?-Synuclein-derived lipoparticles in the study of ?-Synuclein amyloid fibril formation.

ABSTRACT: Aggregation of the protein ?-Synuclein (?Syn) is of great interest due to its involvement in the pathology of Parkinson's disease. However, under in vitro conditions ?Syn is very soluble and kinetically stable for extended time periods. As a result, most ?Syn aggregation assays rely on conditions that artificially induce or enhance aggregation, often by introducing rather non-native conditions. It has been shown that ?Syn interacts with membranes and conditions have been identified in which membranes can promote as well as inhibit ?Syn aggregation. It has also been shown that ?Syn has the intrinsic capability to assemble lipid-protein-particles, in a similar way as apolipoproteins can form lipid-bilayer nanodiscs. Here we show that these ?Syn-lipid particles (?Syn-LiPs) can also effectively induce, accelerate or inhibit ?Syn aggregation, depending on the applied conditions. ?Syn-LiPs therefore provide a general platform and additional tool, complementary to other setups, to study various aspects of ?Syn amyloid fibril formation.

SUBMITTER: Falke M 

PROVIDER: S-EPMC6451039 | biostudies-literature | 2019 May

REPOSITORIES: biostudies-literature