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 (http://aps.unmc.edu/AP).
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.
Keywords: Anticancer peptides, anti-HIV peptides, antimalarial peptides, antimicrobial peptides, bioinformatics, scorpions,
spiders, structural biology.
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