Binding of a binaphthoquinone derivative namely, 5a,5b-dimethyldibenzo[b,h]biphenylene-5,6,11,12(5aH,5bH,11aH,11bH)-tetraone (L, C22H16O4) with bovine serum albumin (BSA) and human serum albumin (HSA) have been examined by using fluorescence spectroscopy. The fluorescence emission of the L is quenched upon addition of L to a solution of BSA or that of HSA, but the BSA has shown a higher affinity towards L over the HSA protein. A molecular docking study is also performed to suggest the sites of BSA for weak interactions to bind the L. The docking analysis, has revealed the N-H•••O hydrogen bonds of L with different amino acid residues. The L is located at about 7.7Å away from the Trp-213 which is the fluorescent unit of the BSA suggesting the role of environment of the tryptophan residue to be an important to have changed the emission intensities.

中文翻译：

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联萘醌衍生物与血清白蛋白结合的荧光光谱研究

联萘醌衍生物，即 5a,5b-二甲基二苯并[b,h]联亚苯基-5,6,11,12(5aH,5bH,11aH,11bH)-四酮 (L, C22H16O4) 与牛血清白蛋白 (BSA) 和人血清白蛋白 (HSA) 已通过荧光光谱法进行了检测。在向 BSA 或 HSA 溶液中加入 L 后，L 的荧光发射被淬灭，但 BSA 对 L 的亲和力高于 HSA 蛋白。还进行了分子对接研究，以表明 BSA 与 L 结合的弱相互作用位点。对接分析揭示了 L 与不同氨基酸残基的 NH•••O 氢键。L 距离 Trp-213 约 7.7Å，Trp-213 是 BSA 的荧光单位，表明色氨酸残基的环境对改变发射强度很重要。