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  • Refolding of helical soluble α-synuclein through transient interaction with lipid interfaces.

Refolding of helical soluble α-synuclein through transient interaction with lipid interfaces.

FEBS letters (2018-04-11)
Matteo Rovere, John B Sanderson, Luis Fonseca-Ornelas, Dushyant S Patel, Tim Bartels
ABSTRACT

α-Synuclein (αSyn) is a key player in the pathogenesis of Parkinson's disease and other synucleinopathies. Here, we report the existence of a novel soluble α-helical conformer of αSyn, obtained through transient interaction with lipid interfaces, and propose dynamic oligomerization as the mechanism underlying its stability. The conformational space of αSyn appears to be highly context-dependent, and lipid bilayers might thus play crucial roles as molecular chaperones in a cellular environment.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Anti-α-Synuclein Antibody, clone SOY1, clone SOY1, from mouse
Sigma-Aldrich
Anti-α-Synuclein Antibody, clone 2F12, clone 2F12, from mouse
Sigma-Aldrich
Human DSC-3 ELISA Kit, for cell culture supernatants, plasma, and serum samples