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Keywords:

  • aggregation;
  • amyloid-β-protein;
  • conformation;
  • neuroblastoma cell;
  • specific binding

Abstract:

In flow cytometry using two detecting methods, we have found that amyloid-β-protein(1–40) [Aβ(1–40)] has high affinity to IMR-32 neuroblastoma cell membrane when it is aggregated to form β-sheet conformation, whereas random coil small Aβ-species has low affinity. The difference in the binding ability to the cell membranes well accounts for the cytotoxicity of Aβ(1–40); namely, aggregated β-sheet Aβ(1–40) gives cytotoxicity higher than random coil Aβ(1–40). Specific binding between Aβ(1–40) and ganglioside GM1 of the raft-like domain in lipid membrane is suggested from a surface plasmon resonance (SPR) experiment.