Soluble multimeric Alzheimer β(1-40) pre-amyloid complexes in dilute solution

Harry Levine

Research output: Contribution to journalArticlepeer-review

97 Scopus citations


Aqueous solutions of β(1-40) peptide spontaneously associate to form pentameric/hexameric complexes that can be demonstrated by SDS-PAGE following treatment with glutaraldehyde and borohydride reduction. Under amyloidogenic conditions of pH and high peptide concentration these aggregates can further associate to form sedimentable and filterable structures with β-sheet amyloid characteristics of Thioflavine T fluorescence. The presence of such preamyloid structures at low peptide concentration suggests a mechanism by which amyloid plaques can accrete additional material by a cooperative rather than monomeric growth. The existence of a monomer {left and right arrow, wavy} multimer equilibrium may partly explain the divergence of biological consequences with respect to neurotoxicity.

Original languageEnglish
Pages (from-to)755-764
Number of pages10
JournalNeurobiology of Aging
Issue number5
StatePublished - 1995


  • Borohydride reduction SDS-PAGE
  • Crosslinking
  • Fibril formation model
  • Glutaraldehyde
  • Multimers
  • Synthetic peptide
  • pH dependence

ASJC Scopus subject areas

  • General Neuroscience
  • Aging
  • Clinical Neurology
  • Developmental Biology
  • Geriatrics and Gerontology


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