Abstract We investigated quantum-chemical characteristics of gemcitabine (GEM), fluorescence quenching of bovine serum albumin (BSA) in aqueous solutions with the presence of GEM. The static mechanism of the complex formation with moderate binding constant () and number of binding sites was established to take place in the solutions. Studying the energy transfer efficiency we found that molecules of GEM are localized near polar charged amino acid residues of the protein biomolecules at the average distance The calculated thermodynamic parameters demonstrate the presence of both hydrogen bonds and hydrophobic interaction between the protein and ligand molecules.

中文翻译：

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牛血清白蛋白与抗癌药吉西他滨相互作用的机制

摘要 我们研究了吉西他滨 (GEM) 的量子化学特性，以及 GEM 存在下水溶液中牛血清白蛋白 (BSA) 的荧光猝灭。在溶液中建立了具有中等结合常数 () 和结合位点数量的复合物形成的静态机制。研究能量转移效率，我们发现 GEM 分子位于蛋白质生物分子的极性带电氨基酸残基附近，平均距离。计算的热力学参数证明蛋白质和配体分子之间存在氢键和疏水相互作用。