Extending the Role of NAC Domain Hydrophobic Residues in αSynuclein: Implications for Seed-Competent Fibril Formation

Zenodo Dataset Description This dataset provides the raw experimental and computational data supporting the manuscript:"Extending the Role of NAC Domain Hydrophobic Residues in αSynuclein: Implications for Seed-Competent Fibril Formation" Each file is explicitly linked to the figure(s) it supports, ensuring traceability and reproducibility. Source Data Files Source Data File 1 (Figure 1):Raw thioflavin T (ThT) fluorescence kinetics data for NAC35, NAC16, and NAC11 peptides under neutral and variable pH conditions, as presented in Figure 1b, 1e–g. Source Data File 2 (Figure 2):UV-Vis absorbance data of soluble and insoluble fractions of NAC peptides to evaluate solubility differences, shown in Figure 2. Source Data File 3 (Figure 3):Aggregation kinetics of αSyn in the presence of preformed fibrils (NAC35, NAC16, NAC11, αSyn), corresponding to Figure 3a. Source Data File 4 (Figure 4):αSyn aggregation kinetics in the presence of inhibitor peptides (PD, PL, PB), corresponding to Figure 4c. Source Data File 5 (Figure 5):Biosensor cell seeding assay data including CFP/YFP inclusion counts and FRET-based seeding quantification for total and insoluble fractions, presented in Figure 5c–e. Source Data File 6 (Figure 6):Aggregation kinetics data for NAC35, NAC16, and NAC11 with and without inhibitors, as shown in Figure 6a-c. Source Data File 7 (Figure 8):MD simulation data on hydrogen bonding patterns in NAC-only vs. NAC+PB systems, corresponding to Figure 8. Source Data File 8 (Figure 9):Root mean square deviation (RMSD) and solvent-accessible surface area (SASA) profiles for NAC peptides in the presence and absence of PB inhibitor, supporting Figure 9a–b. Source Data File 9 (Figure 10):Residue-level contact frequency data between NAC peptides and PB over the simulation time course, shown in Figure 10a–c. Supplementary Source Files Source Data File S1 (Figure S2):UV-Vis analysis of NAC peptide fractions, presented in Figure S2. Source Data File S2 (Figure S3):Raman spectroscopy data confirming β-sheet formation in fibrillar NAC35, NAC16, and NAC11, as presented in Figure S3. Source Data File S3 (Figure S4):Control ThT fluorescence data for preformed fibrils used in seeded aggregation experiments, shown in Figure S4.