Study on the interaction between Besifloxacin and bovine serum albumin by spectroscopic techniques.

The interaction between Besifloxacin (BFLX) and bovine serum albumin (BSA) was investigated by spectroscopic (fluorescence, UV-Vis absorption and circular dichroism) techniques under imitated physiological conditions. The experiments were conducted at different temperatures (298, 304 and 310 K) and the results showed that the BFLX caused the fluorescence quenching of BSA through a static quenching procedure. The binding constant (Ka), binding sites (n) were obtained.

Study on the interaction between 21-(Ph-NN)-NCTPP and bovine serum albumin by spectroscopic techniques.

The interaction between 21-(Ph-NN)-NCTPP and bovine serum albumin (BSA) was investigated by fluorescence and ultraviolet-visible (UV-Vis) spectroscopy under imitated physiological conditions. The results showed that the intrinsic fluorescence of BSA was quenched strongly by 21-(Ph-NN)-NCTPP. The binding constants (Ka) and the binding sites (n) were obtained at three different temperatures (298, 304, and 310K).

Spectroscopic analyses on interaction of bovine serum albumin with novel spiro[cyclopropane-pyrrolizin].

The interaction between novel spiro[cyclopropane-pyrrolizin] (NSCP) and bovine serum albumin (BSA) was analyzed by fluorescence and ultraviolet-visible (UV-Vis) spectroscopy at 298 K, 304 K and 310 K under simulative physiological conditions. The results showed that NSCP can effectively quench the intrinsic fluorescence of BSA via static quenching. The binding constants, binding sites of NSCP with BSA were calculated.

Study on the interaction between carbonyl-fused N-confused porphyrin and bovine serum albumin by spectroscopic techniques.

The interaction between carbonyl-fused N-confused porphyrin (CF-NCP) and bovine serum albumin (BSA) was investigated by fluorescence and ultraviolet-visible (UV-Vis) spectroscopy. The results indicated that CF-NCP has strong ability to quench the intrinsic fluorescence of BSA by forming complexes. The binding constants (Ka), binding sites (n) were obtained.

Interaction between pirenoxine and bovine serum albumin in aqueous solution.

This work concerns the interaction of prenoxine sodium (PRX) and bovine serum albumin (BSA), which was conducted by spectroscopic means: fluorescence spectra, ultraviolet-visible spectra (UV-vis) and circular dichroism spectra (CD spectra) in physiological conditions. The results revealed the PRX can quench the fluorescence of BSA remarkably in aqueous solution. The quench mechanism has been obtained after corrected the fluorescence intensities for inner filter effects.

Spectroscopic studies on the interaction of Phacolysin and bovine serum albumin.

The interaction between Phacolysin (PCL) and bovine serum albumin (BSA) under imitated physiological conditions was investigated by spectroscopic (fluorescence, UV-Vis absorption and Circular dichroism) techniques. The experiments were conducted at different temperatures (294K, 302K, 306K and 310K) and the results showed that the PCL caused the fluorescence quenching of BSA through a static quenching procedure. The binding constant (Ka), binding sites (n) were obtained.

The investigation of the interaction between Tropicamide and bovine serum albumin by spectroscopic methods.

The fluorescence and ultraviolet-visible (UV-Vis) spectroscopy were explored to study the interaction between Tropicamide (TA) and bovine serum albumin (BSA) at three different temperatures (292, 301 and 310K) under imitated physiological conditions. The experimental results showed that the fluorescence quenching mechanism between TA and BSA was static quenching procedure. The binding constant (Ka), binding sites (n) were obtained.