β-アミロイド凝集に及ぼすトレハロースの効果(平成17年度 第51回低温低物工学会研究報告)

  • 渡邉 亜沙子
    東京工業大学バイオ研究基盤支援総合センター
  • 岡畑 恵雄
    東京工業大学フロンティア創造共同研究センター:東京工業大学大学院生命理工学研究科
  • 古澤 宏幸
    東京工業大学大学院生命理工学研究科
  • 星 美奈子
    東京工業大学大学院生命理工学研究科:三菱化学生命科学研究所アルツハイマー病研究グループ
  • 櫻井 実
    東京工業大学バイオ研究基盤支援総合センター

書誌事項

タイトル別名
  • The Effect of Trehalose on the Aggregation of β-amyloid(Papers presented at the 51^<st> Annual Meeting)
  • β-アミロイド凝集に及ぼすトレハロースの効果
  • ベータ アミロイド ギョウシュウ ニ オヨボス トレハロース ノ コウカ

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抄録

The effect of trehalose on the aggregation of β-amyloid (Aβ) was investigated using quartz crystal microbalance (QCM) and circular dichroism spectroscopy (CD). Here we prepared three types of host Aβ-guest Aβ systems differing in a combination of their secondary structures: namely, β-sheet-β-sheet (system (1)), β-sheet-random coil (system(2)) and random coil-random coil (system(3)). The host Aβ was fixed on the electrode of QCM, and the guest Aβ was dissolved in a buffer solution. The host-guest interaction was monitored through a frequency shift (ΔF) of the quartz vibration: a larger ΔF value means the occurrence of a larger degree of host-guest aggregation. When disaccharide (trehalose, neotrehalose or maltose) was added in the above system, the time dependent profile of ΔF was significantly affected. In systems (1) and (2), any of these disaccharides depressed significantly the host-guest aggregation: maltose and trehalose exhibited the strongest effect in systems (1) and (2), respectively. Interestingly, in system(3), trehalose rather promoted the aggregation compared with the control (without disaccharide), while both maltose and neotrehalose depressed the aggregation as much as in the cases of systems (1) and (2). The results of systems (2) and (3) imply that trehalose more strongly interacts with Aβ in a random coil than that in p-sheets. In fact, CD measurements indicated that trehalose retarded the transformation of Aβ from a random coil to β-sheet. Taken together, these results open up the possibility that trehalose modifies the aggregation process of Aβ through its preferential interaction with the random coil state of Aβ.

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