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α-Synuclein insertion into supported lipid bilayers as seen by in situ X-ray reflectivity.

Abstract：

:Large aggregates of misfolded α-synuclein inside neuronal cells are the hallmarks of Parkinson's disease. The protein's natural function and its supposed toxicity, however, are believed to be closely related to its interaction with cell and vesicle membranes. Upon this interaction, the protein folds into an α-helical structure and intercalates into the membrane. In this study, we focus on the changes in the lipid bilayer caused by this intrusion. In situ X-ray reflectivity was applied to determine the vertical density structure of the bilayer before and after exposure to α-synuclein. It was found that the α-synuclein insertion, wild type and E57K variant, caused a reduction in bilayer thickness. This effect may be one factor in the membrane pore formation ability of α-synuclein.

journal_name

ACS Chem Neurosci

journal_title

ACS chemical neuroscience

authors

Hähl H,Möller I,Kiesel I,Campioni S,Riek R,Verdes D,Seeger S

doi

10.1021/cn5002683

subject

Has Abstract

pub_date

2015-03-18 00:00:00

pages

374-9

issue

3

issn

1948-7193

journal_volume

6

pub_type

杂志文章

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