α-Synuclein interaction with POPC/POPS vesicles

We have investigated the adsorption of the amyloid-forming protein α-Synuclein (αSyn) onto small unilamellar vesicles composed of a mixture of zwitterionic POPC and anionic POPS lipids. αSyn monomers adsorb onto the anionic lipid vesicles where they adopt an α-helical secondary structure. The degree of adsorption depends on the fraction of anionic lipid in the mixed lipid membrane, but one needs to consider the electrostatic shift of the serine p<i>K</i><sub>a</sub> with increasing fraction of POPS. The vesicles with adsorbed αSyn monomers are kinetically stable. However, after fibrils have been formed, here triggered by the addition of a small concentration of pre-formed fibrils (seeds), we observed that the average vesicle size increased by approximately a factor of two. This increase in the vesicle size can be explained by vesicle fusion taking place during the fibril formation process.

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Publication Details

Journal
Soft Matter
Published
2025-01-01
DOI
https://doi.org/10.1039/d4sm01036a
Citations
2
Primary Topic
Parkinson's Disease Mechanisms and Treatments
Type
article
Field-Weighted Citation Impact
2.78

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article

α-Synuclein interaction with POPC/POPS vesicles

Ulf Olsson, Michael Haertlein, Juliette M. Devos, Marija Dubackic et al.
2 citations
Soft Matter
Parkinson's Disease Mechanisms and Treatments
2.78
article

α-Synuclein interaction with POPC/POPS vesicles

Ulf Olsson, Michael Haertlein, Juliette M. Devos, Marija Dubackic, Sara Snogerup Linse, Emma Sparr, Veronica Lattanzi, Yun Liu
article en
2 citations

Abstract

We have investigated the adsorption of the amyloid-forming protein α-Synuclein (αSyn) onto small unilamellar vesicles composed of a mixture of zwitterionic POPC and anionic POPS lipids. αSyn monomers adsorb onto the anionic lipid vesicles where they adopt an α-helical secondary structure. The degree of adsorption depends on the fraction of anionic lipid in the mixed lipid membrane, but one needs to consider the electrostatic shift of the serine p<i>K</i><sub>a</sub> with increasing fraction of POPS. The vesicles with adsorbed αSyn monomers are kinetically stable. However, after fibrils have been formed, here triggered by the addition of a small concentration of pre-formed fibrils (seeds), we observed that the average vesicle size increased by approximately a factor of two. This increase in the vesicle size can be explained by vesicle fusion taking place during the fibril formation process.

Soft MatterVol. 21(5)
National Institute of Standards and Technology (US), Lund University (SE), Institut Laue-Langevin (FR), NIST Center for Neutron Research (US), University of Delaware (US)
Stiftelsen för Strategisk Forskning, Knut och Alice Wallenbergs Stiftelse, Vetenskapsrådet, National Institute of Standards and Technology
Clean water and sanitation
Openalex Percentile: Top 13%
Parkinson's Disease Mechanisms and Treatments
2.78
DOIOpen Access PDFOpenAlex
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α-Synuclein interaction with POPC/POPS vesicles — Ulf Olsson, Michael Haertlein, et al. · Soft Matter (2025) | TGRS Research Map | TGRS