Review: formation and properties of amyloid-like fibrils derived from alpha-synuclein and related proteins.

O.M. El-Agnaf, Brent Irvine

Research output: Contribution to journalArticle

79 Citations (Scopus)

Abstract

Synucleins are small proteins that are highly expressed in brain tissue and are localised at presynaptic terminals in neurons. alpha-Synuclein has been identified as a component of intracellular fibrillar protein deposits in several neurodegenerative diseases, and two mutant forms of alpha-synuclein have been associated with autosomal-dominant Parkinson's Disease. A fragment of alpha-synuclein has also been identified as the non-Abeta component of Alzheimer's Disease amyloid. In this review we describe some structural properties of alpha-synuclein and the two mutant forms, as well as alpha-synuclein fragments, with particular emphasis on their ability to form beta-sheet on ageing and aggregate to form amyloid-like fibrils. Differences in the rates of aggregation and morphologies of the fibrils formed by alpha-synuclein and the two mutant proteins are highlighted. Interactions between alpha-synuclein and other proteins, especially those that are components of amyloid or Lewy bodies, are considered. The toxicity of alpha-synuclein and related peptides towards neurons is also discussing in relation to the aetiology of neurodegenerative diseases.
Original languageEnglish
Pages (from-to)300-309
Number of pages10
JournalJournal of structural biology
Volume130(2-3)
Issue number2-3
DOIs
Publication statusPublished - 2000

ASJC Scopus subject areas

  • Structural Biology

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