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Portrait of Sara Snogerup Linse

Sara Linse


Portrait of Sara Snogerup Linse

Membrane Interaction of α-Synuclein in Different Aggregation States


  • Marie Grey
  • Sara Linse
  • Hanna Nilsson
  • Patrik Brundin
  • Emma Sparr

Summary, in English

Aggregated α-synuclein in Lewy bodies is one of the hallmarks of Parkinson's disease (PD). Earlier observations of α-synuclein aggregates in neurons grafted into brains of PD patients suggested cell-to-cell transfer of α-synuclein and a prion-like mechanism. This prompted the current investigation of whether α-synuclein passes over model phospholipid bilayers. We generated giant unilamellar vesicles (GUVs) containing a small amount of a lipid-conjugated red emitting dye (rhodamine B) and varied the membrane charge by using different molar ratios of DOPC and DOPS or cardiolipin. We then used confocal fluorescence microscopy to examine how monomer, fibril as well as on-pathway α-synuclein species labeled with a green emitting fluorophore (Alexa488) interacted with the phospholipid bilayers of the GUV. We defined conditions that yielded reproducible aggregation kinetics under basal conditions and with none or moderate shaking. We found that on-pathway α-synuclein species and equilibrium amyloid aggregates, but not α-synuclein monomers, bound to lipid membranes. α-Synuclein was particularly strongly associated with GUVs containing the anionic lipids cardiolipin or DOPS, whereas it did not associate with GUVs containing only zwitterionic DOPC. We found that α-synuclein progressively aggregated at the surface of the GUVs, typically in distinct domains rather than uniformly covering the membrane, and that both lipid and protein were incorporated in the aggregates. Importantly, we never observed transport of α-synuclein over the GUV bilayer. This suggests that α-synuclein transport over membranes requires additional molecular players and that it might rely on active transport.


  • Physical Chemistry
  • Biochemistry and Structural Biology
  • Biophysical Chemistry
  • Department of Experimental Medical Science
  • MultiPark: Multidisciplinary research focused on Parkinson´s disease

Publishing year







Journal of Parkinson's Disease





Document type

Journal article


IOS Press


  • Neurology




  • ISSN: 1877-718X