Evidence of native α-synuclein conformers in the human brain

J Biol Chem. 2014 Mar 14;289(11):7929-34. doi: 10.1074/jbc.C113.538249. Epub 2014 Jan 28.

Abstract

α-Synuclein aggregation is central to the pathogenesis of several brain disorders. However, the native conformations and functions of this protein in the human brain are not precisely known. The native state of α-synuclein was probed by gel filtration coupled with native gradient gel separation, an array of antibodies with non-overlapping epitopes, and mass spectrometry. The existence of metastable conformers and stable monomer was revealed in the human brain.

Keywords: Alpha-Synuclein; Human Brain; Native State; Neurodegenerative Diseases; Parkinson Disease; Protein Conformation; Protein Folding.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Brain / metabolism*
  • Chromatography, Gel
  • Epitope Mapping
  • Epitopes / chemistry
  • Humans
  • Hydrogen Bonding
  • Mass Spectrometry
  • Neurodegenerative Diseases / metabolism
  • Parkinson Disease / metabolism
  • Protein Binding
  • Protein Folding
  • Protein Structure, Tertiary
  • Sucrose / chemistry
  • Ultracentrifugation
  • alpha-Synuclein / chemistry*

Substances

  • Epitopes
  • alpha-Synuclein
  • Sucrose