• Journal of Korean Society of Environmental Engineers
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• v.34 no.12
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• pp.828-834
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• 2012

The ecotoxicity detection device for preliminary test (Test jig) was manufactured to develop the biological early warning system using Vibrio fischeri. In this study, the ecotoxicity detection charateristics of the Test jig was investigated for 6 heavy metals (Cr, Zn, Pb, Cd, Cu and Hg). It was observed that relative luminescence unit (RLU) of Vibrio fischeri constantly decreased by the concentrations of the tested heavy metals. In contrast with other heavy metals, RLUs of Pb and Hg constantly decreased even at low concentrations. RLU of Hg drastically decreased when its concentration increased from 0.13 mg/L to 0.25 mg/L. $EC_{50}$ values of Cr, Zn, Pb and Cd gradually decreased with exposure time, whereas there was no significant change in $EC_{50}$ values of Cu and Hg with time. On the other hand, $EC_{50}$ values between the Test jig and Reference device were compared to evaluate the ecotoxicity detection performance of the Test jig. No big difference was found in $EC_{50}$ vlaues between the two devices, indicating that the Test jig could be applied as the ecotoxicity detection device for heavy metals.

• Microbiology and Biotechnology Letters
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• v.37 no.3
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• pp.248-257
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• 2009

The inhibitors against Vibrio harveyi quorum sensing (QS) signaling were developed by modifying the molecular structure of the major signal, N-3-hydroxybutanoyl-L-homoserine lactone (3-OH-$C_4$-HSL). A series of structural derivatives, N-(3-hydroxysulfonyl)-L-homoserine lactones (HSHLs) were synthesized by the solid-phase organic synthesis method. The in vivo QS inhibition by these compounds was measured by a bioassay system using the V. harveyi bioluminescence, and all showed significant inhibitory effects. To analyze the interaction between these compounds and LuxN, a 3-OH-$C_4$-HSL receptor protein of V. harveyi, we tentatively determined the putative signal binding domain of LuxN based on the sequence homology with other acyl-HSL binding proteins, and predicted the partial 3-D structure of the putative signal binding domain of LuxN by using ORCHESTRA program, and further estimated the binding poses and energies (docking scores) of 3-OH-$C_4$-HSL and HSHLs within the domain. In comparison of the result from this modeling study with that of in vivo bioassay, we suggest that the in silica interpretation of the interaction between ligands and their receptor proteins can be a valuable way to develop better competitive inhibitors, especially in the case that the structural information of the protein is limited.