Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10596691 | Bioorganic & Medicinal Chemistry Letters | 2010 | 4 Pages |
Abstract
A docking-based virtual screening was used within the ligand binding sites of LuxR-type proteins to screen a chemical library of 2344 compounds. Biological evaluation of hit candidates on LuxR-dependent quorum sensing led to the discovery of six new inhibitors. Notably, calmidazolium (see picture) was identified as one of the most potent AHL-structurally unrelated LuxR inhibitors.
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Authors
Laurent Soulère, Mohamad Sabbah, Fanny Fontaine, Yves Queneau, Alain Doutheau,