Synthesis of Azepinoindoles via Pd-Catalyzed C(sp2)-H Imidoylative Cyclization Reactions.

An efficient and convenient method for the construction of diverse free (N-H)-benzazepinoindoles by Pd-catalyzed C(sp2)-H imidoylative cyclization of 3-(2-isocyanobenzyl)-1H-indoles was developed. The reaction shows a wide substrate scope and can be scaled up, providing a practical route to valuable bioactive azepinoindoles.

BST-2 binding with cellular MT1-MMP blocks cell growth and migration via decreasing MMP2 activity.

MT1-MMP (membrane type 1-matrix metalloproteinase) plays important roles in cell growth and tumor invasion via mediating cleavage of MMP2/gelatinase A and a variety of substrates including type I collagen. BST-2 (bone marrow stromal cell antigen 2) is a membrane tetherin whose expression dramatically reduces the release of a broad range of enveloped viruses including HIV from infected cells. In this study, we provided evidence that both transient and IFN-α induced BST-2 could decrease the activity of MMP2 via binding to cellular MT1-MMP on its C-terminus and inhibiting its proteolytic activity; and finally block cell growth and migration. Zymography gel and Western blot experiments demonstrated that BST-2 decreased MMP2 activity, but no effect on the expression of MMP2 and MT1-MMP genes. Confocal and immunoprecipitation data showed that BST-2 co-localized and interacted with MT1-MMP. This interaction inhibited the proteolytic enzyme activity of MT1-MMP, and blocked the activation of proMMP2. Experimental results of C-terminus deletion mutant of MT1-MMP showed that activity of MMP2 was no change and also no interaction existed between the mutant and BST-2 after co-transfection with the mutant and BST-2. It meant that C-terminus of MT1-MMP played a key role in the interaction with BST-2. In addition, cell growth in 3D type I collagen gel lattice and cell migration were all inhibited by BST-2. Taken together, BST-2, as a membrane protein and a tetherin of enveloped viruses, was a novel inhibitor of MT1-MMP and could be considerable as an inhibitor of cancer cell growth and migration on clinic.

Development of randomly amplified polymorphic DNA-sequence characterized amplified region marker for identification of Apocynum venetum LINN. from A. pictum SCHRENK.

Apocynum venetum LINN. is an important Chinese crude drug, and its sibling species A. pictum SCHRENK is a confusable herb which is similar to it. The purpose of this study is to develop DNA molecular markers to distinguish A. venetum from A. pictum through the combinative technologies of bulked segregate analysis (BSA) and randomly amplified polymorphic DNA (RAPD). Two putative markers B08-407 and B03-1368 specific for A. venetum were identified and sequenced. Based on the sequence information, two pairs of primers were designed and synthesized for sequence characterized amplified region (SCAR) markers. But only one primer pair, B03-1368, produced a clear SCAR band in all samples of A. venetum and not in A. pictum. This SCAR marker was found useful for rapid identification of A. venetum from A. pictum.

[Experiment on extraction, sulfonate of paeonol and its antibiotic effect on plant pathogen].

Paeonol contents in root barks, cores, stems and leaves of Paeonia suffruticosa Andr. from Nanling county, Anhui province were determined and paeonol was extracted with alcohol, acid alcohol and alkali alcohol. Sodium paeonol sulfonate was synthesized by treating paeonol with concentrated sulfuric acid and oleums, and its physicochemical properties were surveyed by HPLC, TLC, FTIR and UV. Antibiotic experiment on plant pathogenic fungi and bacteria showed that paeonol and sodium paeonol sulfonate had remarkably inhibitive effects on Xanthmonas oryzae pv. oryzicola, Pseudomonas solanacearum, Phyllosticta mali and Rhizoctonia solani. Paeonol and sodium paeonol sulfonate had antibiotic effect on maize sheath blight.