Stake Laboratory of Food Science and Technology, Department of Chemistry, Nanchang University, Nanchang, Jiangxi 330031, China.
Spectrochim Acta A Mol Biomol Spectrosc. 2011 Jan;78(1):443-8. doi: 10.1016/j.saa.2010.11.007. Epub 2010 Nov 23.
Interaction of chlorotetracycline (CTC) with bovine serum albumin (BSA) was investigated under simulated physiological conditions by spectroscopy with the aid of multivariate curve resolution-alternating least squares (MCR-ALS). Eosin Y was selected as an alternative site I marker on the BSA to study the above molecular interaction. The binding of Eosin Y and CTC to BSA showed that CTC was displaced from CTC-BSA complex by Eosin Y, and Eosin Y-BSA complex was formed. However, the recorded fluorescence spectra of Eosin Y and Eosin Y-BSA overlapped and MCR-ALS was applied to resolve the two-way fluorescence spectra. From the resolved equilibrium concentration profiles, it was observed that Eosin Y competed with CTC in the binding process with BSA; it was also shown that the binding site of CTC on BSA was site I, and this was further confirmed by the fluorescence polarization method. Compared with some common site I markers for BSA, the fluorescence and UV-vis spectral shapes of the Eosin Y-BSA complex were quite different from that of Eosin Y, and this feature facilitated the investigation of the small molecule-BSA interaction.
在模拟生理条件下，通过光谱法并借助多变量曲线分辨-交替最小二乘法（MCR-ALS）研究了氯四环素（CTC）与牛血清白蛋白（BSA）的相互作用。曙红 Y 被选为 BSA 上的替代 I 型结合位标记物，以研究上述分子相互作用。曙红 Y 和 CTC 与 BSA 的结合表明，CTC 被曙红 Y 从 CTC-BSA 复合物中置换出来，并形成了曙红 Y-BSA 复合物。然而，曙红 Y 和曙红 Y-BSA 的记录荧光光谱重叠，因此应用 MCR-ALS 来解析双向荧光光谱。从解析的平衡浓度曲线可以看出，曙红 Y 在与 BSA 结合的过程中与 CTC 竞争；还表明 CTC 在 BSA 上的结合位点是 I 型结合位，这通过荧光偏振法进一步得到了证实。与 BSA 的一些常见 I 型结合位标记物相比，曙红 Y-BSA 复合物的荧光和紫外-可见光谱形状与曙红 Y 有很大的不同，这一特点有助于研究小分子-BSA 相互作用。
