Fig. 3: Stapled peptide 1907 displays greater binding to FAT helix 2–3 site as demonstrated by HSQC-NMR studies.

a Overlay of 2D HSQC spectra acquired with varying concentrations of 1907 and 100 μM FAT. Two-dimensional signals represented in magenta, green, purple, red, and blue were acquired in the presence of 100, 50, 10, 1, and 0 μM of 1907 respectively. Residues that were previously shown to have notable chemical shift perturbations in the presence of LD2 and have notable differences in integration between high and low concentrations of 1907, are indicated. b Molecular model (PDB ID: 1OW8²⁴) of the LD2 binding surfaces of FAT. Residues with a ¹H-¹⁵N HSQC peak volume decrease of more than 1 standard deviation upon incubation with 6 μM 1907 are highlighted in salmon. c Histogram of the residue-wise HSQC peak volume change, shown as percent relative to DMSO upon incubation of FAT with 6 μM 1907. Highlighted residues match those in panel (b). d Analysis and K_D estimation of 1907 binding at residues I936, K955, L959, and K1032 from the peak integration studies shown in Supplementary Fig. S6. Source data are provided as a Source data file.