Review: Formation and properties of amyloid-like fibrils derived from α-synuclein and related proteins

Omar M.A. El-Agnaf, G. Brent Irvine

Research output: Contribution to journalReview article

77 Citations (Scopus)

Abstract

Synucleins are small proteins that are highly expressed in brain tissue and are localised at presynaptic terminals in neurons. α-Synuclein has been identified as a component of intracellular fibrillar protein deposits in several neurodegenerative diseases, and two mutant forms of α-synuclein have been associated with autosomal-dominant Parkinson's Disease. A fragment of α-synuclein has also been identified as the non-Aβ component of Alzheimer's Disease amyloid. In this review we describe some structural properties of α-synuclein and the two mutant forms, as well as α-synuclein fragments, with particular emphasis on their ability to form β-sheet on ageing and aggregate to form amyloid-like fibrils. Differences in the rates of aggregation and morphologies of the fibrils formed by α-synuclein and the two mutant proteins are high-lighted. Interactions between α-synuclein and other proteins, especially those that are components of amyloid or Lewy bodies, are considered. The toxicity of α-synuclein and related peptides towards neurons is also discussing in relation to the aetiology of neurodegenerative diseases. (C) 2000 Academic Press.

Original languageEnglish
Pages (from-to)300-309
Number of pages10
JournalJournal of Structural Biology
Volume130
Issue number2-3
DOIs
Publication statusPublished - 1 Jan 2000

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Keywords

  • Alzheimer's Disease
  • Amyloid
  • Amyotrophic lateral sclerosis
  • Fibrils
  • Lewy bodies
  • Multiple system atrophy
  • Parkinson's Disease
  • α-synuclein

ASJC Scopus subject areas

  • Structural Biology

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