Material properties of supra-fibrillar aggregates

 

In vitro produced supra fibrillar aggregates of the α-synuclein protein involved in Parkinson’s disease differ in morphology from the structures observed in vivo. This difference may be the result of the different aggregation conditions or the protein composition of the aggregates in cells. Alternatively environmental factors that are thought to play a role in Parkinson’s disease such as heavy metals and pesticides may affect inter-fibril interactions. Using atomic force microscopy and spectroscopy, fluorescence microscopy and other biophysical techniques we elucidate the factors governing the assembly of fibrils into stable mesoscopic structures with distinctly different morphologies and material properties.

Scanning electron microscopy image of a network of α-synuclein fibrils.

PhD student: Slav Semerdjiev
Project leader: Mireille Claessens