Small heat shock proteins inhibit in vitro Aβ1-42 amyloidogenesis

Yogish C. Kudva, Henry J. Hiddinga, Peter C. Butler, Cheryl S. Mueske, Norman L. Eberhardt

Research output: Contribution to journalArticlepeer-review

95 Scopus citations


We demonstrate that small heat shock proteins (sHsp) inhibit in vitro amyloid formation by the Alzheimer's Aβ1-42 polypeptide as detected by a thioflavine T fluorescence assay and electron microscopy. Human sHsp27 (0.50-3.0 μM) inhibited amyloid formation from 20 μM Aβ1-42 by 23-75% in 24 h. In contrast, treatment of pre-formed amyloid with 0.5-3.0 μM sHsp27 only reduced the fluorescence signal by 6-36%. The data suggest that ordered fibril formation may represent a form of off-pathway aggregation that can he prevented by chaperone action. The data raise the possibility that age-related changes in chaperone function could contribute toward the pathogenesis of Alzheimer's and other amyloid-associated diseases.

Original languageEnglish (US)
Pages (from-to)117-121
Number of pages5
JournalFEBS Letters
Issue number1
StatePublished - Oct 13 1997


  • Alzheimer's disease
  • Amyloidogenesis
  • Chaperone
  • Heat shock protein

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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