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α-Synuclein Interaction with Lipid Bilayer Discs

Dubackic, Marija LU ; Liu, Yun ; Kelley, Elizabeth G. ; Hetherington, Crispin LU orcid ; Haertlein, Michael ; Devos, Juliette M. ; Linse, Sara LU ; Sparr, Emma LU and Olsson, Ulf LU (2022) In Langmuir 38(33). p.10216-10224
Abstract

α-Synuclein (aSyn) is a 140 residue long protein present in presynaptic termini of nerve cells. The protein is associated with Parkinson's disease, in which case it has been found to self-Assemble into long amyloid fibrils forming intracellular inclusions that are also rich in lipids. Furthermore, its synaptic function is proposed to involve interaction with lipid membranes, and hence, it is of interest to understand aSyn-lipid membrane interactions in detail. In this paper we report on the interaction of aSyn with model membranes in the form of lipid bilayer discs. Using a combination of cryogenic transmission electron microscopy and small-Angle neutron scattering, we show that circular discs undergo a significant shape transition... (More)

α-Synuclein (aSyn) is a 140 residue long protein present in presynaptic termini of nerve cells. The protein is associated with Parkinson's disease, in which case it has been found to self-Assemble into long amyloid fibrils forming intracellular inclusions that are also rich in lipids. Furthermore, its synaptic function is proposed to involve interaction with lipid membranes, and hence, it is of interest to understand aSyn-lipid membrane interactions in detail. In this paper we report on the interaction of aSyn with model membranes in the form of lipid bilayer discs. Using a combination of cryogenic transmission electron microscopy and small-Angle neutron scattering, we show that circular discs undergo a significant shape transition after the adsorption of aSyn. When aSyn self-Assembles into fibrils, aSyn molecules desorb from the bilayer discs, allowing them to recover to their original shape. Interestingly, the desorption process has an all-or-none character, resulting in a binary coexistence of circular bilayer discs with no adsorbed aSyn and deformed bilayer discs having a maximum amount of adsorbed protein. The observed coexistence is consistent with the recent finding of cooperative aSyn adsorption to anionic lipid bilayers.

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author
; ; ; ; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Langmuir
volume
38
issue
33
pages
9 pages
publisher
The American Chemical Society (ACS)
external identifiers
  • scopus:85136610891
  • pmid:35952001
ISSN
0743-7463
DOI
10.1021/acs.langmuir.2c01368
language
English
LU publication?
yes
id
a4293f2a-0c90-440f-8497-66459512aa62
date added to LUP
2022-10-18 14:44:45
date last changed
2024-06-13 14:19:25
@article{a4293f2a-0c90-440f-8497-66459512aa62,
  abstract     = {{<p>α-Synuclein (aSyn) is a 140 residue long protein present in presynaptic termini of nerve cells. The protein is associated with Parkinson's disease, in which case it has been found to self-Assemble into long amyloid fibrils forming intracellular inclusions that are also rich in lipids. Furthermore, its synaptic function is proposed to involve interaction with lipid membranes, and hence, it is of interest to understand aSyn-lipid membrane interactions in detail. In this paper we report on the interaction of aSyn with model membranes in the form of lipid bilayer discs. Using a combination of cryogenic transmission electron microscopy and small-Angle neutron scattering, we show that circular discs undergo a significant shape transition after the adsorption of aSyn. When aSyn self-Assembles into fibrils, aSyn molecules desorb from the bilayer discs, allowing them to recover to their original shape. Interestingly, the desorption process has an all-or-none character, resulting in a binary coexistence of circular bilayer discs with no adsorbed aSyn and deformed bilayer discs having a maximum amount of adsorbed protein. The observed coexistence is consistent with the recent finding of cooperative aSyn adsorption to anionic lipid bilayers.</p>}},
  author       = {{Dubackic, Marija and Liu, Yun and Kelley, Elizabeth G. and Hetherington, Crispin and Haertlein, Michael and Devos, Juliette M. and Linse, Sara and Sparr, Emma and Olsson, Ulf}},
  issn         = {{0743-7463}},
  language     = {{eng}},
  month        = {{08}},
  number       = {{33}},
  pages        = {{10216--10224}},
  publisher    = {{The American Chemical Society (ACS)}},
  series       = {{Langmuir}},
  title        = {{α-Synuclein Interaction with Lipid Bilayer Discs}},
  url          = {{http://dx.doi.org/10.1021/acs.langmuir.2c01368}},
  doi          = {{10.1021/acs.langmuir.2c01368}},
  volume       = {{38}},
  year         = {{2022}},
}