(E)-4-(2-Chloro­benzyl­ideneamino)-3-(2-chloro­phen­yl)-1H-1,2,4-triazole-5(4H)-thione–(E)-1,5-bis­(2-chloro­benzyl­idene)thio­carbonohydrazide–methanol (1/1/1)

In the title compound, C15H12Cl2N4S·C15H10Cl2N4S·C2H6O, the two chloro­phenyl rings of the triazole derivative form dihedral angles of 65.7 (2) and 44.2 (2)° with the triazole ring. In the thio­carbonohydrazide derivative, the dihedral angle between the two chloro­phenyl rings is 5.4 (2)°. In the crystal, the triazole, thio­carbonohydrazide and methanol mol­ecules are linked by N—H⋯O, N—H⋯S and O—H⋯S hydrogen bonds, forming a hexa­meric unit

Effect of Original Layer Thicknesses on the Interface Bonding and Mechanical Properties of Ti-Al Laminate Composites

It is of great significance in high-temperature aeroengine applications for large-surface-area TiAl laminate composites to be fabricated into Ti-Al3Ti parts by plastic forming and subsequent vacuum hot pressing. Then the original layer thicknesses have an important influence on the interface bonding and mechanical properties of TiAl laminate composites, but only few reports about it have been published so far. In the present study, vacuum hot pressing was employed to fabricate TiAl laminate composites using Ti and Al foils of different thickness. The resulting interface bond and mechanical properties of TiAl laminate composites were then studied to determine the optimum sheet configuration and thickness. To further assess their formability and develop a forming limit diagram (FLD), 0.1/0.15 TiAl laminate composites were operated on bending and forming tests to provide guidance for subsequent plastic forming of complex geometries. The results indicated that hot pressed laminates composed of alternating 0.1 (Al) and 0.15 (Ti) mm thick sheets exhibited enhanced superior interface bonding and mechanical properties compared with 0.2/0.25 and 0.4/0.4 sheets. The 0.1/0.15 TiAl laminate composites had excellent bending characteristics and reasonable formability. Fabrication of a drawn cup further confirms the potential for hot pressed TiAl laminate composites to be fabricated into complex shapes

Study of charm hadronization and in-medium modification at the Electron-ion Collider in China

Charm quark production and its hadronization in ep and eA collisions at the future Electron-Ion Collider in China (EicC) will help us understand the quark/gluon fragmentation processes and the hadronization mechanisms in the nuclear medium, especially within a poorly constrained kinematic region ($x<0.1$). In this paper, we report a study on the production of charmed hadrons, $D^0$ and $\Lambda_c^+$, reconstructed with a dedicated GEANT4 simulation of vertex$\,\&\,$tracking detectors designed for EicC. The $\Lambda_c^+$/$D^0$ ratios as functions of multiplicity and $p_T$, as well as the $D^0$ double ratio are presented with projected statistical precision.Comment: 9 pages, 12 figure

In-silico investigations into natural products as nonnucleoside DNA methyltransferase 1 inhibitors for treating epi-mutation in gastric cancer

Purpose: To explore in silico methods to search for the best reported non-nucleoside DNA methyltransferase 1 (DNMT1) inhibitor of epimutation in gastric cancer.Methods: A dataset of reported non-nucleoside DNMT1 inhibitors was used to target the active site of crystallized DNMT1 protein. Molecular docking simulations were carried out using AutoDock 4.2.6 l. The results were analyzed using Discovery studio visualizer.Results: In silico analysis of known natural non-nucleoside DNMT1 inhibitors gave genistein as the top ranked compound with ΔG of -6.39 Kcal/mol. Further, the results indicated that epigallocatechin gallate and curcumin are poor non-nucleoside DNMT1 inhibitors, as the in silico data suggest that they failed to bind to the catalytic site of DNMT1.Conclusion: The results indicate that genistein is the top rated compound for DNMT1 inhibition. Previous in vitro and in vivo work by other researchers seem to validate the findings of the study.Keywords: Epi-mutation, DNA methyltransferase, Non-nucleoside, DNMT1 inhibitor, Dockin