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The acpP-targeting antisense PNA CTCATACTCT, particularly when linked to the cell wall/membrane-active peptide KFFKFFKFFK, demonstrated a remarkable increase in antisense efficacy in E. coli, up to a hundredfold, while maintaining their target specificity.

The Peptide-PNA Conjugate represents a novel class of antimicrobial agents designed to combat multidrug-resistant (MDR) bacteria. This conjugate combines the unique properties of peptide nucleic acids (PNAs) with a specialized peptide sequence to enhance bacterial uptake and antisense activity.

Key Features:

  1. Structure and Composition: The conjugate consists of a linear, cationic peptide sequence (KFFKFFKFFK) covalently attached to a PNA oligomer with the sequence {CTCATACTCT}-NH2. This design leverages the envelope-disrupting properties of cationic bacteria penetrating peptides (BPPs).

  2. Targeted Action Against MDR Bacteria: Specifically formulated to address the growing concern of antibiotic resistance, particularly in Gram-negative bacteria, which are resistant to many antibiotic classes.

  3. Enhanced Bacterial Uptake: The cationic peptide component (KFFKFFKFFK) facilitates the translocation of the PNA across bacterial membranes, including the challenging multibarrier envelopes with lipopolysaccharide (LPS) layers.

  4. Antisense Mechanism: The PNA component targets essential bacterial genes, capable of killing bacteria at low micromolar concentrations, offering a new avenue for antibiotic drug discovery.

  5. SbmA Independent Activity: The conjugate's design allows for efficient crossing of the inner bacterial membrane without reliance on the SbmA transporter, overcoming a common resistance mechanism.

  6. Stability and Metabolism Considerations: The peptide-PNA conjugate is designed with stability in mind, considering the susceptibility to degradation by bacterial proteases/peptidases.


  • Antibacterial Research: Ideal for studies focused on novel antibacterial agents, particularly against MDR bacteria.
  • Drug Discovery: A promising candidate for the development of new antibiotics leveraging antisense technology.
  • Mechanistic Studies: Useful in exploring the uptake processes and mode of action of antisense antibacterials.


  • High Efficacy: Demonstrates potent antibacterial activity at low concentrations.
  • Reduced Resistance Risk: Designed to circumvent common bacterial resistance mechanisms.
  • Target Specificity: The PNA component allows for precise targeting of bacterial genes.


  • Peptide Stability: The intact bacteria penetrating peptides (BPPs) are crucial for uptake but not for antisense activity, highlighting the importance of peptide stability in the bacterial environment.
  • Mechanism of Action: Understanding the uptake and degradation processes is key to maximizing the efficacy of this conjugate.

The Peptide-PNA Conjugate (KFFKFFKFFK-{CTCATACTCT}-NH2) represents a cutting-edge approach in the fight against multidrug-resistant bacteria, offering a novel mechanism of action and enhanced efficacy. Its design and functionality make it a valuable tool for researchers and pharmaceutical developers aiming to address the critical challenge of antibiotic resistance.


1. Niloofar Yavari, Lise Goltermann, and Peter E. Nielsen ACS Chemical Biology 2021 16 (3), 471-479 DOI: 10.1021/acschembio.0c00822

2. Good, L., Awasthi, S., Dryselius, R. et al. Bactericidal antisense effects of peptide–PNA conjugates. Nat Biotechnol 19, 360–364 (2001). https://doi.org/10.1038/86753

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