Iron-mediated interaction of alpha synuclein with lipid raft model membranes.
Ferrous Compounds
/ chemistry
Humans
Iron
/ chemistry
Lipid Bilayers
/ chemistry
Membrane Microdomains
/ chemistry
Microscopy, Atomic Force
Mutagenesis, Site-Directed
Parkinson Disease
/ metabolism
Protein Aggregates
Protein Binding
Spectroscopy, Fourier Transform Infrared
alpha-Synuclein
/ chemistry
Journal
Nanoscale
ISSN: 2040-3372
Titre abrégé: Nanoscale
Pays: England
ID NLM: 101525249
Informations de publication
Date de publication:
14 Apr 2020
14 Apr 2020
Historique:
pubmed:
28
2
2020
medline:
31
12
2020
entrez:
28
2
2020
Statut:
ppublish
Résumé
The aberrant misfolding and aggregation of alpha synuclein (αS) into toxic oligomeric species is one of the key features associated with the pathogenesis of Parkinson's disease (PD). It involves different biochemical and biophysical factors as plasma membrane binding and interaction with heavy metal ions. In the present work, atomic force microscopy (AFM) is combined with Fourier Transform Infrared Spectroscopy (FTIR) measurements to investigate the interaction of wild-type (WT) and A53T mutated alpha synuclein with artificial lipid bilayers mimicking lipid raft (LR) domains, before and after ferrous cations (Fe
Substances chimiques
Ferrous Compounds
0
Lipid Bilayers
0
Protein Aggregates
0
alpha-Synuclein
0
Iron
E1UOL152H7
ferrous chloride
S3Y25PHP1W
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM