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Mo-CBP3-PepI, Mo-CBP3-PepII, and Mo-CBP3-PepIII are synthetic antimicrobial peptides active against human pathogens

Jose T A Oliveira1, Pedro F N Souza2, Ilka M Vasconcelos1

  • 1Department of Biochemistry and Molecular Biology, Federal University of Ceara, Fortaleza, Ceara, 60451, Brazil.

Biochimie
|November 4, 2018
PubMed

Insights

New antimicrobial peptides (AMPs) were synthesized, inspired by a Moringa oleifera protein. Mo-CBP3-PepIII shows potent activity against Staphylococcus aureus and Candida species without harming human cells, suggesting potential for new treatments.

Area of Science:

  • Microbiology
  • Biochemistry
  • Drug Discovery

Background:

  • Declining efficacy of current antimicrobial drugs necessitates novel therapeutic agents.
  • Antimicrobial peptides (AMPs) are emerging as promising candidates due to their broad-spectrum activity.
  • Mo-CBP3, an antimicrobial protein from Moringa oleifera seeds, serves as inspiration for new peptide designs.

Purpose of the Study:

  • To design and synthesize novel antimicrobial peptides (AMPs) inspired by Mo-CBP3.
  • To evaluate the antimicrobial activity, cell penetration, and toxicity of the synthesized peptides.
  • To investigate the mechanism of action of the most potent peptide against key human pathogens.

Main Methods:

  • Design and synthesis of three AMPs: Mo-CBP3-PepI, Mo-CBP3-PepII, and Mo-CBP3-PepIII.
  • Antimicrobial susceptibility testing against Candida species and pathogenic bacteria.
  • Hemolysis and cytotoxicity assays using human cells.
  • Confocal microscopy for cell penetration studies.
  • Membrane permeabilization and reactive oxygen species (ROS) assays.
  • Bioinformatics analysis for enzyme resistance prediction.

Main Results:

  • All synthesized peptides inhibited microbial growth and penetrated microbial cells without exhibiting hemolytic or toxic effects on human cells.
  • Mo-CBP3-PepIII demonstrated the strongest antimicrobial activity against Staphylococcus aureus and Candida species.
  • Mo-CBP3-PepIII increased plasma membrane permeabilization in S. aureus and induced pore formation and ROS overproduction in Candida parapsilosis.
  • Bioinformatics analysis indicated Mo-CBP3-PepIII resistance to gastrointestinal proteolytic enzymes.

Conclusions:

  • Mo-CBP3-PepIII is a potent antimicrobial agent with a promising safety profile against human cells.
  • The peptide's mechanism involves disruption of microbial cell membranes and ROS induction.
  • Mo-CBP3-PepIII's resistance to enzymatic degradation suggests potential for oral administration, offering a novel therapeutic strategy.
Keywords:
AntimicrobialPathogenic bacteriaPathogenic yeastsSynthetic peptides

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