Combined multispectroscopic and molecular docking investigation on the interaction between delphinidin-3-O-glucoside and bovine serum albumin.
Combined multispectroscopic and molecular docking investigation on the interaction between delphinidin-3-O-glucoside and bovine serum albumin.
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DOI：
10.1002/bio.2704
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发表时间：
2015-02
期刊：
影响因子：
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通讯作者：
Huijun Zuo;L. Tang;Shu Li;Junwei Huang
中科院分区：
文献类型：
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作者：
Huijun Zuo;L. Tang;Shu Li;Junwei Huang
花青素是黄酮类植物色素中的一种，对健康有特殊的好处。用荧光光谱、同步荧光光谱、三维荧光光谱、紫外-可见吸收光谱、圆二色谱和分子模拟等方法研究了飞蝶素-3-O-葡萄糖苷(D3G)与牛血清白蛋白(BSA)的相互作用。D3G通过静态猝灭有效地猝灭了BSA的内源荧光。测定了结合位点数和结合常数Ka，氢键和范德华力在稳定D3G-BSA络合物中起主要作用。根据Förster理论，得到给体与受体之间的距离r=2.81 nm。此外，还讨论了pH和金属离子对结合常数的影响。同步荧光、三维荧光和圆二色谱研究结果表明，D3G的加入改变了蛋白质的二级结构，蛋白质的α-螺旋含量从56.1%下降到52.4%。此外，位点标记竞争实验和分子模拟研究表明，D3G可以与BSA的I位结合，该位点位于IIA亚区的大疏水空腔中。
Anthocyanin is one of the flavonoid phytopigments with specific health benefits. The interaction between delphinidin-3-O-glucoside (D3G) and bovine serum albumin (BSA) was investigated by fluorescence spectroscopy, synchronous fluorescence spectroscopy, three-dimensional fluorescence spectroscopy, ultraviolet-visible absorption spectroscopy, circular dichroism spectroscopy and molecular modeling. D3G effectively quenched the intrinsic fluorescence of BSA via static quenching. The number of binding sites and binding constant Ka were determined, and the hydrogen bonds and van der Waals forces played major roles in stabilizing the D3G-BSA complex. The distance r between donor and acceptor was obtained as 2.81 nm according to Förster's theory. In addition, the effects of pH and metal ions on the binding constants were discussed. The results studied by synchronous fluorescence, three-dimensional fluorescence and circular dichroism experiments indicated that the secondary structures of the protein has been changed by the addition of D3G and the α-helix content of BSA decreased (from 56.1% to 52.4%). Furthermore, the study of site marker competitive experiments and molecular modeling indicated that D3G could bind to site I of BSA, which was in the large hydrophobic cavity of subdomain IIA.