Fig. 4: Molecular modeling suggests that substitution of A14 and A17 with phenylalanine can increase binding affinity to Mdm2.
From: Design-rules for stapled peptides with in vivo activity and their application to Mdm2/X antagonists
a A helical wheel representation of MP-040 sequence with introduced Phe (F14 and F17) residues highlighted with an asterisk. Black circles represent positions with apolar residues whereas those with blue circles are negatively charged positions and those with green circles are uncharged polar positions. Stapling residues are indicated with an X. b Structural representation of MD snapshot of MP-040 / Mdm2 complex. Mdm2 is shown as surface (grey) and bound peptide (green) is shown as cartoon with interacting residues and the two Phe residues (magenta) highlighted in sticks. The hydrocarbon linker is highlighted in salmon.
