Fig. 3: αS dynamics in electrostatic complex coacervates.
a–c FRAP analysis of αS dynamics (2% AF488-labeled αS) within electrostatic coacervates. Representative images of a triplicate αS/Tau441 FRAP assay are shown in (a), where the red circle indicates the bleached area. Scale bar is 5 μm. b Mean FRAP curves and (c) calculated diffusion coefficients (D) of 5–6 (N) different droplets from a triplicate experiment with 100 μM αS and equimolar concentrations of Tau441 (red) or ΔNt-Tau (blue) or tenfold concentration of pLK (green) under LLPS conditions. The standard deviations of the FRAP curves are shown as shaded colors. For comparison, the diffusion coefficient of αS in the dispersed phase was determined in triplicate by fluorescence correlation spectroscopy (FCS) (see Supplementary Fig. 3 and methods for more information). d CW X-Band EPR spectra of 100 μM TEMPOL-122-αS in LLPS buffer without any poly-cation (black) or in the presence of a 100 μM Tau441 (red) or ΔNt-Tau (blue), or 1 mM pLK (green). The inset shows a zoom into the high-field line, where the most significant changes occur. e Binding curves of 50 μM TEMPOL-122-αS to the different poly-cations in the absence of LLPS (no PEG). The decrease in amplitude of band III relative to Band II (IIII/III) of normalized EPR spectra are shown for increasing molar ratios of Tau441 (red), ΔNt-Tau (blue) and pLK (green). Colored lines show the fit to data using an approximate binding model with n-identical and independent binding sites for each curve. Source data are provided as a Source Data file.
