KMID : 1234420090370030248
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Korean Journal of Microbiololgy and Biotechnology 2009 Volume.37 No. 3 p.248 ~ p.257
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Kim Cheol-Jin
Park Hyung-Yeon Kim Jae-Eun Park Hee-Jin Lee Bon-Su Choi Yu-Sang Lee Joon-Hee Yoon Je-Yong
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Abstract
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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-OHC4-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-C4-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-C4-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 silico 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.
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KEYWORD
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Quorum sensing inhibitors, autoinducer (AI-1), N-(3-hydroxysulfonyl)-L-homoserine lactone(HSL), Vibrio harveyi
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