Amyloid-β annular protofibrils evade fibrillar fate in Alzheimer disease brain

Cristian A. Lasagna-Reeves, Charles G. Glabe, Rakez Kayed

Research output: Contribution to journalArticlepeer-review

123 Scopus citations


Annular protofibrils (APFs) represent a new and distinct class of amyloid structures formed by disease-associated proteins. In vitro, these pore-like structures have been implicated in membrane permeabilization and ion homeostasis via pore formation. Still, evidence for their formation and relevance in vivo is lacking. Herein, we report that APFs are in a distinct pathway from fibril formation in vitro and in vivo. In human Alzheimer disease brain samples, amyloid-β APFs were associated with diffuse plaques, but not compact plaques; moreover, we show the formation of intracellular APFs. Our results together with previous studies suggest that the prevention of amyloid-β annular protofibril formation could be a relevant target for the prevention of amyloid-β toxicity in Alzheimer disease.

Original languageEnglish (US)
Pages (from-to)22122-22130
Number of pages9
JournalJournal of Biological Chemistry
Issue number25
StatePublished - Jun 24 2011

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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