The Binding of Four Licorice Flavonoids to Bovine Serum Albumin by Multi-Spectroscopic and Molecular Docking Methods: Structure-Affinity Relationship | |
Hou J(侯嘉)1,2; Liang Q(梁卿)1; Shao SJ(邵士俊)1 | |
刊名 | Journal of Applied Spectroscopy |
2017 | |
卷号 | 84期号:1页码:177-187 |
关键词 | licorice flavonoids fluorescence emission spectrometry molecular docking bovine serum albumin |
ISSN号 | 0021-9037 |
通讯作者 | 邵士俊 |
英文摘要 | Flavanones are the main compound of licorice, and the C'-4 position substitution is a significant structural feature for their biological activity. The ability of three selected flavanones (liquiritigenin, liquiritin, and liquiritin apioside) bearing different substituents (hydroxyl groups, glucose, and glucose–apiose sugar moiety) at the C'-4 position and a chalcone ( isoliquiritigenin, an isomer of liquiritigenin) to bind bovine serum albumin (BSA) was studied by multispectroscopic and molecular docking methods under physiological conditions. The binding mechanism of fl avonoids to BSA can be explained by the formation of a flavonoids–BSA complex, and the binding affinity is the strongest for isoliquiritigenin, followed by liquiritin apioside, liquiritin, and liquiritigenin. The thermodynamic analysis and the molecular docking indicated that the interaction between flavonoids and BSA was dominated by the hydrophobic force and hydrogen bonds. The competitive experiments as well as the molecular docking results suggested the most possible binding site of licorice flavonoids on BSA at subdomain IIA. These results revealed that the basic skeleton structure and the substituents at the C'-4 position of flavanones significantly affect the structure–affinity relationships of the licorice flavonoid binding to BSA. |
学科主题 | 分析化学与药物化学 |
收录类别 | SCI |
语种 | 英语 |
WOS记录号 | WOS:000400076100031 |
内容类型 | 期刊论文 |
源URL | [http://210.77.64.217/handle/362003/22183] |
专题 | 兰州化学物理研究所_中科院西北特色植物资源化学重点实验室/甘肃省天然药物重点实验室 |
作者单位 | 1.Chinese Acad Sci, Lanzhou Inst Chem Phys, Lanzhou 730000, Peoples R China 2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China |
推荐引用方式 GB/T 7714 | Hou J,Liang Q,Shao SJ. The Binding of Four Licorice Flavonoids to Bovine Serum Albumin by Multi-Spectroscopic and Molecular Docking Methods: Structure-Affinity Relationship[J]. Journal of Applied Spectroscopy,2017,84(1):177-187. |
APA | Hou J,Liang Q,&Shao SJ.(2017).The Binding of Four Licorice Flavonoids to Bovine Serum Albumin by Multi-Spectroscopic and Molecular Docking Methods: Structure-Affinity Relationship.Journal of Applied Spectroscopy,84(1),177-187. |
MLA | Hou J,et al."The Binding of Four Licorice Flavonoids to Bovine Serum Albumin by Multi-Spectroscopic and Molecular Docking Methods: Structure-Affinity Relationship".Journal of Applied Spectroscopy 84.1(2017):177-187. |
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