Probing the interaction of ellagic acid with human serum albumin: A fluorescence spectroscopic study
Probing the interaction of ellagic acid with human serum albumin: A fluorescence spectroscopic study
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DOI：
10.1016/j.jphotochem.2007.05.018
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发表时间：
2007-12-15
影响因子：
4.3
通讯作者：
Banerjee, Rintu
中科院分区：
文献类型：
--
作者：
Nanda, Ranjan Kumar;Sarkar, Nilmoni;Banerjee, Rintu
人血清白蛋白（HSA）是一种主要的血浆蛋白，携带药物分子到达人体的靶点。鞣花酸（EA）是由鞣花单宁衍生而来的，由于其独特的药理学性质而作为药物发挥着重要的作用。在类似于人体生理条件下，采用荧光光谱技术研究了EA与HSA之间的相互作用。结合参数已通过荧光猝灭法进行了评估。结果表明，EA与HSA相互作用时，HSA荧光猝灭的机理是EA与HSA形成复合物。热力学参数Δ H和Δ S分别为-17.32 kJ/mol和34.91 J/mol/K，证明了氢键和疏水键等弱相互作用力的参与.分子对接研究表明EA与HSA分子间存在氢键距离。根据Forster的非辐射能量转移理论获得供体（HSA）和受体（EA）之间的距离r，并且发现为1.96nm。本研究将对药物在人体生理条件下转运过程中的稳定性和靶点释放效率的评价提供见解。
Human serum albumin (HSA) is a principal plasma protein, carries the drug molecules to target sites in human body. Ellagic acid (EA) derived from ellagitannins plays an important role as a drug because of its unique pharmacological properties. The interactions between EA and HSA were studied by fluorescence spectroscopic techniques under similar to human physiologic conditions. The binding parameters have been evaluated by fluorescence quenching methods. The results proved the mechanism of fluorescence quenching of HSA while interacting with EA is due to the formation of EA - HSA complex formation. The thermodynamic parameters like Delta H and Delta S were calculated to be - 17.32 kJ/mol and 34.91 J/mol/K, respectively, which proves the involvement of weak interactive forces like hydrogen and hydrophobic bonds during the interaction. Molecular docking study shows hydrogen-bonding distance between EA and HSA molecule. The distance r between donor (HSA) and acceptor (EA) was obtained according to the Forster's theory of non-radiative energy transfer and found to be 1.96 nm. This study will give an insight on the evaluation of the drug stability during transport and releasing efficiency at the target site in human physiological conditions.