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He J.-B.,Key Laboratory of Pesticide and Chemical Biology CCNU | He J.-B.,Wuhan Polytechnic University | He J.-B.,Hubei Collaborative Innovation Center for Processing of Agricultural Products | He H.-F.,Key Laboratory of Pesticide and Chemical Biology CCNU | And 6 more authors.
Bioorganic and Medicinal Chemistry | Year: 2015

To identify new antifungal lead compound based on inhibitors of pyruvate dehydrogenase complex E1, a series of 5-iodo-1,4-disubstituted-1,2,3-triazole derivatives 3 were prepared and evaluated for their Escherichia coli PDHc-E1 inhibitory activity and antifungal activity. The in vitro bioassay for the PDHc-E1 inhibition indicated all the compounds exhibited significant inhibition against E. coli PDHc-E1 (IC50 <21 μM), special compound 3g showed the most potent inhibitory activity (IC50 = 4.21 ± 0.11 μM) and was demonstrated to act as a competitive inhibitor of PDHc-E1. Meanwhile, inhibitor 3g exhibited very good enzyme-selective inhibition of PDHc-E1 between pig heart and E. coli. The assay of antifungal activity showed compounds 3e, 3g, and 3n exhibited fair to good activity against Rhizoctonia solani and Botrytis cinerea even at 12.5 μg/mL. Especially compound 3n (EC50 = 5.4 μg/mL; EC90 = 21.1 μg/mL) exhibited almost 5.50 times inhibitory potency against B. cinerea than that of pyrimethanil (EC50 = 29.6 μg/mL; EC90 = 113.4 μg/mL). Therefore, in this study, compound 3n was found to be a novel lead compound for further optimization to find more potent antifungal compounds as microbial PDHc-E1 inhibitors. © 2015 Elsevier Ltd. All rights reserved.

Tu Q.-D.,Key Laboratory of Pesticide and Chemical Biology CCNU | Tu Q.-D.,Central China Normal University | Tu Q.-D.,Jiangxi Science and Technology Normal University | Li D.,Key Laboratory of Pesticide and Chemical Biology CCNU | And 17 more authors.
Bioorganic and Medicinal Chemistry | Year: 2013

Cyanobacterial fructose-1,6-/sedoheptulose-1,7-bisphoshatase (Cy-FBP/SBPase) is an important target enzyme for finding inhibitors to solve harmful algal bloom (HAB). In this study, as potential inhibitors of Cy-FBP/SBPase, a series of novel chromone-connecting benzohydrazone compounds (Novel N′-((4-oxo-4H-chromen-3-yl)methylene)benzohydrazide) were designed and synthesized. Their inhibitory activities against Cy-FBP/SBPase were further examined in vitro. Some of these compounds, such as f6-f8, f11, f12 and f16, exhibit higher inhibitory activities (IC50 = 11.2-16.1 μM), especially, the compound f7 was identified as the most potent inhibitor with IC50 value of 11.2 μM. The probable binding-mode of compound f7 was further analyzed carefully by molecular docking methods. These results indicate that compound f7 could be used as a lead compound for further optimization and might have potential to be developed as a new algicide. © 2013 Elsevier Ltd. All rights reserved.

Zhang W.,Central China Normal University | Yuan L.,Central China Normal University | Zhang L.,Central China Normal University | Li N.,Central China Normal University | And 6 more authors.
5th International Conference on Bioinformatics and Biomedical Engineering, iCBBE 2011 | Year: 2011

The gene encoding acetylcholinesterase (AChE) was cloned from Kunming mouse brain. The full length cDNA was 1845 bp, corresponding to a protein of 614 amino acids. The specific protein bend with molecular masses of 68 kDa was observed by SDS-PAGE analysis. After purified 2,400 fold, it was exhibited the specific activity of 742 U/mg. Then, an interface embedded in situ gold nanoparticles (AuNPs) and biotin in chitosan hydrogel was constructed by one-step electrochemical deposition. A.C. impedance was used to characterize this interface. The immobilized AChE, as a model, provided a quantitative measurement of organophosphate pesticide. Under the optimal experimental conditions, the inhibition of dimethoate was proportional to its concentrations in the range of 0.05 to 15 μg/mL with detection limit of 0.001 μg/mL. © 2011 IEEE.

Zhang J.,Central China Normal University | Zhao L.,Central China Normal University | Zhao L.,Qingdao Agricultural University | Han R.,Central China Normal University | And 6 more authors.
Pest Management Science | Year: 2010

BACKGROUND: Sterol 14α-demethylase (CYP51), a key target of azole (DMI) fungicides, can be expressed in both prokaryotes and eukaryotes. Green mould of citrus, caused by Penicillium digitatum (Pers.) Sacc., is a serious post-harvest disease. To develop specific and more effective fungicides against this disease, the characteristics of the interaction between sterol 14α-demethylase from P. digitatum (PdCYP51) and possible new fungicides were analysed. The cyp51 gene of P. digitatum was cloned and expressed under different conditions in Escherichia coli (Mig.) Cast. & Chalm., and the binding spectra of PdCYP51 were explored by the addition of two commercial azoles and four new nitrogen compounds.RESULTS: The yield of soluble protein (PdCYP51) was largest when expressed in Rosetta (DE3) induced by 0.5 mM IPTG for 8 h at 30 °C. Compound B (7-methoxy-2H-benzo[b][1,4]thiazine-3-amine) showed the strongest binding activity of the four new nitrogen compounds, with a Kd value of 0.268 μM. The Kd values of the six compounds were significantly correlated with their EC50 values.CONCLUSION: The spectral analysis and bioassay results could be used to screen the new chemical entities effectively. Compound B, selected by virtual screening from a commercial chemical library, is a candidate for a new DMI fungicide. These results provide a theoretical basis and new ideas for efficient design and development of new antifungal agents. Copyright © 2010 Society of Chemical Industry Copyright © 2010 Society of Chemical Industry.

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