Amyloidogenic protein-membrane interactions: Mechanistic insight from model systems

Sara M. Butterfield, Hilal A. Lashuel

Research output: Contribution to journalArticle

356 Citations (Scopus)

Abstract

The toxicity of amyloid-forming proteins is correlated with their interactions with cell membranes. Binding events between amyloidogenic proteins and membranes result in mutally disruptive structural perturbations, which are associated with toxicity. Membrane surfaces promote the conversion of amyloid-forming proteins into toxic aggregates, and amyloidogenic proteins, in turn, compromise the structural integrity of the cell membrane. Recent studies with artificial model membranes have highlighted the striking resemblance of the mechanisms of membrane permeabilization of amyloid-forming proteins to those of pore-forming toxins and antimicrobial peptides.

Original languageEnglish
Pages (from-to)5628-5654
Number of pages27
JournalAngewandte Chemie - International Edition
Volume49
Issue number33
DOIs
Publication statusPublished - 2 Aug 2010
Externally publishedYes

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Keywords

  • Amyloid toxicity
  • Artificial membranes
  • Fibrillogenesis
  • Permeabilization
  • Pore-forming proteins

ASJC Scopus subject areas

  • Chemistry(all)
  • Catalysis

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