Authors: TUĞBA DOĞAN, NAŞİT İĞCİ, AYŞENUR BİBER, SELİN GEREKCİ, HEPŞEN HAZAL HÜSNÜGİL, AFİFE İZBIRAK, CAN ÖZEN
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.
Keywords: Scorpion venom, peptide, peptidomics, antimicrobial effect, cytotoxicity, mass spectrometry
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