Tau-proteins form aggregates that are associated with neurodegenerative diseases such as Alzheimer's disease and dementia. The mechanisms by which tau protein spatially organizes into aggregates remain largely unknown. We use Molecular Dynamics (MD) simulations to model tau proteins in solution and we apply methods from topology to rigorously characterize their structure. Recent research suggests that the presence of RNA molecules may be driving aggregation. We use MD simulations of tau proteins and RNA molecules to examine the role of RNA on tau protein conformations and test this hypothesis. Our results reveal for the first time how protein self-entanglement and pairwise entanglement varies in the presence of RNA. Our methods can be used to provide a novel model of protein aggregation in the future.
Topological effects in Tau-protein aggregation
Masumi Sugiyama, University of Tennessee at Chattanooga
2022 AWM Research Symposium