Heterotypic aggregation of Aβ42 with disease-relevant proteins in Alzheimer’s disease

It is still unclear why amyloid aggregation is toxic in neurodegenerative diseases. Previously, I showed that proteins with sequence segments homologous to Aβ aggregation-prone regions can affect Aβ aggregation and modify fibril morphology, a mechanism that could help explain regional vulnerability to protein aggregation. Here, I will study this co-aggregation and co-deposition mechanism in a more disease-relevant cellular model that also considers the contribution of microglia to plaque formation, with a focus on proteins that are disease-relevant because of their function, and tissue- and cell-specific expression patterns. This research will dive deeper into heterotypic aggregation and will unravel important aspects of Aβ toxicity by mapping sequence-specific interactions between disease amyloids and the brain proteome.

Keywords:heterotypic aggregation, Alzheimer's disease, amyloid beta

Disciplines:Molecular and cell biology not elsewhere classified, Neurosciences not elsewhere classified, Neurological and neuromuscular diseases, Proteins