INVESTIGATION OF THE BINDING ABILITY OF A NEW THIOSEMICARBAZONE-BASED LIGAND AND ITS Zn(II) COMPLEX TOWARD PROTEINS AND DNA: SPECTRAL, STRUCTURAL, THEORETICAL, AND DOCKING STUDIES

new thiosemicarbazone derivative ligand N -(4-chlorophenyl)-2-(pyridin-2-ylmethylene)hydrazine-1-carbothioamide (HL) and its zinc(II) complex [ZnL 2 ]·CH 2 Cl 2 ( 1 ) are prepared and characterized by elemental analysis, FTIR and 1 H NMR spectroscopy, and single crystal X-ray diffraction (for 1 ). The X-ray analysis reveals that the zinc atom is octahedrally coordinated by two N Py N imine S thiolate -donor ligands with the mer form. The HL ligand is deprotonated during the complexation process through the thiol group. In the crystal network of 1 , the N–H⋯S hydrogen bonds form R_2^2 (8) hydrogen bond motifs. In addition, the crystal network is more stabilized by π–π stacking and C–H⋯π interactions. The ability of complex 1 to interact with ten selected biomacromolecules (BRAF kinase, CatB, DNA gyrase, HDAC7, rHA, RNR, TrxR, TS, Top II, and B-DNA) is investigated by docking studies. The results show that in many cases, complex 1 can interact with proteins better than doxorubicin.