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

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. March 2019

The aggregation of α-synuclein is linked to Parkinson's disease, though under in vitro conditions it can be stable for extended periods.

In this paper Falke et al use the Fluidity One in conjunction with other techniques to probe the interactions of α-synuclein with lipid particles. In particular the authors note that many assays used to study aggregation involve non-native conditions which artificially influence the aggregation process - something that Fluidity One avoids through in-solution, low concentration, unlabelled testing.

The combined insights from multiple techniques used in this study resulted in a detailed picture of the protein-lipid interactions.

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