Refolding of helical soluble α-synuclein through transient interaction with lipid interfaces.
FEBS Lett
; 592(9): 1464-1472, 2018 05.
Article
en En
| MEDLINE
| ID: mdl-29633780
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.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Alfa-Sinucleína
/
Metabolismo de los Lípidos
/
Replegamiento Proteico
Límite:
Humans
Idioma:
En
Revista:
FEBS Lett
Año:
2018
Tipo del documento:
Article
País de afiliación:
Estados Unidos