Fig. 1

Full-length Tau protein and diagrammatic representation of the experiment. a Full-length Tau protein (hTau40^WT) is a 45-kDa microtubule-binding axonal protein. The hTau40^WT has a flexible N- and C-terminal domain organization with which it plays a role in cargo transport and microtubule stabilization, respectively. N-terminal region contains two inserts, and C-terminal includes four repeat regions, which mediate microtubule interaction in physiological condition and also intermolecular interaction leading to oligomerization in AD condition. The two-hexapeptide motif (VQIINK and VQIVYK) in the repeat region plays a critical role in the initiation of Tau oligomerization. b Diagrammatic representation illustrates the workflow for oligomer preparation, where hTau40^WT was induced with heparin for oligomerization for 12 h. Then, the oligomers were separated by size-exclusion chromatography. Western blot, ThS, and ANS fluorescence were used to characterize the oligomers. The size of the oligomers was confirmed by transmission electron microscopy, and the oligomers were mapped by A11 oligomer-specific antibody