Sentil Kumar Thangaraj, UTwente

Title: Sequestering of cytoskeleton (associated) proteins by amyloid aggregates
Session: Tuesday 6 October, 11:00


Neuronal accumulation of α-synuclein (αS) amyloid aggregates and axonal transport deficits are the characteristic pathological hallmarks of several neurodegenerative diseases including Parkinson's disease. Though the exact mechanism causing the disease is unclear, sequestration of various proteins by intracellular amyloid fibrils has been suggested to play a role in the toxicity of amyloid diseases. Axons are rich in cytoskeletal proteins trigger the idea that amyloid formation may affect the organization of the cytoskeletal (associated) proteins and thereby, neuronal function. Our aim is to investigate the distribution and functionality of these proteins in presence of αS amyloid aggregates in vitro. Preliminary quantitative characterization showed the sequestration and immobilization of cytoskeletal proteins by αS aggregates. Using nanotechnological tools, further analyses examine the biochemical and biophysical properties of motor proteins (Kif5a, in particular) in presence of microtubules and fibrillary αS aggregates.





 to be announced


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