No abstract

A new imine-based molecule 2-((E)-(6-fluorobenzo[d]thiazol-2-ylimino) methyl)-4chlorophenol (FBt) was synthesized by microwave and conventional method. It was structurally characterized by spectral techniques (NMR, FT-IR, LC-MS and electronic absorption), elemental analysis and single-crystal X-ray diffraction methods. Hirshfeld surface analysis was employed to ensure the existence of intermolecular interactions in FBt structure. A preliminary in vitro susceptibility test against two pathogenic fungi with respect to standard has shown that the ligand is proved to be a potent antifungal agent. Since the carrying of a drug by BSA may effect on its structure and action, the investigation on the interaction between model protein BSA and FBt was carried out by employing UV-Vis and fluorescence spectroscopy. The characteristics of the binding, i.e., binding constant, number of binding sites, and nature of binding were determined. Besides, the Förster's parameters associated with the binding process were calculated. Molecular docking was also carried on interaction study of the FBt with BSA.

One of the highly soluble protein presents in circulatory system of bovine body is bovine serum albumin (BSA). Bupropion hydrochloride (BRN) served to treat prime smoking cessation and disorder due to depressive. BRN binding to BSA was studied by molecular docking and lots of spectroscopic (UV-vis, emission, synchronous, 3D fluorescence, CD and FT-IR) methods at pH = 7.40. Static quenching with strong binding was obtained for BSA-BRN system by forming complex. Secondary structures, conformations and microenvironments of BSA were altered after BRN interaction. Distance between BRN and BSA was also achieved. Biologically active metal ions (Cu2+, Ca2+, Mg2+, Fe2+ and Zn2+) were also influenced on the BSA-BRN complex. Bonds of hydrogen and Van der Waals were major binding forces to stabilize BSA-BRN complex at site I (IIA) of BSA. Hence, binding of BRN to transport protein (BSA) is of prominent importance and these findings could be helpful for BRN pharmacology and potential clinical research.

The triptan drug such as eletriptan in combination with hydrochloride (ETP) is a 5-HT1 receptor agonist used to treat the migraine headache. Human serum albumin (HSA), the fundamental serum protein, executes various functions, that includes transporting and binding of many ligands. HSA binding interaction with ETP is elucidated from molecular docking in composite with fluorescence (emission, 3D and synchronous), UV-vis and FT-IR spectroscopy at 296, 304 and 312 K (pH = 7.40). ETP after interaction modified the HSA secondary structure and its micro-environments. Energy transfer and thermodynamic parameters were evaluated. Various quenching and binding constants were computed for formed ETP-HSA complex. The dominant interactive forces for ETP and HSA binding are hydrogen bonds join up with van der Waals extent possibly at site III (IB). The presence of Ca2+, Co2+, Na+, Mg2+ and Fe3+ ions significantly affected binding ability of ETP towards HSA. The essentialness of this investigation is beneficial in life sciences, medicinal chemistry, pharmaceutical industry and clinical medicine.