Fig. 7
From: Tau local structure shields an amyloid-forming motif and controls aggregation propensity
Enhancing β-hairpin structure rescues spontaneous aggregation phenotypes. a Cartoon schematic representation of the tryptophan zipper motif (green bar) and controls used to stabilize a β-hairpin structure in an R2R3-P301L peptide fragment (Supplementary Table 2). b Aggregation reactions of the tryptophan zipper peptide and controls measured by ThT fluorescence. The Trp-R2R3-P301L-Trp fragment peptide yielded no detectible ThT signal change (less than twofold ratio to background signal) over the course of the experiment (see Supplementary Data 1) ThT signals are shown as average of triplicates with standard deviation and were normalized to the maximum for each condition. c Schematic of proline and fluorinated proline analogs used to generate cis and trans proline conformers at the position corresponding to P301 (red circle) in peptide models. d ThT aggregation reactions of the cis, trans, and neutral proline analogs substituted into the R2R3 peptide fragment. ThT signals are an average of six independent experiments with standard deviation shown
