The binding interaction of peripheral H receptor antagonist drug, fexofenadine hydrochloride to bovine serum albumin (BSA) is investigated by fluorescence spectroscopy in combination with UV-absorption spectroscopy under physiological conditions. The Stern-Volmer plots at different temperatures and the steady state fluorescence suggested a static type of interaction between fexofenadine and BSA. Binding constants were determined to provide a measure of the binding affinity between fexofenadine and BSA. It was found that BSA has one binding site for fexofenadine. On the basis of the competitive site marker experiments and thermodynamic results, it was considered that fexofenadine was primarily bound to the site I of BSA mainly by hydrogen bond and van der Waals force. Utilising Förster resonance energy transfer the distance, r between the donor, BSA and acceptor fexofenadine was obtained. Furthermore, the results of circular dichroism and synchronous fluorescence spectrum indicated that the secondary structure of BSA was changed in the presence of fexofenadine. Molecular docking was applied to further define the interaction of fexofenadine with BSA.
The kinetics of the oxidation of fosfomycin disodium salt by cerium(IV) in an aqueous perchloric acid medium at constant ionic strength, I D 1.10 mol dm ¡3 , has been investigated spectrophotometrically at 25 C. The reaction is of first order in cerium(IV) concentration, fractional order in both fosfomycin and H C ion concentrations. The active species of oxidant is found to be Ce (OH) 3C . Based on the experimental results a suitable mechanism is proposed. The reaction constants involved in the different steps of the reaction mechanism and the activation parameters with respect to the slow step of the mechanism are determined and discussed.
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