アミロイドベータペプチドの機能解明を目指したO-アシルイソペプチドの利用

• 相馬 洋平

  京都薬科大学、薬品化学分野

• 平山 雄太

  京都薬科大学、薬品化学分野

• 谷口 敦彦

  京都薬科大学、薬品化学分野

• 向井 秀仁

  京都薬科大学、薬品化学分野

• 木曽 良明

  京都薬科大学、薬品化学分野

書誌事項

タイトル別名

• Use of the O-Acyl Isopeptide towards Understanding the Functions of Amyloid Beta Peptides

抄録

The intense and uncontrollable self-assembling natures of Abeta1-42 might lead to irreproducible or discrepant results. As an experimental tool to overcome this problem, we proposed an idea that monomer Abeta could be obtained in situ from the O-acyl isopeptide ("click peptide" concept). The O-acyl isopeptide of Abeta1-42, possessing an ester bond (instead of an amide bond) at the Gly25-Ser26 sequence, adopted a monomeric, random coil state under acidic conditions. Upon change to neutral pH, the O-acyl isopeptide converted to Abeta1-42 promptly through an O-to-N intramolecular acyl migration. As a result of this quick and irreversible conversion, monomer Abeta1-42 with a random coil structure was produced in situ. Moreover, amyloid fibril formation and conformational changes of the produced Abeta1-42 were observed over time. This click peptide strategy might provide a useful experimental system in Alzheimer's disease research.

収録刊行物

• 反応と合成の進歩シンポジウム 発表要旨概要

  反応と合成の進歩シンポジウム 発表要旨概要 36 (0), 146-146, 2010

  日本薬学会化学系薬学部会

キーワード

• acyl migration
• amyloid
• click
• isopeptide
• peptide

詳細情報

• CRID: 1390282680611652352
• NII論文ID: 130006997412
• DOI: 10.14895/hannou.36.0.146.0
• 本文言語コード: ja
• データソース種別:
  • JaLC
  • CiNii Articles
• 抄録ライセンスフラグ: 使用不可