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Antibacterial Activity and Toxicity of Analogs of Scorpion Venom IsCT Peptides.

ABSTRACT: 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.

SUBMITTER: de la Salud Bea R

PROVIDER: S-EPMC5617977 | biostudies-literature | 2017 Jun

REPOSITORIES: biostudies-literature

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Antibacterial Activity and Toxicity of Analogs of Scorpion Venom IsCT Peptides.

de la Salud Bea Roberto R Petraglia Adam F AF Ascuitto Michael R MR Buck Quentin M QM

Antibiotics (Basel, Switzerland) 20170628 3

Seven analogs of the natural, α-helix peptides IsCT1 and IsCT2-found in the venom of scorpion <i>Opithancatus Madagascariensis</i>-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 ...[more]

PMID: 28657596

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