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Discovery of potent 1,1-diarylthiogalactoside glycomimetic inhibitors of Pseudomonas aeruginosa LecA with antibiofilm properties

  • Alexandre Bruneau
  • , Emilie Gillon
  • , Aurélie Furiga
  • , Etienne Brachet
  • , Mouad Alami
  • , Christine Roques
  • , Annabelle Varrot
  • , Anne Imberty
  • , Samir Messaoudi
  • CNRS
  • Université Paris-Saclay
  • UPR 5301 CNRS
  • LCG
  • Université Paul Sabatier

Research output: Contribution to journal › Article › peer-review

9 Citations (Scopus)

Abstract

In this work, β-thiogalactoside mimetics bearing 1,1-diarylmethylene or benzophenone aglycons have been prepared and assayed for their affinity towards LecA, a lectin and virulence factor from Pseudomonas aeruginosa involved in bacterial adhesion and biofilm formation. The hit compound presents higher efficiency than previously described monovalent inhibitors and the crystal structure confirmed the occurrence of additional contacts between the aglycone and the protein surface. The highest affinity (160 nM) was obtained for a divalent ligand containing two galactosides. The monovalent high affinity compound (Kd = 1 μM) obtained through structure-activity relationship (SAR) showed efficient antibiofilm activity with no associated bactericidal activity.

Original languageEnglish
Article number115025
JournalEuropean Journal of Medicinal Chemistry
Volume247
DOIs
Publication statusPublished - 5 Feb 2023
Externally publishedYes

Keywords

  • Antibiofilm activity
  • Pseudomonas aeruginosa
  • Structure-activity relationship
  • Thiogalactoside

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