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CxxC Zinc Finger Protein Derived Peptide, MF18 Functions Against Biofilm Formation

Prabha Nagaram1, Mukesh Pasupuleti2, Jesu Arockiaraj3

  • 1Department of Microbiology, SRM Arts and Science College, Kattankulathur, Chennai, 603 203, India.

The Protein Journal
|July 5, 2020
PubMed

Insights

Biofilm infections pose a major threat due to antibiotic resistance. Researchers identified a novel antimicrobial peptide (AMP), MF18, derived from fish CxxC zinc finger protein, showing potent activity against resistant bacteria.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Pharmacology

Background:

  • Bacterial biofilm infections present a significant challenge in modern medicine, often exhibiting high tolerance to conventional antibiotics.
  • Antimicrobial peptides (AMPs) are emerging as promising alternatives to traditional antibiotics for combating drug-resistant bacterial infections.

Purpose of the Study:

  • To investigate the biological role and antimicrobial activity of a novel peptide, MF18, derived from a CxxC zinc finger protein.
  • To evaluate the efficacy of MF18 against biofilm-forming bacteria and assess its safety profile.

Main Methods:

  • In-silico analysis of a CxxC zinc finger protein from teleost fish to identify potential antimicrobial peptides.
  • Synthesis and characterization of the identified antimicrobial peptide MF18.
  • Antimicrobial activity testing against clinical isolates (Staphylococcus aureus, Escherichia coli) using Minimum Inhibitory Concentration (MIC) determination.
  • Mechanism of action studies using scanning electron microscopy to assess membrane permeabilization.
  • Toxicity assessment using MTT assay on RAW 264.7 cell lines and haemolytic assay on peripheral red blood cells.

Main Results:

  • The peptide MF18 demonstrated significant antimicrobial activity against biofilm-forming Staphylococcus aureus and Escherichia coli, with an MIC of 320 µM.
  • Scanning electron microscopy revealed that MF18 damages bacterial cell morphology, indicating membrane permeabilization as a mechanism of action.
  • MF18 exhibited no observable toxicity towards RAW 264.7 cells or peripheral red blood cells at effective concentrations.

Conclusions:

  • The CxxC zinc finger protein-derived peptide MF18 is a potent antimicrobial agent effective against key biofilm-forming bacteria.
  • MF18 demonstrates a favorable safety profile, suggesting its potential as a therapeutic agent in the pharmaceutical industry for treating resistant infections.
Keywords:
BiofilmCxxC zinc finger proteinMembrane permeabilizationScanning electron microscopyToxicity

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