The biological function of the intrinsically disordered protein alpha synuclein is unknown. What is known, is that the protein plays an important role in the formation of Lewy bodies in Parkinsons Disease.
Intrinsically disordered proteins can be regarded as polymers consisting of groups with different physical chemical properties. Which physical chemical interactions dominate, depends on the environment. We have strong indications that this protein can behave like a neutral hydrophilic- charged diblock copolymer. There are indications that the protein can also form “classical” micellar structures due to hydrophobic interactions.
In this project the formation of the latter micelles is the central theme. This formation can be studied with a variety of techniques: light scattering, conductivity, fluorescence assays and possibly AFM.
Since there are several alpha synuclein (disease) mutants available we would like to know whether the formation of these micelles is different for the mutants. This may eventually lead to better understand the biological function of the protein.
For more information contact:
Dr. Saskia Lindhoud