Amino acid substitutions in an alpha-helical antimicrobial arachnid peptide affect its chemical properties and biological activity towards pathogenic bacteria but improves its therapeutic index

摘要: Four variants of the highly hemolytic antimicrobial peptide Pin2 were chemically synthesized with aim to investigate role proline residue in this peptide, by replacing it motif glycine-valine-glycine [GVG], which was found confer low activity a spider peptide. The position 14 substituted [V], [GV], [VG] and [GVG]. Only variant for [GVG] less compared that all other variants. kept its Muller–Hilton agar diffusion assays, whereas three effective. However, variants, active when challenged against Gram-positive bacteria broth assays suggesting chemical properties peptides such as hydrophobicity is an important indication semi-solid environments.