Curcumin possesses a great deal of

Curcumin possesses a great deal of structural similarity with AHLs. Curcumin possesses aromatic ring systems, which are phenols and are connected by two α, β-unsaturated carbonyl groups. The diketones form stable enols. The phenolic moiety of curcumin mimics lactone moiety of AHL. The ketone group in curcumin is identical to the one found in AHLs. Further, curcumin is reported to have antibacterial properties [26, 27]. With all these traits, curcumin was used for its evaluation as QSI molecule with in silico and in vitro studies. Packiavathy et al. [27] showed curcumin to effectively inhibit the QS in P. aeruginosa and have reported curcumin to reduce in the biofilm formation along with other QS-derived traits. However, in silico study supporting this claim is rare. Binding of curcumin with LasR of Pseudomonas is a preliminary step. As we are also studying the interaction of curcumin with LuxR, it is prudent to compare the similarity of LuxR and LasR. The superimposition of LuxR and LasR revealed that despite both proteins being structurally different, possessed the same ligand-binding cleft that comprised five-stranded antiparallel β-sheet packed against three α-helices on each side as represented in Fig. 1