Fig. 1 Amyloidogenic properties of NKB. A. Predicted aggregation propensity (using TANGO) of NKB(WT) and the mutants investigated in this study. B. Time-resolved ThT fluorescence of NKB(WT) and mutants NKB(F6W), NKB(F5W) and NKB(F5,6W) shows that mutations in the diphenylalanine motif severely disrupt the ability of the peptide to form fibrils. C. Time-resolved ThT fluorescence of NKB(+A6) which inserts an alanine within the diphenylalanine motif shows limited fibril formation. D. Time-resolved ThT fluorescence of the zebrafish NKB (zf-NKB) shows some fibril formation, but much less compared to mammalian wild-type NKB. All peptides were 200 μM in 10 mM nEM, pH 7.4.
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