Synthesis,computational, molecular docking studies and photophysical properties of (Z)-N-(pyrimidin-2-yl)-4-(thiophen-2-ylmethylene)amino) benzenesulfonamide

The (Z)-N-(pyrimidin-2-yl)-4-(thiophen-2-ylmethylene)amino) benzenesulfonamide (TH2DA) were synthesized and characterized by the Infrared, UV–Visible, and NMR analysis. Using density functional theory, the current work is a set of theoretical studies on TH2DA. The compound molecular structure and geometry were defined using DFT. Topological studies, like ELF, LOL, ALIE, and RDG studies, were done with the Multiwfn-3.8 to find the main binding areas and weak interactions in the molecule. Using the IEFPCM solvation model were used to study the calculated UV–Visible spectrum. The HOMO-LUMO, MEP, and NLO properties were carried out in the gas phase. The NBO calculations are used to study how charges move between and within the molecule and stability of this molecule. A pharmacological analysis is done using online tool like Swiss-ADME, to see if the molecule could be potential drug candidate; this evaluation looks at the drug-likeness, ADME and eco-friendly toxicity properties of the TH2DA molecule. Auto-dock suite and Discovery studio Visualizer are used to do molecular docking studies.     

Molecular modeling and spectroscopic studies on binding of 2,6-bis[4-(4-amino-2-trifluoromethylphenoxy)benzoyl] pyridine to human serum albumin

BAFP (2,6-bis[4-(4-amino-2-trifluoromethylphenoxy)benzoyl] pyridine), a synthesized polyimide compound, was exploited for the first time to analyze its interaction with human serum albumin (HSA) by molecular modeling, fluorescence and Fourier transform infrared attenuated total reflection spectroscopy (FTIR ATR) with drug concentrations of 3.3 × 10⁻⁶ to 3.0 × 10⁻⁵ mol L⁻¹. Molecular docking was performed to reveal the possible binding mode. The results suggested that BAFP can strongly bind to human serum albumin (HSA) and the primary binding site of BAFP is located in site II of HSA, which is supported by the results from the competitive experiment. The binding constants for the interaction of BAFP with HSA have been evaluated from relevant fluorescence data at different temperatures (296, 303, 310 and 308 K). The alterations of the protein secondary structure in the presence of BAFP in aqueous solution were quantitatively calculated by the evidences from FTIR ATR spectroscopes. The binding process was exothermic and spontaneous, as indicated by the thermodynamic analyses, and the major part of the binding energy is hydrophobic interaction, which is also in good agreement with the results of molecule modeling study. The enthalpy change ΔH⁰, the free energy change ΔG⁰ and the entropy change ΔS⁰ of 296 K were calculated to be −7.75, −27.68 kJ mol⁻¹ and 67.33 J mol⁻¹ K⁻¹, respectively.