STRUCTURAL EVALUATION AND ANALYSIS OF THE BIOLOGICAL ACTIVITIES OF STIGMURIN
ANALOGUE PEPTIDES IN THE Tityus stigmurus VENOM
Antimicrobial peptide; Antiparasitic activity; Antiproliferative activity; Circular dichroism.
Tityus stigmurus it’s the predominant scorpion specie in Northeast region from Brazil, it’s considered one of the main cause of scorpion accidents in this region. In T. stigmurus venom, which is a complex mixture of high and low molecular mass molecules, was identified an antimicrobial peptide denominated Stigmurin. Antimicrobial peptides are small molecules considered the first line of defense against microorganisms, they show broad spectrum action. Many authors have proved that these peptides can also be effective on cancerous cells. Mutation in these molecules sequence has been held aiming the increase in the activity maintaining its low toxicity. Therefore, it is proposed the characterization of the structure in silico and by circular dichroism, as well the antimicrobial, antiparasitic, anti-proliferative and hemolytic activities of two analog peptides from Stigmurin, denominated StigA3 and StigA4. We performed an in silico analysis for these peptides, where we were able to observe α-helix structure, which was confirmed by circular dichroism. We were also able to find that the analog peptides net charge and hydrophobic moment were higher than Sitgmurin’s, which can explain the increase in antimicrobial and antiparasitic activity. The peptides StigA3 e StigA4 showed activity on cancerous cells similiar to the native peptide, except when tested on a normal cell we were able to find that they’re less toxic. Therefore, these results indicate a potential biotechnological application for the analogs peptides, even as prototype to new therapeutic agents.