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Updated: Jul 14, 2026

Synthesis and Assay of Vibrio Quorum Sensing Inhibitors
Published on: May 31, 2024
Exploring the active site of acyl homoserine lactones-dependent transcriptional regulators with bacterial quorum
Laurent Soulère1, Marine Frezza, Yves Queneau
1ICBMS, Institut de Chimie et Biochimie Moléculaires et Supramoléculaires, université de Lyon, université Lyon 1, CNRS, UMR5246, Lyon F-69622, France.
Abstract:
A comparative molecular modelling study of acyl homoserine lactones-dependent transcriptional regulators (TraR, SdiA, LuxR and LasR) involved in bacterial quorum sensing (QS) revealed a high structural homology of their active site. Docking studies within the active site of TraR of fixed conformations obtained using molecular mechanics calculations showed that TraR, for which the crystalline structure is known, is a relevant model for the study of other protein-ligand interactions in the same protein family. Structure-activity relationships of AHLs derived QS modulators including carboxamides, sulfonamides and ureas were thus investigated. The results show that Tyr61, a residue conserved in the LuxR-proteins family, is involved in attractive interactions with aromatic carboxamide antagonists. Tyr53, Tyr61 and Asp70, conserved residues, are implicated in both the development of additional hydrogen bonds and attractive interactions with the N-sulfonyl homoserine lactones and AHLs derived ureas antagonists.
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