Abstract
Protoiurus kraepelini is a scorpion species found in parts of Turkey and Greece. In this study, the peptide profile of its venom was determined for the first time. The electrophoretic profile of the crude venom showed a protein distribution from 2 to 130 kDa. MALDI-TOF MS analysis of the venom peptide fraction yielded 27 peptides between 1059 and 4623 Da in mass. Several ion channelblocking and antimicrobial peptides were identified by peptide mass fingerprinting analysis. Cytotoxic and antimicrobial effects of the venom were also demonstrated on Jurkat cells and Escherichia coli, respectively. As the first peptidomic characterization study on P. kraepelini venom, this report lays the foundation for detailed future studies that may lead to the discovery of novel bioactive peptides.
Highlights
A wide variety of species have been producing toxins over millions of years in order to capture prey or as a defense mechanism
Protein content and electrophoretic profile of the venom The amount of protein based on dry weight of the crude venom was found to be 70% (w/w) by Bradford protein assay
The peptide fraction was further fractionated by RP-HPLC and five peak sets were pooled separately for bioactivity assays
Summary
A wide variety of species have been producing toxins over millions of years in order to capture prey or as a defense mechanism Some of these active compounds have been used in the development of new drugs for the treatment of various diseases (Harvey, 1995; Clardy and Walsh, 2004; Newman and Cragg, 2007). Such pharmacologically active biomolecules show their biological activity by inducing or inhibiting apoptosis and angiogenesis, inhibiting protein synthesis, or displaying antimicrobial effects. Venoms are composed mostly of proteins and peptides, encompassing a large variety of Olivera, 2006; Newman and Cragg, 2007)
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