ArticleChemistry and physics of lipids2019
α-Synuclein-derived lipoparticles in the study of α-Synuclein amyloid fibril formation.
Article in Chemistry and physics of lipids, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 9 citations in OpenAlex.
- Single-molecule digital sizing of proteins in solution.Nature communications · 2024Article
- Structural Specificity of Polymorphic Forms of α-Synuclein Amyloid.Biomedicines · 2023Article
- Rapid Formation of Peptide/Lipid Coaggregates by the Amyloidogenic Seminal Peptide PAPBiophysical journal · 2020Article
- Clustering of human prion protein and α-synuclein oligomers requires the prion protein N-terminus.Communications biology · 2020Article
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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 we 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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