| pubmed-article:17623271 | pubmed:abstractText | The interactions of 2-nitroaniline (2-NA), 3-nitroaniline (3-NA) and 4-nitroaniline (4-NA) with bovine serum albumin (BSA) have been investigated by means of fluorescence spectrometry, synchronous fluorescence spectrometry and UV absorption spectrometry under the simulative physiological conditions. Association constants (K(A)) were estimated by the remarkable static quenching effect of 2-NA, 3-NA and 4-NA to the intrinsic fluorescence of BSA, and thermodynamic parameters such as enthalpy change (DeltaH) and entropy change (DeltaS) were calculated according to van't Hoff equation. The results show that hydrophobic force plays a main role in the interaction of nitroanilines to BSA, nitroanilines have high affinity to BSA and the affinity order is as follows: 4-NA > 2-NA > 3-NA. On the basis of this study, it is found that percents of the binding of nitroanilines to BSA are almost no relative to the concentrations of nitroanilines, and correlation between K(A) and logK (ow) is disclosed. In the meantime, relationships between the combination of nitroanilines with BSA and toxicological implications were also discussed. In addition, synchronous fluorescence method was used to study the interaction mechanisms between nitroanilines and BSA, and energy transfer distances from BSA to nitroanilines were estimated based on the Förster's non-radiation energy transfer theory. The results suggest that the binding site for nitroanilines on BSA is close to the sub-domain IIA where Trp 214 is located. | lld:pubmed |
