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α-Synuclein interaction with POPC/POPS vesicles

Dubackic, Marija LU ; Lattanzi, Veronica LU ; Liu, Yun ; Haertlein, Michael ; Devos, Juliette M. ; Sparr, Emma LU ; Linse, Sara LU and Ulf Olsson, Olsson LU (2025) In Soft Matter 21(5). p.914-926
Abstract

We have investigated the adsorption of the amyloid-forming protein a-Synuclein (aSyn) onto small unilamellar vesicles composed of a mixture of zwitterionic POPC and anionic POPS lipids. aSyn monomers adsorb onto the anionic lipid vesicles where they adopt an a-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 pKa with increasing fraction of POPS. The vesicles with adsorbed aSyn 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... (More)

We have investigated the adsorption of the amyloid-forming protein a-Synuclein (aSyn) onto small unilamellar vesicles composed of a mixture of zwitterionic POPC and anionic POPS lipids. aSyn monomers adsorb onto the anionic lipid vesicles where they adopt an a-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 pKa with increasing fraction of POPS. The vesicles with adsorbed aSyn 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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author
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organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Soft Matter
volume
21
issue
5
pages
914 - 926
publisher
Royal Society of Chemistry
external identifiers
  • scopus:85215826837
  • pmid:39803688
ISSN
1744-683X
DOI
10.1039/d4sm01036a
language
English
LU publication?
yes
id
697a52f6-42ed-418a-93d0-c2f067c49709
date added to LUP
2025-05-27 10:00:05
date last changed
2025-07-08 13:44:29
@article{697a52f6-42ed-418a-93d0-c2f067c49709,
  abstract     = {{<p>We have investigated the adsorption of the amyloid-forming protein a-Synuclein (aSyn) onto small unilamellar vesicles composed of a mixture of zwitterionic POPC and anionic POPS lipids. aSyn monomers adsorb onto the anionic lipid vesicles where they adopt an a-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 pK<sub>a</sub> with increasing fraction of POPS. The vesicles with adsorbed aSyn 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.</p>}},
  author       = {{Dubackic, Marija and Lattanzi, Veronica and Liu, Yun and Haertlein, Michael and Devos, Juliette M. and Sparr, Emma and Linse, Sara and Ulf Olsson, Olsson}},
  issn         = {{1744-683X}},
  language     = {{eng}},
  number       = {{5}},
  pages        = {{914--926}},
  publisher    = {{Royal Society of Chemistry}},
  series       = {{Soft Matter}},
  title        = {{α-Synuclein interaction with POPC/POPS vesicles}},
  url          = {{http://dx.doi.org/10.1039/d4sm01036a}},
  doi          = {{10.1039/d4sm01036a}},
  volume       = {{21}},
  year         = {{2025}},
}