Aggregation-state–resolved analysis of the tau interactome in Alzheimer’s disease

ABSTRACT: This project investigates how tau-associated protein networks are remodelled in Alzheimer’s disease and how these changes relate to the progression of tau aggregation in the human brain. Using post-mortem brain tissue from individuals with Alzheimer’s disease and age-matched healthy controls, the study integrates quantitative proteomics with single-molecule approaches to characterise tau species and their associated protein interactions across aggregation states. Tau-containing complexes were isolated using a panel of antibodies recognising different tau conformational and phosphorylation states, enabling comparison of tau-associated protein profiles from soluble to more aggregated forms. Single-molecule imaging and pull-down assays were used alongside proteomic analyses to directly visualise tau aggregates and validate interaction patterns at the level of individual assemblies. In parallel, total brain proteomes were analysed to provide context for disease-associated changes. Overall, this dataset supports a multi-scale analysis of tau pathology in human brain tissue, linking single-aggregate measurements with proteome-wide changes, and provides a resource for studying dynamic remodelling of the tau interactome in disease.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Brain

DISEASE(S): Alzheimer's Disease

SUBMITTER: Dorothea Boeken  

LAB HEAD: David Klenerman

PROVIDER: PXD072117 | Pride | 2026-09-28

REPOSITORIES: Pride