Design and characterization of a binary CT complex of imidazole-oxyresveratrol: exploring its pharmacological and computational aspects.

A new binary charge transfer (CT) complex between imidazole (IMZ) and oxyresveratrol (OXA) was synthesized and characterized experimentally and theoretically. The experimental work was carried out in solution and solid state in selected solvents such as chloroform (CHL), methanol (Me-OH), ethanol (Et-OH), and acetonitrile (AN). The newly synthesized CT complex () has been characterized by various techniques such as UV-visible spectroscopy, FTIR, H-NMR, and powder-XRD. The 1:1 composition of is confirmed by Jobs' method of continuous variation and spectrophotometric (at λ 554 nm) methods at 298 K. The infrared spectra of confirmed the existence of proton transfer hydrogen bond beside charge transfer interaction. These findings indicate that the cation and anion are joined together by the weak hydrogen bonding as N-H-O. Reactivity parameters strongly recommended that IMZ behaves as a good electron donor and OXA an efficient electron acceptor. Density functional theory (DFT) computations with basis set B3LYP/6-31G (d,p) was applied to support the experimental results. TD-DFT calculations gives HOMO (-5.12 eV) → LUMO (-1.14 eV) electronic energy gap ( to be 3.80 eV. The bioorganic chemistry of was well established after antioxidant, antimicrobial, and toxicity screening in Wistar rat. The type of interactions between HSA and at the molecular level was studied through fluorescence spectroscopy. Binding constant along with the type of quenching mechanism, was investigated through the Stern-Volmer equation. Molecular docking demonstrated that binds perfectly with human serum albumin and EGFR (1M17) and exposes free energy of binding (FEB) values of -295.2 and -283.3 kcal/mol, respectively. The fits successfully into the minor groove of HAS and 1M17, the results of molecular docking show that the binds perfectly with the HAS and 1M17, the higher value of binding energy shows stronger interaction between HAS and 1M17 with . Our synthesized complex shows good binding results with HAS compared to 1M17.Communicated by Ramaswamy H. Sarma.