We report growth of quaternary Cu2 ZnSnS4 (CZTS) thin films prepared by the electrochemical deposition from salt precursors containing Cu (II), Zn (II) and Sn (IV) metals. The influence of different sulfurization times t (t = 75, 90, 105, and 120 min) on the structural, compositional, morphological, and optical properties, as well as on the electrical properties is studied. The films sulfurized 2 hours showed a prominent kesterite phase with a nearly stoichiometric composition. Samples were characterized by X-ray diffraction (XRD), field-emission scanning electron microscopy (FESEM), and Raman and UV-VIS-NIR spectrometer at different stages of work. X-ray diffraction and Raman spectroscopy analyses confirmed the formation of phase-pure CZTS films. (FESEM) shows that compact and dense morphology and enhanced photo-sensitivity. STEM - EDS elemental map of CZTS cross-section confirms homogeneous distribution. From optical study, energy gap was enlarged with a changed sulfurization times in the range of 1.37-1.47 eV.
Some novel hydrazone derivatives 6a-o were synthesized from the key intermediate 4-Chloro-N-(2-hydrazinocarbonyl-phenyl)-benzamide 5 and characterized using IR, ¹H-NMR, 13C-NMR, mass spectroscopy and elemental analysis. The inhibitory potential against two secretory phospholipase A₂ (sPLA₂), three protease enzymes and eleven bacterial strains were evaluated. The results revealed that all compounds showed preferential inhibition towards hGIIA isoform of sPLA₂ rather than DrG-IB with compounds 6l and 6e being the most active. The tested compounds exhibited excellent antiprotease activity against proteinase K and protease from Bacillus sp. with compound 6l being the most active against both enzymes. Furthermore, the maximum zones of inhibition against bacterial growth were exhibited by compounds; 6a, 6m, and 6o against P. aeruginosa; 6a, 6b, 6d, 6f, 6l, 6m, 6n, and 6o against Serratia; 6k against S. mutans; and compounds 6a, 6d, 6e, 6m, and 6n against E. feacalis. The docking simulations of hydrazones 6a-o with GIIA sPLA₂, proteinase K and hydrazones 6a-e with glutamine-fructose-6-phosphate transaminase were performed to obtain information regarding the mechanism of action.