Anti-oligomeric single chain variable domain antibody differentially affects huntingtin and α-synuclein aggregates

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13 Scopus citations

Abstract

Huntington's and Parkinson's diseases are both neurodegenerative disorders caused at least in part by misfolding and aggregation of huntingtin (htt) and α-synuclein, respectively. Here we use a single chain antibody fragment (scFv) isolated against oligomeric α-synuclein to probe similarities and differences between the aggregation and toxic mechanisms of htt and α-synuclein. When incubated with htt, the scFv both blocks formation of and promotes dissociation of fibrillar aggregates, but stabilizes formation of cytotoxic oligomeric aggregates. Previous studies with monomeric α-synuclein showed the scFv prevented fibrillar aggregation, but blocked toxicity of oligomeric aggregates. These divergent effects suggest the toxic mechanisms of oligomeric aggregates differ among amyloidogenic protein species.

Original languageEnglish (US)
Pages (from-to)517-522
Number of pages6
JournalFEBS Letters
Volume582
Issue number4
DOIs
StatePublished - Feb 20 2008

Keywords

  • Atomic force microscopy
  • Huntingtin
  • Oligomer
  • Single chain variable domain antibody fragment
  • Toxicity
  • α-synuclein

ASJC Scopus subject areas

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

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