**1.1.2 Dermaseptins peptides**

These peptides were extracted from Phyllomedusa genus frog skin secretions. Some of them present a proline-induced kink in the middle of the alpha helix (Shin et al., 2001). Others have a glycine in the same relative position that has been suggested to give the flexibility needed for the membrane lysis activity (Xiao et al., 2006). This structural plasticity has been defined as a molecular determinant for the antimicrobial vs eucaryont membrane specificity (Shin et al., 1999; Shin et al., 2000; Shin et al., 2001), together with overall net positive charge and hydrophibic moment. They present hydrophobic and positively charged amino acid in an alternate pattern. Though mature dermaseptin amino acid sequences are highly variable, their acidic pro-peptides are strikingly conserved (Azevedo Calderon et al., 2010).
