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

Research output: Contribution to journalArticle

105 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)23212-23224
Number of pages13
JournalJournal of Biological Chemistry
Volume288
Issue number32
DOIs
Publication statusPublished - 2013 Aug 9

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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    Sato, M., Murakami, K., Uno, M., Nakagawa, Y., Katayama, S., Akagi, K. I., Masuda, Y., Takegoshi, K., & Irie, K. (2013). Site-specific inhibitory mechanism for amyloid β42 aggregation by catechol-type flavonoids targeting the lys residues. Journal of Biological Chemistry, 288(32), 23212-23224. https://doi.org/10.1074/jbc.M113.464222