Background: Studies on the interaction between bioactive molecules and HIV-1 virus have been the focus of recent research in the scope of medicinal chemistry and pharmacology. Objective: Investigating the structural parameters and physico-chemical properties of elucidating and identifying the antiviral pharmacophore sites. Methods: A mixed computational Petra/Osiris/Molinspiration/DFT (POM/DFT) based model has been developed for the identification of physico-chemical parameters governing the bioactivity of 22 3-hydroxy-indolin-2-one derivatives of diacetyl-L-tartaric acid and aromatic amines containing combined antiviral/antitumor/antibacterial pharmacophore sites. Molecular docking study was carried out with HIV-1 integrase (pdb ID: 5KGX) in order to provide information about interactions in the binding site of the enzyme. Results: The POM analyses of physico-chemical properties and geometrical parameters of compounds 3a-5j, show that they are bearing a two combined (O,O)-pockets leading to a special platform which is able to coordinate two transition metals. The increased activity of series 3a-5j, as compared to standard drugs, contains (Osp²,O sp³,O sp²)-pharmacophore site. The increase in bioactivity from 4b (R¹, R² = H, H) to 3d (R¹, R² = 4-Br, 2-OCH₃) could be attributed to the existence of π-charge transfer from para-bromo-phenyl to its amid group (CO^δ---NH^δ+). Similar to the indole-based reference ligand (pdb: 7SK), compound 3d forms hydrogen bonding interactions between the residues Glu170, Thr174 and His171 of HIV-1 integrase in the catalytic core domain of the enzyme. Conclusion: Study confirmed the importance of oxygen atoms, especially from the methoxy group of the phenyl ring, and electrophilic amide nitrogen atom for the formation of interactions.

Herein, new substituted ligands based on pyrazole (L₁–L₄) were synthesized via a one-step by condensing (1H-pyrazole-1-yl) methanol with different primary amine compounds. The present work utilized the catalytic properties of the in situ complexes formed by these ligands with various copper (II) salts viz. Cu(CH₃COO)₂, CuSO₄, CuCl₂, and Cu(NO₃)₂ for the oxidation of catechol to o-quinone. The studies showed that the catalytic activities depend on the nature and concentration of the ligand, the nature of the counterion, and the solvent. It was observed that the complex formed by L₂ and Cu(CH₃COO)₂ exhibited good catalytic activity in methanol with V_max of 41.67 µmol L⁻¹ min⁻¹ and K_m of 0.02 mol L⁻¹.

In this work, we report on the catalytic activity of a manganese complex [(Cl)₂Mn(RCOOET)], where RCOOET is ethyl-5-methyl-1-(((6-methyl-3-nitropyridin-2-yl)amino)methyl)-1H-pyrazole-3-carboxylate, in the oxidation of phenol or catechol by atmospheric oxygen to form o-quinone. The [(Cl)₂Mn(RCOOET)] catalyzes the oxidation of catechol at a rate of 3.74 µmol L⁻¹ min⁻¹ in tetrahydrofuran (THF), in a similar manner to catecholase or tyrosinase.

A new double-open-cubane core Cd(II)-O-Cu(II) bimetallic ligand mixed cluster of type [Cl₂Cu₄Cd₂(NNO)₆(NN)₂(NO₃)₂].CH₃CN was made available in EtOH/CH₃CN solution. The 1-hydroxymethyl-3,5-dimethylpyrazole (NNOH) and 3,5-dimethylpyrazole (NNH) act as N,O-polydentate anion ligands in coordinating the Cu(II) and Cd(II) centers. The structure of the cluster in the solid state was proved by XRD study and confirmed in the liquid state by UV-vis analysis. The XRD result supported the construction of two octahedral and one square pyramid geometries types around the four Cu(II) centers and only octahedral geometry around Cd(II) two centers. Interestingly, NNOH ligand acts as a tetra-µ³-oxo and tri-µ²-oxo ligand; meanwhile, the N-N in NNH acts as classical bidentate anion/neutral ligands. The interactions in the lattice were detected experimentally by the XRD-packing result and computed via Hirschfeld surface analysis (HSA). The UV-vis., FT-IR and Energy Dispersive X-ray (EDX), supported the desired double-open cubane cluster composition. The oxidation potential of the desired cluster was evaluated using a 3,5-DTB-catechol 3,5-DTB-quinone as a catecholase model reaction.