The Binding of Four Licorice Flavonoids to Bovine Serum Albumin by Multi-Spectroscopic and Molecular Docking Methods: Structure-Affinity Relationship | |
Department | 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 |
Hou J(侯嘉)1,2; Liang Q(梁卿)1; Shao SJ(邵士俊)1; Shao SJ(邵士俊) | |
2017 | |
Source Publication | Journal of Applied Spectroscopy |
ISSN | 0021-9037 |
Volume | 84Issue:1Pages:177-187 |
Abstract | 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. |
Keyword | Licorice Flavonoids Fluorescence Emission Spectrometry Molecular Docking Bovine Serum Albumin |
Subject Area | 分析化学与药物化学 |
DOI | 10.1007/s10812-017-0447-x |
Indexed By | SCI |
If | 0.572 |
Language | 英语 |
Funding Project | 药物分子识别研究组 |
compositor | 第一作者单位 |
Citation statistics | |
Document Type | 期刊论文 |
Identifier | http://ir.licp.cn/handle/362003/22183 |
Collection | 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 |
Corresponding Author | Shao SJ(邵士俊) |
Affiliation | 1.Chinese Acad Sci, Lanzhou Inst Chem Phys, Lanzhou 730000, Peoples R China 2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China |
Recommended Citation GB/T 7714 | Hou J,Liang Q,Shao SJ,et al. 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,&邵士俊.(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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