The processes of α-synuclein amyloid protein complexes involved in the pathogenesis of Parkinson’s disease
Artikel i vetenskaplig tidskrift, 2018

Objective. To analyze interactions between α-synuclein (αS) protein and lipids using biophysical methods. Material and methods. Recombinant α-synuclein synthesized in prokaryotic cells was used. To characterize the interaction of αS with negatively charged vesicles of DOPS (1,2-dioleoyl-sn-glycero-3-phospho-L-serine, sodium salt) and DOPG (1,2-dioleoyl-sn-glycero-3-phospho-(1′-rac-glycerol), sodium salt) and the consequences of such interactions on αS amyloid formation, combined circular dichroism, fluorescence and imaging methods in vitro were applied. Results and conclusion. Lipid head-group chemistry modulates αS interactions and also affects amyloid fiber formation. Pre-formed αS oligomers, typically present in a small amount in the αS starting material, acted as templates for linear growth of anomalous amyloid fibers in the presence of vesicles. At the same time, the remaining αS monomers were restricted from vesicle-mediated nucleation of amyloid fibers. Although not a dominant process in bulk experiments, this hidden αS aggregation pathway may be of importance in vivo.

α-synuclein

Circular dichroism spectroscopy

Misfolding

Membrane interactions

Phospholipid vesicles

Aggregation

Atomic power microscopy

Författare

Juris Kiskis

Chalmers, Biologi och bioteknik, Kemisk biologi

Istvan Horvath

Chalmers, Biologi och bioteknik, Kemisk biologi

Pernilla Wittung Stafshede

Chalmers, Biologi och bioteknik, Kemisk biologi

Sandra Rocha

Chalmers, Biologi och bioteknik, Kemisk biologi

Zhurnal Nevrologii i Psikhiatrii imeni S.S. Korsakova

1997-7298 (ISSN)

Vol. 118 8 75-81

Ämneskategorier

Fysikalisk kemi

Biofysik

Medicinsk bioteknologi (med inriktning mot cellbiologi (inklusive stamcellsbiologi), molekylärbiologi, mikrobiologi, biokemi eller biofarmaci)

DOI

10.17116/jnevro201811808175

Mer information

Senast uppdaterat

2018-12-10