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Related Experiment Video

Updated: Feb 13, 2026

Capture Compound Mass Spectrometry - A Powerful Tool to Identify Novel c-di-GMP Effector Proteins
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Functionalized Proline-Rich Peptides Bind the Bacterial Second Messenger c-di-GMP.

Carlotta Foletti1, Rolf A Kramer1, Harald Mauser2

  • 1Laboratorium für Organische Chemie, D-CHAB, ETH Zürich, Vladimir-Prelog-Weg 3, 8093, Zürich, Switzerland.

Angewandte Chemie (International Ed. in English)
|March 10, 2018
PubMed
Summary

Researchers identified a peptide that binds to cyclic di-GMP (c-di-GMP), a molecule crucial for bacterial infections. This peptide effectively inhibits biofilm formation in Pseudomonas aeruginosa, offering a potential new strategy against bacterial pathogens.

Keywords:
antimicrobial compoundsbiofilmsc-di-GMPinhibitorspeptides

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Establishment of a High-throughput Setup for Screening Small Molecules That Modulate c-di-GMP Signaling in Pseudomonas aeruginosa
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Related Experiment Videos

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Establishment of a High-throughput Setup for Screening Small Molecules That Modulate c-di-GMP Signaling in Pseudomonas aeruginosa
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Peptide-based Identification of Functional Motifs and their Binding Partners
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Peptide-based Identification of Functional Motifs and their Binding Partners

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Area of Science:

  • Microbiology
  • Biochemistry
  • Drug Discovery

Background:

  • Cyclic di-GMP (c-di-GMP) is a vital second messenger regulating bacterial pathogenesis, including biofilm formation and virulence.
  • Targeting c-di-GMP is a promising strategy for combating bacterial infections.

Purpose of the Study:

  • To identify novel molecules that bind to c-di-GMP.
  • To investigate the potential of these molecules as inhibitors of bacterial biofilm formation.

Main Methods:

  • Screening of a combinatorial peptide library to identify c-di-GMP binding peptides.
  • Computational and Circular Dichroism (CD) spectroscopic studies to elucidate binding modes.
  • Biological assays to evaluate the efficacy of identified peptides against bacterial biofilm growth.

Main Results:

  • Identification of a proline-rich tetrapeptide (Gup-Gup-Nap-Arg) with selective binding to c-di-GMP in aqueous solution.
  • Elucidation of a potential binding mode and design of a higher-affinity pentapeptide.
  • Demonstration that the tetrapeptide inhibits biofilm formation in the opportunistic pathogen *Pseudomonas aeruginosa*.

Conclusions:

  • Peptide-based molecules can effectively target c-di-GMP.
  • The identified tetrapeptide is a promising lead compound for developing new anti-biofilm agents.
  • This approach offers a novel strategy to combat bacterial infections by disrupting essential cellular processes.