Multiple ligand interaction of α-synuclein produced various forms of protein aggregates in the presence of Aβ25-35, copper, and eosin

Young Sik Kim, Daekyun Lee, Eun Kyung Lee, Jee Young Sung, Kwang Chul Chung, Jongsun Kim, Seung R. Paik

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Various protein aggregates of α-synuclein developed by way of the common protein self-oligomerization in the presence of Aβ25-35, copper, and eosin were examined. All the aggregates exhibited congo red birefringence although the actual amounts of the aggregates were varied as determined by thioflavin T binding fluorescence. When their morphologies were analyzed in relation to in vitro cytotoxicity, the smallest granular aggregates obtained with copper exhibited the highest cytotoxicity, while the fibrous structures by eosin did not affect the cell.

Original languageEnglish
Pages (from-to)93-98
Number of pages6
JournalBrain Research
Issue number1
Publication statusPublished - 2001 Jul 10



  • α-synuclein
  • Cytotoxicity
  • Parkinson's disease
  • Protein aggregation
  • Self-oligomerization

ASJC Scopus subject areas

  • Neuroscience(all)

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