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The density of anionic lipids modulates the adsorption of α-Synuclein onto lipid membranes

Andersson, Alexandra LU ; Linse, Sara LU ; Sparr, Emma LU ; Fornasier, Marco LU orcid and Jönsson, Peter LU (2024) In Biophysical Chemistry 305.
Abstract

α-Synuclein is an intrinsically disordered presynaptic protein associated with Parkinson's disease. The physiological role of α-Synuclein is not fully understood, but the protein is known to interact with lipid membranes. We here study how membrane charge affects the adsorption of α-Synuclein to (i) supported lipid bilayers and (ii) small unilamellar vesicles with varying amounts of anionic lipids. The results showed that α-Synuclein adsorbs onto membranes containing ≥5% anionic phosphatidylserine (DOPS) lipids, but not to membranes containing ≤1% DOPS. The density of adsorbed α-Synuclein increased steadily with the DOPS content up to 20% DOPS, after which it leveled off. The vesicles were saturated with α-Synuclein at a 3–5 times... (More)

α-Synuclein is an intrinsically disordered presynaptic protein associated with Parkinson's disease. The physiological role of α-Synuclein is not fully understood, but the protein is known to interact with lipid membranes. We here study how membrane charge affects the adsorption of α-Synuclein to (i) supported lipid bilayers and (ii) small unilamellar vesicles with varying amounts of anionic lipids. The results showed that α-Synuclein adsorbs onto membranes containing ≥5% anionic phosphatidylserine (DOPS) lipids, but not to membranes containing ≤1% DOPS. The density of adsorbed α-Synuclein increased steadily with the DOPS content up to 20% DOPS, after which it leveled off. The vesicles were saturated with α-Synuclein at a 3–5 times higher protein density compared to the supported bilayers, which suggests that a more deformable membrane binds more α-Synuclein. Altogether, the results show that both membrane charge density and flexibility influence the association of α-Synuclein to lipid membranes.

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author
; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Alpha-synuclein, Circular dichroism spectroscopy, Fluorescence microscopy, Lipid bilayer mobility, Protein adsorption, Supported lipid bilayers
in
Biophysical Chemistry
volume
305
article number
107143
publisher
Elsevier
external identifiers
  • pmid:38100855
  • scopus:85179920483
ISSN
0301-4622
DOI
10.1016/j.bpc.2023.107143
language
English
LU publication?
yes
id
34d7428a-c565-4d91-bf0c-62787e4d7dcc
date added to LUP
2024-01-31 10:15:46
date last changed
2024-04-16 22:32:18
@article{34d7428a-c565-4d91-bf0c-62787e4d7dcc,
  abstract     = {{<p>α-Synuclein is an intrinsically disordered presynaptic protein associated with Parkinson's disease. The physiological role of α-Synuclein is not fully understood, but the protein is known to interact with lipid membranes. We here study how membrane charge affects the adsorption of α-Synuclein to (i) supported lipid bilayers and (ii) small unilamellar vesicles with varying amounts of anionic lipids. The results showed that α-Synuclein adsorbs onto membranes containing ≥5% anionic phosphatidylserine (DOPS) lipids, but not to membranes containing ≤1% DOPS. The density of adsorbed α-Synuclein increased steadily with the DOPS content up to 20% DOPS, after which it leveled off. The vesicles were saturated with α-Synuclein at a 3–5 times higher protein density compared to the supported bilayers, which suggests that a more deformable membrane binds more α-Synuclein. Altogether, the results show that both membrane charge density and flexibility influence the association of α-Synuclein to lipid membranes.</p>}},
  author       = {{Andersson, Alexandra and Linse, Sara and Sparr, Emma and Fornasier, Marco and Jönsson, Peter}},
  issn         = {{0301-4622}},
  keywords     = {{Alpha-synuclein; Circular dichroism spectroscopy; Fluorescence microscopy; Lipid bilayer mobility; Protein adsorption; Supported lipid bilayers}},
  language     = {{eng}},
  publisher    = {{Elsevier}},
  series       = {{Biophysical Chemistry}},
  title        = {{The density of anionic lipids modulates the adsorption of α-Synuclein onto lipid membranes}},
  url          = {{http://dx.doi.org/10.1016/j.bpc.2023.107143}},
  doi          = {{10.1016/j.bpc.2023.107143}},
  volume       = {{305}},
  year         = {{2024}},
}