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Antibiotics 2017, 6(3), 13;

Antibacterial Activity and Toxicity of Analogs of Scorpion Venom IsCT Peptides

Department of Chemistry, Rhodes College, 2000 North Parkway, Memphis, TN 38112, USA
Author to whom correspondence should be addressed.
Academic Editor: Naresh Kumar
Received: 6 June 2017 / Revised: 19 June 2017 / Accepted: 26 June 2017 / Published: 28 June 2017
(This article belongs to the Special Issue Antibiotic Synthesis)
Full-Text   |   PDF [694 KB, uploaded 28 June 2017]   |  


Seven analogs of the natural, α-helix peptides IsCT1 and IsCT2—found in the venom of scorpion Opithancatus Madagascariensis—have been synthesized and tested to compare their antibacterial and hemolytic activity against natural peptides. In general, results show that increasing hydrophobicity by substituting positions 5 and 9 of the sequences with alanine, valine, and leucine, enhances antibacterial activity. However, this also increases hemolytic activity. The analog with an increased net positive charge from +1 to +3 produces moderate bacterial growth inhibition but also has high hemolytic activity. On the other hand, the analog with a negative net charge (−1) has low antibacterial properties but also no cytotoxicity under the tested conditions, a similar result was found for five of the seven studied analogs. View Full-Text
Keywords: antimicrobial peptides; α-Helix; amphipathic; hemolysis antimicrobial peptides; α-Helix; amphipathic; hemolysis

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de la Salud Bea, R.; Petraglia, A.F.; Ascuitto, M.R.; Buck, Q.M. Antibacterial Activity and Toxicity of Analogs of Scorpion Venom IsCT Peptides. Antibiotics 2017, 6, 13.

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