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.
Highlights
␣-Synuclein aggregation is central to the pathogenesis of several brain disorders
␣-Synuclein is a soluble protein consisting of 140 amino acids with a predicted molecular mass of 14,460.16 Da and an isoelectric point of 4.67. ␣-Synuclein is expressed in neurons throughout the central nervous system [1, 2]
Evaluation of protein sizes under native states that rely on methods based on first principles such as sedimentation equilibrium ultracentrifugation and scanning transmission electron microscopy (STEM)2 suggested that ␣-synuclein isolated from fresh human red blood cells or cultured neuroblastoma cells exhibited the properties of a natively folded tetramer rich in ␣-helical content [26]
Summary
␣-Synuclein aggregation is central to the pathogenesis of several brain disorders. the native conformations and functions of this protein in the human brain are not precisely known. ␣-Synuclein was eluted from gel filtration columns into four main fractions corresponding to Stokes radii of 32.3–37.5 Å for both the native and the heat-denatured brain extracts.
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