Fig. 1
From: Rational design of synthetic antimicrobial peptides based on the Escherichia coli ShoB toxin
Initial strategy to improve solubility of the ShoB peptide. (a) Overview of the amino acid sequence of the native ShoB peptide versus the initially modified peptide 1a. Color code: yellow, hydrophobic; purple, threonine (T); grey, small residues (glycine (G) and alanine (A)); red, acidic; pink, glutamine (Q); blue, lysine (K) and arginine (R). (b) Helical-wheel diagrams (made by Heliquest https://heliquest.ipmc.cnrs.fr/cgi-bin/ComputParamsV2.py) of the native ShoB peptide divided into residues 1–18 (left panel) and 9–26 (right panel). Arrows represent direction and magnitude of the hydrophobic moment. Residues marked C and N (in red) are the C-terminal and N-terminal residues, respectively. Color coding as described above for panel (a). (c) Helical-wheel diagrams of peptide 1a divided into residues 1–18 (left panel) and 9–26 (right panel). Arrows represent direction and magnitude of the hydrophobic moment. Residues marked C and N are C-terminal and N-terminal residues of the peptide helix, respectively.
