Copper-mediated growth of amyloid β fibrils in the presence of oxidized and negatively charged liposomes

Toshinori Shimanouchi, Ryo Onishi, Nachi Kitaura, Hiroshi Umakoshi, Ryoichi Kuboi

Research output: Contribution to journalArticle

8 Citations (Scopus)


Amyloid β protein (Aβ) from Alzheimer's disease formed fibrillar aggregates and their morphology depended on oxidized and negatively charged liposomes. The morphology of fibrillar aggregates was affected by Cu 2+, together with their growth kinetics. This is because Cu 2+ inhibited the nucleation step in the formation of amyloid Aβ fibrillar aggregates by forming Aβ/Cu complex inactive to the growth of fibrillar aggregates. In addition, this is probably because Cu 2+ affected the fibrillar aggregate formed on the surface of liposomes. These findings would give a better understanding of the formation mechanism of amyloid fibrils on biomembranes.

Original languageEnglish
Pages (from-to)611-615
Number of pages5
JournalJournal of Bioscience and Bioengineering
Issue number6
Publication statusPublished - Dec 1 2011
Externally publishedYes



  • Amyloid β protein
  • Copper ion
  • Liposome
  • Morphology

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology

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