membrane-mediated aggregation and fibril formation of the amyloidogenic N–terminal fragment of apoA–I. We also briefly introduce the membrane–mediated aggregation behavior of α– synuclein that has similar lipid-binding property to apoA–I.

収録刊行物

  • 膜

    膜 46 (1), 25-31, 2021

    日本膜学会

関連プロジェクト

もっと見る

キーワード

詳細情報 詳細情報について

問題の指摘

ページトップへ