Potent and Broad-Spectrum Antimicrobial Activity of Analogs from the Scorpion Peptide Stigmurin

Amorim-Carmo, Bruno, Daniele-Silva, Alessandra, Parente, Adriana M.S., Furtado, Allanny Alves, Carvalho, Enéas De, Oliveira, Johny W.F., Santos, Elizabeth Cristina Gomes, MS Silva, Silva, Sérgio R.B., Silva-Júnior, Arnóbio Antônio Da, Monteiro, Norberto K., Fernandes-Pedrosa, Matheus De Freitas

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17 Citations (Scopus)


Scorpion venom constitutes a rich source of biologically active compounds with high potential for therapeutic and biotechnological applications that can be used as prototypes for the design of new drugs. The aim of this study was to characterize the structural conformation, evaluate the antimicrobial activity, and gain insight into the possible action mechanism underlying it, for two new analog peptides of the scorpion peptide Stigmurin, named StigA25 and StigA31. The amino acid substitutions in the native sequence for lysine residues resulted in peptides with higher positive net charge and hydrophobicity, with an increase in the theoretical helical content. StigA25 and StigA31 showed the capacity to modify their structural conformation according to the environment, and were stable to pH and temperature variation-results similar to the native peptide. Both analog peptides demonstrated broad-spectrum antimicrobial activity in vitro, showing an effect superior to that of the native peptide, being non-hemolytic at the biologically active concentrations. Therefore, this study demonstrates the therapeutic potential of the analog peptides from Stigmurin and the promising approach of rational drug design based on scorpion venom peptide to obtain new anti-infective agents.
Original languageEnglish
Article number623
Pages (from-to)623-644
Number of pages21
JournalInternational Journal of Molecular Sciences
VolumeVol. 20
Issue numbern.º 3
Publication statusPublished - 31 Jan 2019


  • Tityus stigmurus
  • Analog peptides
  • Antimicrobial agents
  • Bacterial membrane
  • Molecular dynamics
  • Scorpion venom

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