Figure 1

Figure 1

Predicted helical secondary and three-dimensional structures of MP06 anticancer peptide. (A) Two-dimensional drawing of the peptide using the PepDraw software (https://pepdraw.com, accessed on 12 April 2022) (B) The predicted three-dimensional secondary structure of MP06 from PEP-FOLD3. (C) Helical wheel plots of MP06 sequences showing amphipathicity quantified as hydrophobic moments. Shows hydrophilic residues as circles, hydrophobic residues as diamonds, and potentially positively/negatively charged as triangles/pentagons. The most hydrophobic residue is green, and the amount of green decreases proportionally to the hydrophobicity, with zero hydrophobicity coded as yellow. Hydrophilic residues are coded red, with pure red being the most hydrophilic (uncharged) residue and the amount of red decreasing proportionally to the hydrophilicity. The potentially charged residues are light blue. The arrow in the middle of the circle indicates the hydrophobic direction formed by amino acids with high hydrophobicity.