Insights into Antimicrobial Peptides from Spiders and Scorpions

Protein Pept Lett. 2016;23(8):707-21. doi: 10.2174/0929866523666160511151320.


The venoms of spiders and scorpions contain a variety of chemical compounds. Antimicrobial peptides (AMPs) from these organisms were first discovered in the 1990s. As of May 2015, there were 42 spider's and 63 scorpion's AMPs in the Antimicrobial Peptide Database ( These peptides have demonstrated broad or narrow-spectrum activities against bacteria, fungi, viruses, and parasites. In addition, they can be toxic to cancer cells, insects and erythrocytes. To provide insight into such an activity spectrum, this article discusses the discovery, classification, structure and activity relationships, bioinformatics analysis, and potential applications of spider and scorpion AMPs. Our analysis reveals that, in the case of linear peptides, spiders use both glycine-rich and helical peptide models for defense, whereas scorpions use two distinct helical peptide models with different amino acid compositions to exert the observed antimicrobial activities and hemolytic toxicity. Our structural bioinformatics study improves the knowledge in the field and can be used to design more selective peptides to combat tumors, parasites, and viruses.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Anti-Infective Agents / chemistry*
  • Anti-Infective Agents / pharmacology
  • Antimicrobial Cationic Peptides / chemistry*
  • Antimicrobial Cationic Peptides / pharmacology*
  • Antineoplastic Agents / chemistry
  • Antineoplastic Agents / pharmacology
  • Computational Biology / methods
  • Models, Molecular
  • Scorpion Venoms / chemistry
  • Scorpions / metabolism*
  • Spider Venoms / chemistry
  • Spiders / metabolism*
  • Structure-Activity Relationship


  • Anti-Infective Agents
  • Antimicrobial Cationic Peptides
  • Antineoplastic Agents
  • Scorpion Venoms
  • Spider Venoms