Studies on the interaction between 1-hexylcarbamoyl-5-fluorouracil and bovine serum albumin
Studies on the interaction between 1-hexylcarbamoyl-5-fluorouracil and bovine serum albumin
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DOI：
10.1016/j.molstruc.2004.11.062
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发表时间：
2005-03-14
影响因子：
3.8
通讯作者：
Qu, SS
中科院分区：
文献类型：
--
作者：
Hu, YJ;Liu, Y;Qu, SS
采用荧光光谱法、圆二色光谱（CD）和紫外 - 可见吸收光谱等光谱方法研究了抗肿瘤药物1 - 己基氨甲酰基 - 5 - 氟尿嘧啶（卡莫氟）与牛血清白蛋白（BSA）之间的相互作用。探讨了卡莫氟对BSA荧光的猝灭机制。通过荧光猝灭法测定了结合位点的数目n和表观结合常数Kb。计算了不同温度下的热力学参数ΔH、ΔG、ΔS，结果表明结合反应主要是熵驱动的，并且疏水作用力在反应中起主要作用。根据福斯特非辐射能量转移理论得到了供体（BSA）和受体（卡莫氟）之间的距离r。利用圆二色光谱研究了加入卡莫氟后BSA分子的结构变化，结果表明在卡莫氟存在的情况下，BSA分子的二级结构发生了改变。（c）2004爱思唯尔公司。版权所有。
The interaction between anti-tumor drug, 1-hexylcarbamoyl-5-fluorouracil (Cannofur), and bovine serum albumin (BSA) were studied by spectroscopic methods including fluorescence spectroscopy, circular dichroism (CD) and UV-Visible absorption spectrum. The quenching mechanism of fluorescence of BSA by Carmofur was discussed. The number of binding sites n and apparent binding constant Kb was measured by fluorescence quenching method. The thermodynamic parameters Delta H, Delta G, Delta S at different temperatures were calculated and the results indicate the binding reaction is mainly entropy-driven and hydrophobic forces played major role in the reaction. The distance r between donor (BSA) and acceptor (Carmofur) was obtained according to Forster theory of non-radiation energy transfer. CD spectrum were used to investigate the structural change of BSA molecules with addition of Carmofur, the result indicates that the secondary structure of BSA molecules is changed in the presence of Carmofur. (c) 2004 Elsevier B.V. All rights reserved.