Biological Control of Phytopathogenic Fungi by Fatty Acids

The aim of the present study was to evaluate the antifungal activity of fatty acids against phytopathogenic fungi. Two pot experiments were conducted by mixing palmitic and oleic acids in the soil in which poor plant growth was observed. In addition, the antifungal activities of nine fatty acids (butyric acid, caproic acid, caprylic acid, capric acid, lauric acid, myristic acid, palmitic acid, oleic acid, and linoleic acid) against four phytopathogenic fungi: Alternaria solani, Colletotrichum lagenarium, Fusarium oxysporum f. sp. Cucumerinum, and Fusarium oxysporum f. sp. lycopersici, were assessed by measuring mycelial growth and spore germination via Petri dish assay. The results of the pot experiments showed that the mixture of palmitic and oleic acids enhanced the growth of the seedlings of continuous-tomato and continuous-cucumber. Except for oleic acid, in the Petri dish assay, the fatty acids tested were observed to inhibit the mycelial growth of one or more tested fungi. In addition to the suppression of mycelial growth, butyric acid, caproic acid, caprylic acid, capric acid, lauric acid, and palmitic acid showed an inhibitory effect against spore germination and the extent of inhibition varied with both the type of fatty acids, and the fungi. In particular, capric acid displayed strong inhibitory effect against C. lagenarium on the mycelial growth and spore germination. The saturated fatty acids, i.e. palmitic acids, showed stronger antifungal activity than the unsaturated fatty acids, i.e. oleic acid. It suggests that fatty acids might be applicable to exploring for alternative approaches to integrated control of phytopathogens.     

Membrane protein analysis of human breast cancer cell line MCF-7 by different membrane washing methods

Membrane and membrane-associated proteins are rich in known or potential pharmaceutical drug targets for carcinogenesis. In order to systemically analyze membrane proteins of human breast cancer, we isolated membrane from MCF-7 cells by sequential extraction by washing with three different buffers, namely, phosphate buffer (5 mM, pH 8.0), Tris (40 mM, pH 9.5), and sodium carbonate (100 mM pH 11). The extracted proteins were separated by two-dimensional gel electrophoresis (2-DE) using cup-loading and were then analyzed by peptide mass fingerprinting (PMF). A total of 137 spots from the gels of the three procedures were successfully identified. They corresponded to 79 distinct proteins. Among them, 22 exclusive proteins belonging to each washing procedure were also found, including P-glycoprotein, endoplasmin, Stress-70 protein, ADAM 10, protein disulfide isomerase, and glutamate receptor. These results indicate phosphate buffer to be the most beneficial for enrichment of peripheral membrane proteins, and sodium carbonate is beneficial for the presentation of integral membrane proteins but usually with poor resolution. The reference maps and identified proteins will serve as a basis for the further investigation of breast cancer, especially the proteomic comparison among different cell types of breast cancer, or among the different stages in the drug interfering process of the MCF-7 cell line.     

羊栖菜的药用功能研究现状

对经济海藻羊栖菜的药用功能进行综述。认为其功能主要是抗癌、提高机体免疫能力和降血脂、降血压、防治心血管疾病等。     

N-Bromosuccinimide modification of tryptophan 241 at the C-terminus of the manganese stabilizing protein of plant photosystem II influences its structure and function

Life on earth depends upon the ability of oxygenic photosynthesis to oxidize water to molecular oxygen. This process is catalyzed by water–plastoquinone oxido-reductase complex. In addition to the photosystem II (PSII) reaction core, it includes a manganese stabilizing protein (MSP) that plays an important regulatory role in the process in plants and algae. Tryptophan 241, located at the carboxyl-terminus of the MSP, is its sole tryptophan. Modification of MSP by N-bromosuccinimide (NBS) was carried out to explore the role of Trp241 in maintaining its structure and function. Data and arguments are presented to show that it is Trp241, not other tyrosines in MSP, that is involved in the modification and changes observed in this study. Further, the pH-dependence of the modification and the comparison of features of fluorescence spectra of MSP suggested that Trp241 is buried in the hydrophobic interior of the protein. Hydropathy analysis revealed that Trp241 is located in the middle of the hydrophobic region at the C-terminus of MSP. Circular dichroism spectroscopy showed that NBS modification of Trp241 dramatically modified the protein structure. The affinity of MSP to PSII decreased greatly after the modification of Trp241, and no oxygen-evolving activity was recovered after its reconstitution. This study provides a novel demonstration that Trp241 at the C-terminus hydrophobic region of the MSP is critical for maintaining appropriate structure and function of MSP.