Protein aggregation, associated with multiple neurodegenerative disorders, has been a topic of significant scientific interest for decades. However, it is only recently that the aggregation process has been recognized as being influenced by another biologically important phenomenon - liquid-liquid phase separation, which underlies the formation of membraneless organelles. Investigating the role of biomolecular condensates in protein aggregation is essential for understanding the mechanisms of amyloid formation and for identifying new strategies for treatment and prevention. In the talk, I will discuss the key factors through which the physical and chemical environment of a condensate can influence protein aggregation. I will also focus on the specific case of α-synuclein (one of the archetypal amyloid-forming proteins), its aggregation in the presence of model liquid condensates, and the role of condensate interfaces in this process.

References:
B.S. Visser, W.P. Lipiński, E. Spruijt “The role of biomolecular condensates in protein aggregation” Nature Reviews Chemistry, 2024, https://doi.org/10.1038/s41570-024-00635-w
W.P. Lipiński, B.S. Visser, I. Robu, M.A.A. Fakhree, S. Lindhoud, M.M.A.E. Claessens, E. Spruijt “Biomolecular condensates can both accelerate and suppress aggregation of α-synuclein” Science Advances, 2022, https://doi.org/10.1126/sciadv.abq6495
B.S. Visser, M.H.I. van Haren, W.P. Lipiński, K.A. van Leijenhorst-Groener, M.M.A.E. Claessens, M.V.A. Queirós, C.H.I. Ramos, J. Eeftens, E. Spruijt, “Controlling interfacial protein adsorption, desorption and aggregation in biomolecular condensates” bioRxiv preprint, 2024, https://doi.org/10.1101/2024.10.20.619145