Figure 4: Conformational properties of antileishmanial active antimicrobial peptides. The most representative structures for peptide backbones were analyzed regarding their 3D structure. A) bombinin (α–helical of approximately 4.5 turns), B) dermaseptin S1 (α–helical of approximately 3 turns), C) mastoparan (α–helical of approximately 3.5 turns), and D) tachyplesin (antiparallel β–strand). Red ribbons represent α–helixes and green arrows β–strands. Side-chain hydrogens were omitted in this analysis and peptide backbones are N to C orientated.