The density of anionic lipids modulates the adsorption of α-Synuclein onto lipid membranes
(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
- Andersson, Alexandra LU ; Linse, Sara LU ; Sparr, Emma LU ; Fornasier, Marco LU and Jönsson, Peter LU
- organization
-
- LU Profile Area: Light and Materials
- LTH Profile Area: Nanoscience and Semiconductor Technology
- NanoLund: Centre for Nanoscience
- Physical Chemistry
- MultiPark: Multidisciplinary research focused on Parkinson´s disease
- Biochemistry and Structural Biology
- LU Profile Area: Proactive Ageing
- LTH Profile Area: Engineering Health
- publishing date
- 2024-02
- 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}}, }