Effects of the mutations Ala30 to Pro and Ala53 to Thr on the physical and morphological properties of α-synuclein protein implicated in Parkinson's disease

Omar M.A. El-Agnaf, Ross Jakes, Martin D. Curran, Andrew Wallace

Research output: Contribution to journalArticle

211 Citations (Scopus)

Abstract

α-Synuclein (α-syn) protein has been found in association with the pathological lesions of a number of neurodegenerative diseases. Recently, mutations in the α-syn gene have been reported in families susceptible to an inherited form of Parkinson's disease. We report here that human wild-type α-syn, PD-linked mutant α-syn(Ala30Pro) and mutant α-syn(Ala53Thr) proteins can self-aggregate and form amyloid-like filaments. The mutant α-syn forms more β-sheet and mature filaments than the wild-type protein. These findings suggest that accumulation of α-syn as insoluble deposits of amyloid may play a major role in the pathogenesis of these neurodegenerative diseases. Copyright (C) 1998 Federation of European Biochemical Societies.

Original languageEnglish
Pages (from-to)67-70
Number of pages4
JournalFEBS Letters
Volume440
Issue number1-2
DOIs
Publication statusPublished - 27 Nov 1998

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Keywords

  • Amyloid
  • Lewy body
  • Neurodegenerative disease
  • Parkinson's disease
  • Self-aggregation
  • α-Synuclein

ASJC Scopus subject areas

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

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