Jump to main content
Jump to site search

Issue 92, 2016
Previous Article Next Article

Synthetic quinolone signal analogues inhibiting the virulence factor elastase of Pseudomonas aeruginosa

Author affiliations

Abstract

We explore the chemical space of Pseudomonas quinolone signal analogs as privileged structures and report the discovery of a thioquinolone as a potent inhibitor of the important virulence factor elastase of the human pathogen Pseudomonas aeruginosa. We provide evidence that the derivative binds to the active site zinc of elastase and additionally acts as a fluorescent zinc sensor.

Graphical abstract: Synthetic quinolone signal analogues inhibiting the virulence factor elastase of Pseudomonas aeruginosa

Back to tab navigation

Supplementary files

Publication details

The article was received on 29 Jul 2016, accepted on 23 Sep 2016 and first published on 26 Sep 2016


Article type: Communication
DOI: 10.1039/C6CC06295D
Citation: Chem. Commun., 2016,52, 13440-13443
  • Open access: Creative Commons BY license
  •   Request permissions

    Synthetic quinolone signal analogues inhibiting the virulence factor elastase of Pseudomonas aeruginosa

    D. Szamosvári, V. F. Reichle, M. Jureschi and T. Böttcher, Chem. Commun., 2016, 52, 13440
    DOI: 10.1039/C6CC06295D

    This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. Material from this article can be used in other publications provided that the correct acknowledgement is given with the reproduced material.

    Reproduced material should be attributed as follows:

    • For reproduction of material from NJC:
      [Original citation] - Published by The Royal Society of Chemistry (RSC) on behalf of the Centre National de la Recherche Scientifique (CNRS) and the RSC.
    • For reproduction of material from PCCP:
      [Original citation] - Published by the PCCP Owner Societies.
    • For reproduction of material from PPS:
      [Original citation] - Published by The Royal Society of Chemistry (RSC) on behalf of the European Society for Photobiology, the European Photochemistry Association, and RSC.
    • For reproduction of material from all other RSC journals:
      [Original citation] - Published by The Royal Society of Chemistry.

    Information about reproducing material from RSC articles with different licences is available on our Permission Requests page.

Search articles by author

Spotlight

Advertisements