Prediction of the properties and thermodynamics of formation for energetic nitrogen-rich salts composed of triaminoguanidinium cation and 5-nitroiminotetrazolate-based anions.

Density functional theory and volume-based thermodynamics calculations were performed to study the effects of different substituents and linkages on the densities, heats of formation (HOFs), energetic properties, and thermodynamics of formation for a series of energetic nitrogen-rich salts composed of triaminoguanidinium cation and 5-nitroiminotetrazolate anions. The results show that the -NO(2), -NF(2), or -N(3) group is an effective substituent for increasing the densities of the 5-nitroiminotetrazolate salts, whereas the effects of the bridge groups on the density are coupled with those of the substituents. The substitution of the group -NH(2), -NO(2), -NF(2), -N(3), or the nitrogen bridge is helpful for increasing the HOFs of the salts. The calculated energetic properties indicate that the -NO(2), -NF(2), -N(3), or -N=N- group is an effective structural unit for improving the detonation performance for salts. The thermodynamics of formation of the salts show that all the salts may be synthesized easily by the proposed reactions. The structure-property relationships provide basic information for the molecular design of novel high-energy salts.

Suppression of human breast cancer cell metastasis by coptisine in vitro.

BACKGROUND: Coptisine, an isoquinoline alkaloid extracted from Coptidis rhizoma, has many biological activities such as antidiabetic, antimicrobial and antiviral actions. However, whether coptisine exerts anti-cancer metastasis effects remains unknown. MATERIALS AND METHODS: Effects of coptisine on highly metastatic human breast cancer cell MDA-MB-231 proliferation were evaluated by trypan blue assay and on cell adhesion, migration and invasion by gelatin adhesion, wound-healing and matrigel invasion chamber assays, respectively. Expression of two matrix metalloproteinases (MMPs), MMP-9, MMP-2 and their specific inhibitors tissue inhibitor of metalloproteinase 1 (TIMP-1) and tissue inhibitor of metalloproteinase 2 (TIMP-2) were analyzed by RT-PCR. RESULTS: Coptisine obviously inhibited adhesion to an ECM-coated substrate, wound healing migration, and invasion through the matrigel in MDA-MB-231 breast cancer cells. RT-PCR revealed that coptisine reduced the expression of the ECM degradation-associated gene MMP-9 at the mRNA level, and the expression of TIMP-1 was up-regulated in MDA-MB-231 cells, while the expression of MMP-2 and its specific inhibitor TIMP-2 was not affected. CONCLUSIONS: Taken together, our data showed that coptisine suppressed adhesion, migration and invasion of MDA-MB-231 breast cancer cells in vitro, the down-regulation of MMP-9 in combination with the increase of TIMP-1 possibly contributing to the anti-metastatic function. Coptisine might be a potential drug candidate for breast cancer therapy.