摘要
应用三维荧光光谱和三维荧光偏振光谱研究了数种喹诺酮药物与牛血清白蛋白(BSA)分子间的相互作用。由三维荧光(偏振)光谱得到的指纹信息说明了喹诺酮药物与BSA结合反应对BSA分子构象的影响。通过研究喹诺酮药物发生相互作用前后BSA荧光偏振度及各向异性的变化,定量说明了喹诺酮药物-BSA所发生的结合反应。
The conformation of bovine serum albumin （BSA） conformation changes after the binding interaction with several in Tris-HC1 buffer solution and its fluoroquinolone drugs were studied by using three-dimensional fluorescence spectrometry （TDFS）, such as three-dimensional fluorescence （TDF） spectra and three-dimensional fluorescence polarization （TDFP） spectra with tryptophan residues in protein molecules as an intrinsic fluorescence probe. The results show that the microenvironment of tryptophan residues of BSA can be directly indicated and the conformation changes can be clarified by the fingerprinting characteristics. Meantime, the non-covalent bond interaction of fluoroquinolone with BSA has been quantitatively explained by calculating of fluorescence polarization P and anisotropy r.
出处
《分析科学学报》
CAS
CSCD
2007年第4期405-409,共5页
Journal of Analytical Science
关键词
牛血清白蛋白
三维荧光光谱
喹诺酮药物
蛋白质构象
Bovine serum albumin
Three-dimensional fluorescence spectroscopy
Quinolone
Protein conformation
