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

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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Rovere M,Sanderson JB,Fonseca-Ornelas L,Patel DS,Bartels T

doi

10.1002/1873-3468.13047

subject

Has Abstract

pub_date

2018-05-01 00:00:00

pages

1464-1472

issue

9

eissn

0014-5793

issn

1873-3468

journal_volume

592

pub_type

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