Chiral analysis and semi-preparative separation of metconazole stereoisomers by supercritical fluid chromatography and cytotoxicity assessment in vitro.

Metconazole is one of the widely-used chiral triazole fungicides in controlling wheat leaf rust, powdery mildew, Fusarium head blight with high efficacy, and so forth. In the current work, the effects of chiral stationary phases, alcoholic modifiers, and column temperature on the chiral separation of metconazole were discussed in detail. Amylose tris(3,5-dimethylphenylcarbamate)-coated chiral stationary phase exhibited much stronger chiral recognition ability toward metconazole stereoisomers in the CO2 /ethanol mixture as compared to the others. Then, a two-step semi-preparative separation of metconazole was performed through supercritical fluid chromatography and high-performance liquid chromatography, and the enantiomeric excess values of four stereoisomers were achieved over 98%. Moreover, the enantioselective cytotoxicity of cis-metconazole against HepG2 cells has been investigated, and the order of the cell proliferation toxicity against HepG2 cells was (1R, 5S)-metconazole > (1S, 5R)-metconazole > the mixture. Briefly, this study would provide valuable information in the preparative separation of optically pure metconazole products through chromatographic techniques and their environmental risk assessment.

Crucial roles of membrane stability and its related proteins in the tolerance of peach fruit to chilling injury.

Proteome patterns in peach fruit (Prunus persica L.) stored at different low temperatures were examined in order to gain a better understanding why peach fruit is less prone to chilling injury when stored at 0 degrees C than at 5 degrees C. Some differently expressed proteins in peach fruit stored at 0 and 5 degrees C were identified using electrospray ionization quadrupole time-of-flight tandem mass spectrometry. Among these proteins, four membrane stability related proteins, i.e., enolase, temperature-induced lipocalin, major allergen Pru p 1, and type II SK2 dehydrin were enhanced, but three proteins related to phenolic compounds metabolization, cinnamyl-alcohol dehydrogenase 5, cinnamyl-alcohol dehydrogenase 1, and chorismate mutase, were repressed in peach fruit at 0 degrees C as compared to that at 5 degrees C. The abundance of glucose-6-phosphate dehydrogenase, NADP-dependent isocitrate dehydrogenase, and NADP-dependent malic enzyme, which catalyze the reactions during sugar metabolism and energy pathways, was found to decrease in peach fruit stored at 0 degrees C. In addition, our data revealed that low temperature of 0 degrees C might regulate the endogenous H(2)O(2) level, resulting in activating the transcriptional level of genes encoding the proteins related to membrane stability. These results provide a comprehensive knowledge to understand the mechanisms by which peach fruit stored at 0 degrees C showed a higher chilling tolerance than that at 5 degrees C.