α-Synuclein-derived lipoparticles in the study of α-Synuclein amyloid fibril formation

Authors: Marcel Falke, Julian Victor, Michael M. Wördehoff, Alessia Peduzzo, Tao Zhang, Gunnar Schröder, Alexander K. Buell, Wolfgang Hoyer, Manuel Etzkorn

Chemistry and Physics of Lipids, 2019, 220, 57-65. DOI: 10.1016/j.chemphyslip.2019.02.009 



Aggregation of the protein α-Synuclein (αSyn) is of great interest due to its involvement in the pathology of Parkinson’s disease. However, under in vitro conditions αSyn is very soluble and kinetically stable for extended time periods. As a result, most αSyn aggregation assays rely on conditions that artificially induce or enhance aggregation, often by introducing rather non-native conditions. It has been shown that αSyn interacts with membranes and conditions have been identified in which membranes can promote as well as inhibit αSyn aggregation.

It has also been shown that αSyn has the intrinsic capability to assemble lipid-protein-particles, in a similar way as apolipoproteins can form lipid-bilayer nanodiscs. Here they show that these αSyn-lipid particles (αSyn-LiPs) can also effectively induce, accelerate or inhibit αSyn aggregation, depending on the applied conditions. αSyn-LiPs therefore provide a general platform and additional tool, complementary to other setups, to study various aspects of αSyn amyloid fibril formation.

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Instrument: Fluidity One
Therapeutic area: Lipid nanodiscs

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