α-Synuclein interaction with POPC/POPS vesicles

Published

January 1, 2025

Author(s)

Marija Dubackic, Veronica Lattanzi, Yun Liu, Michael Haertlein, Juliette Devos, Emma Sparr, Sara Linse, Ulf Olsson

Abstract

We have investigated the interactions between α-Synuclein (aSyn) and small unilamellar vesicles composed of a mixture of zwitterionic POPC and anionic POPS lipids. aSyn monomers spontaneously adsorb onto the anionic lipid vesicles where they adopt an α-helix secondary structure. The amount of formed α-helices depends on the fraction of anionic lipid in the mixed lipid membrane. Under the conditions where aSyn fibril formation is not occurring, the vesicles with adsorbed monomers are undeformed. However, after fibrils have been formed, here triggered by the addition of a small concentration of pre-formed fibrils (seeds), the average vesicle size has increased by approximately a factor of two, indicating that a few fusion events have been taking place during the aggregation process.

Citation

Soft Matter

Volume

21

Issue

5

Pub Type

Journals

Download Paper

https://doi.org/10.1039/d4sm01036a

Local Download

Keywords

synuclein, lipid, small angle neutron scattering, fibril, aggregation

Citation

Dubackic, M. , Lattanzi, V. , Liu, Y. , Haertlein, M. , Devos, J. , Sparr, E. , Linse, S. and Olsson, U. (2025), α-Synuclein interaction with POPC/POPS vesicles, Soft Matter, [online], https://doi.org/10.1039/d4sm01036a, https://tsapps.nist.gov/publication/get_pdf.cfm?pub_id=958401 (Accessed July 12, 2025)