Abstract：Under the simulative human physiological condition, the interaction of sulfamethoxazole (SMZ) and bovine serum albumin (BSA) with or without Fe3＋ was studied by fluorescence spectra, ultra-violet absorption spectra and FT-IR spectra. The results show that both the quenching mechanism of the intrinsic fluorescence of BSA by sulfamethoxazole with or without Fe3＋ is a static fluorescence quenching procedure. It was found that in the presence of Fe3＋, the binding constant of SMZ and BSA increased and the main binding force between SMZ and BSA was changed from hydrophobic force to hydrogen bonds and van der Waals force. From the synchronous fluorescence and three-dimensional fluorescence spectra, it was found that SMZ change the conformation of BSA. BSA may form a new disordered structure, but the capability of SMZ changing the structure of the BSA was not enhanced in the presence of Fe3＋. Based on fluorescence resonance energy transfer (FRET), the distances (r) between donor (BSA) and acceptor (SMZ and Fe3＋-SMZ) were obtained. According to FT-IR, the secondary structure of BSA changed when Fe3＋ and SMZ were added.
余燕敏, 冯金朝, 刘颖. Fe3＋存在下磺胺甲恶唑与牛血清白蛋白相互作用的光谱学研究[J]. 化学学报, 2011, 69(02): 190-198.
YU Yan-Min, FENG Jin-Chao, LIU Ying. Spectroscopic Study of the Interaction between Sulfamethoxazole and Bovine Serum Albumin in the Presence of Fe3＋. Acta Chimica Sinica, 2011, 69(02): 190-198.