Effect of copper (II) ion against elongation behavior of amyloid β fibrils on liposome membranes

Toshinori Shimanouchi, R. Onishi, N. Kitaura, H. Umakoshi, R. Kuboi

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

The fibril growth behavior of amyloid β protein (Aβ) on cell membranes is relating to the progression of Alzheimer's disease. This growth behavior of Aβ fibrils is sensitively affected by the metal ions, neurotransmitters, or bioreactive substrate. The inhibitory effect of those materials was quantitatively estimated from the viewpoints of "crystal growth". In a bulk aqueous solution, copper (II) ion showed the strong inhibitory effect on the growth of Aβ fibrils. Meanwhile, the addition of a closed-phospholipid bilayer membrane (liposome) could reduce the above inhibitory effect of copper (II) ion.

Original languageEnglish
Pages (from-to)101-108
Number of pages8
JournalCrystal Research and Technology
Volume47
Issue number1
DOIs
Publication statusPublished - Jan 2012
Externally publishedYes

Fingerprint

Liposomes
Amyloid
elongation
Copper
Elongation
Ions
membranes
Membranes
copper
neurotransmitters
Serum Amyloid A Protein
ions
Phospholipids
Cell membranes
Crystallization
Crystal growth
progressions
Metal ions
Neurotransmitter Agents
crystal growth

Keywords

  • amyloid fibrils
  • copper ions
  • inhibitory
  • liposome

ASJC Scopus subject areas

  • Chemistry(all)
  • Materials Science(all)
  • Condensed Matter Physics

Cite this

Effect of copper (II) ion against elongation behavior of amyloid β fibrils on liposome membranes. / Shimanouchi, Toshinori; Onishi, R.; Kitaura, N.; Umakoshi, H.; Kuboi, R.

In: Crystal Research and Technology, Vol. 47, No. 1, 01.2012, p. 101-108.

Research output: Contribution to journalArticle

Shimanouchi, Toshinori ; Onishi, R. ; Kitaura, N. ; Umakoshi, H. ; Kuboi, R. / Effect of copper (II) ion against elongation behavior of amyloid β fibrils on liposome membranes. In: Crystal Research and Technology. 2012 ; Vol. 47, No. 1. pp. 101-108.
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