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Novel designed VmCT1 analogs with increased antimicrobial activity.

Cibele Nicolaski Pedron1, Marcelo Der Torossian Torres1, Julia Aparecida da Silva Lima1

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Antimicrobial peptides from scorpion venom were modified to enhance antibacterial activity. Introducing a lysine residue boosted antimicrobial power but increased red blood cell lysis; other substitutions fine-tuned activity and reduced toxicity.

Keywords:
Antimicrobial peptidesScorpion venomStructure-activity relationshipVmCT1

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Area of Science:

  • Biochemistry and Molecular Biology
  • Immunology
  • Medicinal Chemistry

Background:

  • Antimicrobial peptides (AMPs) are crucial for innate immunity, exhibiting broad-spectrum antimicrobial activity.
  • VmCT1, a cationic peptide from scorpion venom, shows antibacterial properties and a tendency for helical structures.
  • AMPs are of significant interest for developing new antimicrobial agents.

Purpose of the Study:

  • To synthesize and characterize analogs of the VmCT1 peptide.
  • To investigate the impact of single and double substitutions on antimicrobial and hemolytic activities.
  • To understand the structure-activity relationships of VmCT1 analogs.

Main Methods:

  • Peptide synthesis and characterization.
  • Antimicrobial activity assays against bacteria, yeast, and fungi.
  • Hemolytic activity assays using human erythrocytes.
  • Conformational studies using circular dichroism spectroscopy.

Main Results:

  • Lysine substitution ([K]11-VmCT1-NH2) enhanced antimicrobial activity (MICs 0.39–6.25 μmol L−1) but increased hemolytic activity.
  • Other Lysine analogs showed reduced MICs (0.39–25 μmol L−1).
  • Circular dichroism indicated helical structures in TFE/vesicles and coiled structures in water for Lysine analogs.
  • Glutamic acid substitution ([E]4-VmCT1-NH2) reduced hemolytic activity (MHC = 25 μmol L−1).
  • Tryptophan substitutions ([W]9-VmCT1-NH2 and [E]4[W]9-VmCT1-NH2) favored hydrophobic interactions, with [W]9-VmCT1-NH2 showing comparable or lower MICs.

Conclusions:

  • Physicochemical modifications significantly influence the antimicrobial and hemolytic activities of VmCT1 analogs.
  • Charge and hydrophobicity are key parameters in designing potent and safe antimicrobial peptides.
  • Structure-activity relationship studies provide insights for developing novel therapeutic agents based on AMPs.