TABLE 1.
a Peptides are named with the substituted anchor residues.
b The pockets 1, 4, 6, and 9 anchor residues in wild type peptides (WT) and corresponding substituted anchor residues are highlighted in bold and underlined. W1N-me represented peptide with N-methylated tryptophan in pocket 1.
c 50% inhibition concentration calculated from binding competition curves.
d Intrinsic dissociation half-life calculated from the dissociation curves.
e DM-mediated dissociation half-life measured in the presence of 0.5 μm DM calculated from the dissociation curves.
f DM susceptibility, which was calculated as the specific increase in dissociation rate in the presence of DM (koff, DM − koff, in)/[DM], where [DM] = 0.5 μm.