Inhibitory effect of copper complex of indomethacin on bacteria studied by microcalorimetry.

A microcalorimetric technique based on the bacterial heat output was explored to evaluate the effect of copper-indomethacin complex on Staphylococcus aureus and Escherichia coli. The extent and duration of the inhibitory effect on the metabolism as judged from the rate constant (k) in log phase, half inhibitory ratio (IC50). The rate constant of bacteria in the presence of the drugs decreased with increasing concentrations of the drugs. The copper complex exhibited higher antibacterial activity than the parent drug whose IC50 value was 1.5 and 2.3 times lower than that of indomethacin to S. aureus and E. coli, respectively. It was indicated that when the copper ion is coupled with indomethacin, the drug is more potent as a bacteriostatic.

Some properties of the interaction between 2,2'-diselenadibenzoic acid and serum albumins.

The binding of 2,2'-diselenadibenzoic acid to bovine serum albumin (BSA) and human serum albumin (HSA) was studied by using fluorescence spectroscopy. The measurement was performed in Tris-HCl buffer aqueous medium at pH = 7.40. The quenching constant at 303 K was (3.277 +/- 0.046) x 10(13) L mol(-1) s(-1) for BSA, and (3.946 +/- 0.002) x 10(12) L mol(-1) s(-1) for HSA. Decreased quenching was observed in association with increased temperature. Our findings show that the observed binding constant is dependent on the ionic strength of the medium. It is said that electrostatic interactions play a role in the binding of 2,2'-diselenadibenzoic acid to serum albumin, in addition to the hydrophobic association. The decrease of the linearity of S-V plot demonstrates reduced binding of ligand to the protein in the presence of anionic surfactants such as sodium dodecyl sulfate (SDS), which indicates that 2,2'-diselenadibenzoic acid most likely binds to the hydrophobic pockets within sub-domain IIA of serum albumin, the same site as SDS.

Absorption and fluorescence study of the interaction between (2-hydroxy-benzimido)ethyl-n-hexylselenide and bovine serum albumin.

The binding of Schiff base selenide, (2-hydroxy-benzimido)ethyl-n-hexylselenide, to bovine serum albumin (BSA) was studied using fluorescence spectroscopy. The measurement was performed in Tris-HCl buffer aqueous medium at pH 7.4. Stern-Volmer graphs were plotted and quenching constants were estimated. The quenching constant at 303 K was (1.639 +/- 0.046) x 10(13) L mol(-1) s(-1). Decreased quenching was observed as temperature increased, but at the temperature range of 303-313 K, the association of Schiff base selenide to BSA was not significantly different. The static quenching presented in the system of Schiff base selenide and BSA. A complex was possibly formed between Schiff base selenide and BSA, which was responsible for the quenching of the fluorescence of BSA. This fact was also confirmed by differences in the absorption spectra of BSA before and after Schiff base selenide addition. The hydrophobic interaction was found to play a main role in the binding according to the thermodynamic parameters, enthalpy change (DeltaH) and entropy change (DeltaS) of reaction. Schiff base selenide most likely binds to the hydrophobic pockets within sub domain IIA of BSA, which can be proved by competition experiments for sodium dodecyl sulfate. By constant-wavelength synchronous fluorescence spectra, the influence of (2-hydroxy-benzimido)ethyl-n-hexylselenide on the surrounding environment of tyrosine and tryptophan residues in BSA was also investigated. The red shift of the fluorescence peak of tryptophan residues indicated that the hydrophobic amino acid structure surrounding tryptophan residues in BSA collapsed slightly after the addition of (2-hydroxy-benzimido)ethyl-n-hexylselenide.