In the present study the binding of diversin (DIV), a prenylated coumarin isolated from Ferula diversivittata, to bovine serum albumin (BSA) was investigated using surface plasmon resonance (SPR), spectrofluorimetry, and molecular docking approaches. Following the activation of carboxylic groups, via NHS/EDC, BSA was immobilized on the carboxymethyl dextran (CMD) hydrogel coated Au sensor, and was used for real-time monitoring of the interactions between DIV and BSA. KD value of DIV binding to BSA increased with increasing temperature, confirmed that the affinity between BSA and DIV decreases with rising temperature. In addition, the fluorescence and synchronous fluorescence spectroscopic data revealed that the intrinsic emission intensity of BSA was quenched via a dynamic mechanism. In addition, the micro-region around BSA tyrosine residue was changed upon interaction with DIV. The thermodynamic parameter findings suggested that the hydrophobic interactions were dominant in the binding and formation of the BSA and DIV complex. The molecular docking outputs indicated that there is only one binding site on BSA for DIV, in agreement with experimental data, and DIV bind BSA in subdomain IB.

中文翻译：

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牛血清白蛋白与天然香豆素多样化蛋白相互作用的表面等离子体共振，荧光和分子对接研究。

在本研究中，使用表面等离振子共振（SPR），荧光光谱和分子对接方法研究了发散酶（DIV）（一种从杂草费拉分离的异戊烯化香豆素）与牛血清白蛋白（BSA）的结合。羧基活化后，通过NHS / EDC，将BSA固定在羧甲基葡聚糖（CMD）水凝胶包被的Au传感器上，并用于实时监测DIV和BSA之间的相互作用。DIV与BSA结合的KD值随温度升高而增加，证实BSA与DIV之间的亲和力随温度升高而降低。另外，荧光和同步荧光光谱数据表明，BSA的固有发射强度通过动力学机制被淬灭。此外，与DIV相互作用后，BSA酪氨酸残基周围的微区发生了变化。热力学参数发现表明，疏水性相互作用在BSA和DIV配合物的结合和形成中起主要作用。分子对接的输出表明，与实验数据一致，BSA上只有一个DIV结合位点，DIV结合BSA子域中的BSA。