Structural evaluation and in vivo antimicrobial activity of analogs peptides from Stigmurin of the Tityus stigmurus scorpion
Antimicrobial peptide; Scorpion; Tityus stigmurus; Structural evaluation; In vivo activity.
Antimicrobial peptides are molecules that are considered one of the firsts defense lines against microorganisms, they show broad microbicidal action against bacteria, fungi, virus, and parasites. In a study developed by our research group, where the transcriptome of the venom gland was analyzed, an antimicrobial peptide named Stigmurin was identified, from which two analog peptides denominated StigA6 and StigA16 were designed, changing amino acid residues for lysin, and studied. These peptides already presented higher activity against Gram-positive and Gram-negative bacteria and parasites in vitro than the native peptide, as well as a more potent activity against cancerous cells and less toxicity against normal cells than Stigmurin. Therefore, to deepen the study of these peptides we propose their structure evaluation when interacting with lipid vesicles and by nuclear magnetic resonance (NMR), their antibacterial activity in vitro and in vivo in larval infection and the sepsis polymicrobial model, as well as their leishmanicidal activity. At the study of their interaction with lipid vesicles both peptides showed higher interaction with vesicles that mimic the bacterial membrane than with vesicles that mimic eukaryotic membrane. At the NMR evaluation the peptides showed high amphipathic properties and helical structure. Regarding their in vitro antibacterial activity, they showed high activity against multi-resistant S. aureus and P. aeruginosa. In both in vivo antimicrobial models, the peptides were able to control the infection. Regarding their activity against the promastigote form of Leishmania braziliensis, both analog peptides showed greater activity than the native peptide. Therefore, these peptides are interesting targets in the study of new anti-infective molecules.