[Study of interaction between sorbitol and bovine serum albumin by fluorescence spectrometry].

The interaction of sorbitol and bovine serum album (BSA) was studied by fluorescence and ultraviolet absorption spectra. As it is well known to us, the interactional analysis between small molecular drug and biology macromolecule (such as protein, DNA, etc) is one of the important interactional analyses, which can not only offer new biological view but also supply chance for chemist and biochemist to synthesize new drug capable of regulating the biology process effectively. In the present paper, fluorescence spectrophotometry was first employed to study the interaction between BSA and sorbitol. At the same time, the synchronous fluorescence spectroscopy was adopted to review the configuration of BSA influenced by sorbitol, which provides important significance for clinical medication. The results show that sorbitol has strongly quenched the fluorescence of bovine serum albumin in natural physiological condition, the quenching mechanism is a static quenching procedure at different temperatures and drug concentration, and the variational absorption spectra also proves this deduction. At the same time, this article has also examined the influences of sorbitol on the fluorescence quenching of bovine serum albumin at different temperatures and drug concentration. The binding constants and the number of binding sites between sorbitol and BSA were calculated at different temperatures. Furthermore, the enthalpy and entropy changes in the interaction of sorbitol and bovine serum album were also obtained by the equations of Stern-Volmer and Lineweaver-Burk. From the thermodynamic parameters, it can be judged that the primary binding power between sorbitol and BSA is electrostatic force. Moreover, the synchronous fluorescence spectroscopy was applied to examine the effect of sorbitol on the configuration of BSA. The alterative configuration of BSA may be induced by the hydrophobicity environment of tyrosine with the increase in drug concentration. In conclusion, the fluorescence method is highly sensitive and convenient in the study of intermolecular interaction. Further studies in this field will open up the way to applications of biology macromolecule in analytical chemistry and analytical biochemistry.

[Studies on the reaction of balofloxacin with bovine serum albumin].

In the present paper, a fluorescence method was used to study at different pH the fluorescence quenching of bovine serum albumin (BSA) by its interaction with balofloxacin (BLFX). The interaction association constants of BSA and BLFX were determined from a double reciprocal line Weaver-Burk plot. According to the Forster dipole-dipole energy transfer, the distance to be measured between the BLFX and tryptophane is 5.09 nm. From thermodynamical coordination it can be judged that the binding power between BLFX and BSA is electrostatic effect. The effect of BLFX on the conformation of BSA was also analyzed by using synchronous fluorescence spectroscopy.