Fig. 2: Complex electrostatic coacervation of αS with Tau.

a Confocal (CF) microscopy images of αS/Tau441 coacervates in LLPS buffer (10 μM each protein, 0.5 μM AF488-labeled αS and Atto647N-labeled Tau441). b Representative differential interference contrast (DIC) microscopy image of an αS/Tau441 droplet fusion event (10 μM each protein). c Light scattering-based (at 350 nm) phase diagram of Tau441 LLPS (0–15 μM) in the absence (left) or the presence (right) of 50 μM αS. Warmer colors indicate more scattering. d Light scattering of αS/Tau441 LLPS samples with increasing concentrations of αS (Tau441 at 5 μM, N = 2–3 sample replicas, as indicated). e Schematic of some of the Tau protein variants used in this study and the different protein regions: the negatively charged N-terminal domain (in red), the proline-rich region (in blue), the microtubule-binding domain (MTBD, in orange) and the amyloid-forming paired helical filament (PHF) region located within the MTBD (in gray). The net charge per residue (NCPR) diagram of Tau441 is shown. f WF microscopy images of αS or ΔC_t-αS coacervation in LLPS buffer with ΔN_t-Tau (top, 10 μM each protein) or K18 (bottom, 50 μM each protein), using 1 μM AF488-labeled αS and Atto647N-labeled ΔN_t-Tau or K18. The scale bar in one image is indicative of the scale for all the images in the same panel (20 μm for panels a, b and f). Source data of panels c and d are provided as a Source Data file.