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Production and Testing of Antimicrobial Peptides and Their Mimics
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A novel chimeric peptide with antimicrobial activity.

Begum Alaybeyoglu1, Berna Sariyar Akbulut, Elif Ozkirimli

  • 1Chemical Engineering Department, Bogazici University, Bebek, 34342, Istanbul, Turkey.

Journal of Peptide Science : an Official Publication of the European Peptide Society
|January 20, 2015
PubMed
Summary

Modified antimicrobial peptides show promise in combating bacterial drug resistance by inhibiting beta-lactamase. Adding hydrophobic residues enhances cellular uptake and antimicrobial activity against resistant bacteria.

Keywords:
antibiotic resistanceantimicrobial peptidebeta-lactamasecell-penetrating peptidedelivery

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Area of Science:

  • Biochemistry
  • Microbiology
  • Drug Discovery

Background:

  • Bacterial drug resistance, particularly beta-lactamase-mediated resistance, poses a significant threat to infectious disease treatment.
  • Antimicrobial peptides (AMPs) are emerging as potential broad-spectrum alternatives to conventional antibiotics due to evolving resistance.
  • Peptides derived from the beta-lactamase inhibitory protein (BLIP) have demonstrated beta-lactamase inhibitory capabilities.

Purpose of the Study:

  • To engineer a BLIP-derived peptide for enhanced beta-lactamase inhibition and improved cellular uptake.
  • To investigate the antimicrobial activity of the modified peptide against beta-lactam-resistant bacterial strains.
  • To elucidate the molecular mechanism of peptide translocation across cell membranes.

Main Methods:

  • Peptide design incorporating hydrophobic N-terminal residues (LLIIL) based on cell-penetrating sequences.
  • Enzyme kinetics assays to determine the inhibitory constant (Ki) of the modified peptide against beta-lactamase.
  • Cell-based assays to evaluate antimicrobial activity against resistant and non-resistant bacterial strains.
  • Steered molecular dynamics simulations to explore the peptide's membrane interaction mechanism.

Main Results:

  • The modified peptide competitively inhibited beta-lactamase with a Ki value of 58 μM.
  • Incubation with the peptide reduced the viability of beta-lactam-resistant cells but not beta-lactamase-free cells.
  • Molecular dynamics simulations suggested a mechanism for enhanced membrane translocation due to N-terminal hydrophobic residues.

Conclusions:

  • Modification of BLIP-derived peptides with N-terminal hydrophobic residues is a viable strategy for enhancing antimicrobial activity.
  • These modified peptides demonstrate potential as novel therapeutic agents against beta-lactamase-producing bacteria.
  • The findings support the development of AMPs targeting not only beta-lactamase but also other intracellular bacterial targets.