Site-specific inhibitory mechanism for amyloid β42 aggregation by catechol-type flavonoids targeting the lys residues

Mizuho Sato, Kazuma Murakami, Mayumi Uno, Yu Nakagawa, Sumie Katayama, Ken Ichi Akagi, Yuichi Masuda, Kiyonori Takegoshi, Kazuhiro Irie

研究成果: Article査読

121 被引用数 (Scopus)

抄録

Background: The inhibitory mechanism of Aβ42 aggregation by flavonoid is fully unknown. Results: The oxidant enhanced the inhibitory activity of (+)-taxifolin against Aβ42 aggregation by forming Aβ42-taxifolin adducts between the Lys residues and oxidized (+)-taxifolin. Conclusion: The inhibitory activity of catechol-type flavonoids requires autoxidation to form an o-quinone to react with Lys. Significance: These may help design promising inhibitors against Aβ42 aggregation for Alzheimer disease therapy.

本文言語English
ページ(範囲)23212-23224
ページ数13
ジャーナルJournal of Biological Chemistry
288
32
DOI
出版ステータスPublished - 2013 8 9

ASJC Scopus subject areas

  • 生化学
  • 分子生物学
  • 細胞生物学

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