Spectroscopic analysis on structure-affinity relationship in the interactions of different oleanane-type triterpenoids with bovine serum albumin
文献类型：期刊论文
| 作者 | Hou J(侯嘉)1,2,3 ; Wang ZZ(王振忠)1,2,3; Yue Y(岳莹)1,2; Li Q(李欠)1,2; Shao SJ(邵士俊)1,2
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| 刊名 | Luminescence
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| 出版日期 | 2015 |
| 卷号 | 30期号:6页码:780-789 |
| 关键词 | oleanane-type triterpenoids binding affinity fluorescence bovine serum albumin |
| ISSN号 | 1522-7235 |
| 通讯作者 | 邵士俊 |
| 英文摘要 | Oleanane-type triterpenoids serve as an important group of plant secondary metabolites with a variety of biological activities and the C-3 position substitution pattern is a significant structural feature for their biological activities. Three selected oleanane-type triterpenoids (glycyrrhizin, glycyrrhetinic acid, and carbenoxolone) bearing different substituents (glucuronic acid dimer, hydroxyl, and succinyl groups) at the C-3 position were studied for their affinities to bind bovine serum albumin (BSA) by steady-state fluorescence, synchronous, three-dimensional fluorescence and ultraviolet–visible (UV–vis) absorption spectra. The binding mechanism of the triterpenoids to BSA is due to the formation of the triterpenoids–BSA complex and the binding affinity is strongest for carbenoxolone and ranked in the order carbenoxolone > glycyrrhetinic acid > glycyrrhizin. The thermodynamic parameters calculated at different temperatures showed that triterpenoids binding to BSA primarily depended on hydrophobic interaction and hydrogen bonding. The distance between the bound triterpenoid and BSA was determined on the basis of the Förster's energy transfer theory. Displacement experiments using phenylbutazone and ibuprofen showed the binding site of triterpenoids on BSA at subdomain IIA (Sudlow's site I). The effect of triterpenoids on BSA conformation was analyzed by UV–vis absorption, and synchronous and three-dimensional fluorescence spectra. These results revealed that the C-3 position substitution pattern significantly affects the structure–affinity relationships of oleanane-type triterpenoid binding to BSA and further affects the bioavailability of triterpenoids in the blood circulatory system. |
| 学科主题 | 分析化学与药物化学 |
| 收录类别 | SCI |
| 资助信息 | the major goals/breakthroughs program of 'One-Three-Five' Strategic Planning of Lanzhou Institute of Chemical Physics, Chinese Academy of Sciences |
| 语种 | 英语 |
| WOS记录号 | WOS:000364639900012 |
| 源URL | [http://210.77.64.217/handle/362003/19070]  |
| 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, Key Lab Chem Northwestern Plant Resources, Lanzhou 730000, Peoples R China 2.Chinese Acad Sci, Lanzhou Inst Chem Phys, Key Lab Nat Med Gansu Prov, Lanzhou 730000, Peoples R China 3.Univ Chinese Acad Sci, Beijing 100049, Peoples R China |
| 推荐引用方式 GB/T 7714 | Hou J,Wang ZZ,Yue Y,et al. Spectroscopic analysis on structure-affinity relationship in the interactions of different oleanane-type triterpenoids with bovine serum albumin[J]. Luminescence,2015,30(6):780-789. |
| APA | Hou J,Wang ZZ,Yue Y,Li Q,&Shao SJ.(2015).Spectroscopic analysis on structure-affinity relationship in the interactions of different oleanane-type triterpenoids with bovine serum albumin.Luminescence,30(6),780-789. |
| MLA | Hou J,et al."Spectroscopic analysis on structure-affinity relationship in the interactions of different oleanane-type triterpenoids with bovine serum albumin".Luminescence 30.6(2015):780-789. |
入库方式： OAI收割
来源：兰州化学物理研究所
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