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

Dávid Szamosvári; Valentin F. Reichle; Monica Jureschi; Thomas Böttcher

doi:10.1039/c6cc06295d

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

Dávid Szamosvári
, Valentin F. Reichle
, Monica Jureschi
, Thomas Böttcher (Corresponding author)

Publications: Contribution to journal › Article › Peer Reviewed

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.

Original language	English
Pages (from-to)	13440-13443
Number of pages	4
Journal	Chemical Communications
Volume	52
Issue number	92
DOIs	https://doi.org/10.1039/c6cc06295d
Publication status	Published - 2016
Externally published	Yes

Austrian Fields of Science 2012

104004 Chemical biology

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10.1039/c6cc06295d

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title = "Synthetic quinolone signal analogues inhibiting the virulence factor elastase of Pseudomonas aeruginosa",

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.",

author = "D{\'a}vid Szamosv{\'a}ri and Reichle, \{Valentin F.\} and Monica Jureschi and Thomas B{\"o}ttcher",

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AU - Reichle, Valentin F.

AU - Jureschi, Monica

AU - Böttcher, Thomas

N1 - Publisher Copyright: © The Royal Society of Chemistry. Accession Number WOS:000388202900002 PubMed ID 27722551

PY - 2016

Y1 - 2016

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AB - 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.

UR - https://www.scopus.com/pages/publications/84994904755

U2 - 10.1039/c6cc06295d

DO - 10.1039/c6cc06295d

M3 - Article

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VL - 52

SP - 13440

EP - 13443

JO - Chemical Communications

JF - Chemical Communications

IS - 92

ER -

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

Abstract

Austrian Fields of Science 2012

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