Members of the nanobiophysics group worked together with Evan Spruijt from the Radboud University.
The research team studied the protein alpha-synuclein (Parkinson’s disease) to determine how fast the aggregates are formed. “We have studied three different kinds of droplets (coacervates) and created a new variant of the protein which lights up when the protein enters the aggregate to ensure we could measure both where and when aggregates form”, Spruijt explains. They found that condensates can speed up amyloid formation when proteins localize to their interface. However, condensates can also slow down aggregation by sequestering and stabilizing amyloidogenic proteins. “Especially where the protein alpha-synuclein sticks to the edge of the droplets, we see faster aggregation. If the protein is completely incorporated into the droplets, this can slow down aggregation and therefore possibly delay the formation of harmful protein aggregates”, Spruijt says.
Biomolecular condensates can both accelerate and suppress aggregation of α synuclein
Wojciech P. Lipiński, Brent S. Visser, Irina Robu, Mohammad A. A. Fakhree, Saskia Lindhoud,
Mireille M. A. E. Claessens, Evan Spruijt
Science Advances (2022)