Tau protein fibril (aggregated form) (None universally accepted)

Tau protein fibrils are insoluble, β-sheet-rich structures formed from the aggregation of intrinsically disordered tau protein, particularly in its hyperphosphorylated state. These aggregates disrupt normal neuronal function and structure, leading to neurotoxicity and cell death in Alzheimer's disease and related disorders. In healthy brains, tau maintains microtubule stability, but during disease, abnormal post-translational modifications, truncation, and environmental co-factors (like polyanions) drive tau to assemble into filaments and tangles. Aggregated tau exhibits prion-like behavior, propagating pathogenic conformations from cell to cell. Drug discovery efforts focus on preventing tau misfolding, interfering with aggregate formation, or promoting selective clearance of pathological assemblies[1][2][3][4][7][8][9].

Other names

Tau fibrilAggregated tau proteinAmyloid tau fibrilNeurofibrillary tangle (for higher-order tissue structures)

Direct binding to fibril and destabilization/disaggregation. Disruption of β-sheet stacking by charge repulsion and void formation (EGCG). Inhibition of aggregation by binding to repeat/hexapeptide motifs in tau.