Insight into conformational modification of alpha-synuclein in the presence of neuronal whole cells and of their isolated membranes.

Abstract:

:A change in the conformational plasticity of α-Synuclein (α-Syn) is hypothesised to be a key step in the pathogenic mechanism of Parkinson's disease (PD). Here, we report the study of extracellular α-Syn interaction with whole cells and membranes isolated from the neuronal SH-SY5Y cells, exploiting NMR and CD spectroscopies. In addition, the crosslinking agent DSG was used to freeze the conformational and oligomeric state of α-Syn in the presence of cells. These data, in a quasi-physiological environment, confirm the protein monomeric state with a propensity to adopt a transient alpha helical following interaction with biological membranes.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Smaldone G,Diana D,Pollegioni L,Di Gaetano S,Fattorusso R,Pedone E

doi

10.1016/j.febslet.2015.02.012

subject

Has Abstract

pub_date

2015-03-24 00:00:00

pages

798-804

issue

7

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(15)00092-7

journal_volume

589

pub_type

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