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Kaushik Nath Bhaumik1, Anasztázia Hetényi1, Gábor Olajos1

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New antimicrobial foldamers, PGLb1 and PGLb2, combat antibiotic resistance by hyperpolarizing bacterial membranes. These compounds potentiate existing antibiotics against multi-drug resistant bacteria.

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Area of Science:

  • Microbiology
  • Biophysics
  • Drug Discovery

Background:

  • Bacterial membrane potential is critical for cellular functions.
  • Antimicrobial peptides like PGLa offer insights into membrane-targeting strategies.
  • Antibiotic resistance necessitates novel therapeutic approaches.

Purpose of the Study:

  • To design and synthesize novel antimicrobial foldamers inspired by PGLa.
  • To investigate the effect of these foldamers on bacterial membrane potential.
  • To evaluate their efficacy in overcoming antibiotic resistance.

Main Methods:

  • Computer-guided design of PGLa analogues (foldamers).
  • Assessment of membrane hyperpolarization effects.
  • Testing PGLb1 and PGLb2 as adjuvants with antibiotics against clinical isolates of multi-drug resistant bacteria (Escherichia coli, Klebsiella pneumoniae, Shigella flexneri).
  • Analysis of ion transport mechanisms and membrane potential changes.

Main Results:

  • Novel PGLa analogues (PGLb1, PGLb2) were successfully developed.
  • These compounds induce sustained hyperpolarization of bacterial membranes.
  • PGLb1 and PGLb2 significantly reduced antibiotic resistance in multi-drug resistant clinical isolates.
  • The mechanism involves selective ionophore activity, enhancing the Goldman-Hodgkin-Katz potential.

Conclusions:

  • Manipulating bacterial membrane electrophysiology is a promising strategy against antibiotic resistance.
  • PGLa-inspired foldamers can potentiate existing antibiotics by altering membrane potential.
  • This approach offers a new avenue for combating infections caused by multi-drug resistant pathogens.