Formation of spherulitic amyloid β aggregate by anionic liposomes

Toshinori Shimanouchi, Naoya Shimauchi, Ryo Ohnishi, Nachi Kitaura, Hisashi Yagi, Yuji Goto, Hiroshi Umakoshi, Ryoichi Kuboi

Research output: Contribution to journalArticlepeer-review

6 Citations (Scopus)


Alzheimer's disease is the most common form of senile dementia. This neurodegenerative disorder is characterized by an amyloid deposition in senile plaques, composed primarily of fibrils of an aggregated peptide, amyloid β (Aβ). The modeling of a senile plaque formation on a model neuronal membrane under the physiological condition is an attractive issue. In this study, we used anionic liposomes to model the senile plaque formation by Aβ. The growth behavior of amyloid Aβ fibrils was directly observed, revealing that the induction of the spherulitic Aβ aggregates could result from the growth of seeds in the presence of anionic liposomes. The seeds of Aβ fibrils strongly interacted with negatively charged liposome and the subsequent association of the seeds were induced to form the seed cluster with many growth ends, which is advantageous for the formation of spherulitic Aβ aggregates. Therefore, anionic liposomes mediated not only fibril growth but also the aggregation process. These results imply that anionic liposome membranes would affect the aggregate form of Aβ fibrils. The modeling of senile plaque reported here is considered to have great potential for study on the amyloidosis.

Original languageEnglish
Pages (from-to)165-171
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number2
Publication statusPublished - Sept 21 2012
Externally publishedYes


  • Alzheimer's disease
  • Amyloid
  • Liposome
  • Protein aggregation

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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