Interaction of cyclodextrins with human and bovine serum albumins: A combined spectroscopic and computational investigation
Interaction of cyclodextrins with human and bovine serum albumins: A combined spectroscopic and computational investigation
复制标题
DOI：
10.1007/s12039-014-0652-6
复制
发表时间：
2014-07-01
影响因子：
1.7
通讯作者：
Chattopadhyay, Nitin
中科院分区：
文献类型：
--
作者：
Ghosh, Saptarshi;Paul, Bijan Kumar;Chattopadhyay, Nitin
利用稳态荧光光谱、时间分辨荧光光谱、圆二色谱和分子对接模拟技术研究了环糊精（CD）与两种最丰富的蛋白质，即人血清白蛋白（HSA）和牛血清白蛋白（BSA）的相互作用。研究表明，三种CD对血清白蛋白的荧光和荧光寿命的影响不同。然而，荧光各向异性和圆二色性不受影响。根据它们的大小，不同的CD在不同的位置与血清白蛋白结合，导致蛋白质光谱行为的变化。对接研究提示了三种CD与蛋白质的可能结合位点。结合实验和计算的研究表明，足够高浓度的CD导致这些运输蛋白的刚性结构松动，虽然它们的二级结构保持完整。因此，从结构的角度来看，发现CD对血清蛋白是安全的。
Interaction of cyclodextrins (CDs) with the two most abundant proteins, namely human serum albumin (HSA) and bovine serum albumin (BSA), has been investigated using steady-state and time-resolved fluorometric techniques, circular dichroism measurements and molecular docking simulation. The study reveals that the three CDs interact differently on the fluorescence and fluorescence lifetimes of the serum albumins. However, fluorescence anisotropy and circular dichroism are not affected. Depending on their size, different CDs bind to the serum albumins in different positions, resulting in changes in the spectral behaviour of the proteins. Docking study suggests the probable binding sites of the three CDs with the proteins. Combined experimental and computational studies imply that sufficiently high concentration of CDs causes loosening of the rigid structures of these transport proteins, although their secondary structures remain intact. Thus, CDs are found to be safe for the serum proteins from the structural point of view.