Bovine Serum Albumin interactions with new derivatives Schiff base study by spectroscopic techniques

The interaction ofternary Cu(II) complexes of schiffbase tyrosine amino acid derivatives and bipyridine hetrocycle (S) with bovine serum albumin (BSA) was investigated using fluorescence quenching and Fourier transform infrared (FTIR). Fluorescence quenching data showed that the quenching mechanism of BSA treated by the complex was static quenching, which was highly accord with the non-radioactive energy transfer theory. . The quenching data were used for calculation parameters such as binding sites, binding distance. Intermolecular forces between the complex and BSA were also obtained by analyzing the fluorescence spectral data Fourier transform infrared spectroscopic data demonstrated that BSA interacts with Schiff base molecule mainly via both the hydrophobic and hydrophilic interactions with a minor change in the secondary structure of BSA.

Keywords:

Schiff base , BSA , Flourescence , FTIR , interaction