重楼皂苷VI | 55916-51-3

• 物质功能分类: 生物化工 - 提取物
• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 类固醇和类固醇衍生物
• 中文名称: 重楼皂苷VI
• 中文别名: 重楼皂苷 VI
• 英文名称: polyphyllin VI
• 英文别名: pennogenin 3-O-α-L-rhamnopyranosyl-(1→2)-β-D-glucopyranoside；paris saponin VI；pennogenin 3-O-α-L-rhamnopyranosyl-(1-> 2)-β-D-glucopyranoside；(25R)-spirost-5-en-3β,17α-diol 3-O-α-L-rhamnopyranosyl-(1→2)-β-D-glucopyranoside；(2S,3R,4R,5R,6S)-2-[(2R,3R,4S,5S,6R)-4,5-dihydroxy-6-(hydroxymethyl)-2-[(1R,2S,4S,5'R,6R,7S,8S,9S,12S,13R,16S)-8-hydroxy-5',7,9,13-tetramethylspiro[5-oxapentacyclo[10.8.0.02,9.04,8.013,18]icos-18-ene-6,2'-oxane]-16-yl]oxyoxan-3-yl]oxy-6-methyloxane-3,4,5-triol
• CAS: 55916-51-3
• 化学式: C₃₉H₆₂O₁₃
• 分子量: 738.913
• InChiKey: WHWWQGPCTUQCMN-JDDKMXSSSA-N

物化性质

• 熔点：
  216-220°C
• 沸点：
  871.2±65.0 °C(Predicted)
• 密度：
  1.38
• 溶解度：
  可溶于DMSO（少许）、甲醇（少许）

计算性质

• 辛醇/水分配系数(LogP)：
  1.7
• 重原子数：
  52
• 可旋转键数：
  5
• 环数：
  8.0
• sp3杂化的碳原子比例：
  0.95
• 拓扑面积：
  197
• 氢给体数：
  7
• 氢受体数：
  13

制备方法与用途

化学性质
白色结晶粉末，易溶于甲醇和水，来源于重楼。

用途
重楼皂苷Ⅵ具有抗炎、抗肿瘤、抗病毒、降低胆固醇及降血压等多种作用，并可用于含量测定、鉴定及药理实验等。

药理药效
重楼皂苷Ⅵ还表现出止血、祛痰和抑菌、镇静镇痛、抗早孕杀灭精子以及抗细胞毒等多种作用。临床应用中，它用于治疗功能性子宫出血、神经性皮炎、外科炎症以及肿瘤等疾病，均能取得显著疗效。

反应信息

• 作为反应物：
  描述：

  重楼皂苷VI 在 Curvularia lunata 3.4381 作用下， 以 水 为溶剂， 以16 mg的产率得到pennogenin 3-O-β-D-glucopyranoside
  参考文献：
  名称：

  弯孢菌对甾体皂苷的微生物转化

  摘要：

  皂苷的微生物转化I（化合物我），皂苷III（化合物II），皂苷V（化合物III）和皂苷VI（化合物IV通过）弯孢菌为它们相应的subsaponins，例如，薯蓣皂苷配基-3- ö -α- 1-阿拉伯呋喃糖基（1→4）-β-d-吡喃葡萄糖苷（化合物V），薯os皂苷元3- O -α-l-鼠李糖吡喃糖基（1→4）-β-d-吡喃葡萄糖苷（化合物VI），薯os皂苷元-3- O - β -d-吡喃葡萄糖苷（化合物VII）和Pennogenin-3- O - β -d-吡喃葡萄糖苷（化合物VIII）），在本文中进行了研究。弯孢弯曲菌能够水解通过1→2 C–键与甾体皂苷在C-3位糖残基连接的末端鼠李糖基，具有很高的活性和区域选择性。

  DOI：

  10.1016/j.tet.2005.08.115

文献信息

• The substrate specificity of a glucoamylase with steroidal saponin-rhamnosidase activity from Curvularia lunata
  作者：Bing Feng、Li-ping Kang、Bai-ping Ma、Bo Quan、Wen-bin Zhou、Yong-ze Wang、Yu Zhao、Yi-xun Liu、Sheng-qi Wang

  DOI：10.1016/j.tet.2007.04.076

  日期：2007.7

  In previous work, we studied and reported that an enzyme from Curvularia lunata 3.4381 had the novel specificity to hydrolyze the terminal rhamnosyl at C-3 position of steroidal saponin and obtained four transformed products; the enzyme was purified and ascertained as glucoamylase (EC 3.2.1.3 GA). In this work, the enzyme exhibiting steroidal saponin-rhamnosidase activity was systematically studied on 21 steroidal saponins and 6 ginsenosides. The results showed that the alpha-1,2-linked end-rhamnosyl residues at C-3 position of steroidal saponins could be hydrolyzed to corresponding secondary steroidal saponins, among which 18 compounds were isolated and identified, including 3 new secondary compounds. For the furostanosides having glucosyl residues at the C-26 position, hydrolysis occurred first at end- rhamnosyl at C-3 position to produce secondary furostanosides. The reaction of hydrolyzing glucosyl at C-26 position depended considerably on longer reaction times yielding the corresponding secondary spirostanosides ( without rhamnosyl and glucosyl residues). The enzyme had the strict specificity for the terminal alpha-1,2-linked rhamnosyl residues of linear chain, or the terminal alpha-1,2-linked rhamnosyl residues with branched chain of 1,4-linked glycosyl residues of sugar chain at C-3 position of steroidal saponins, it was not specific for different aglycones, different glycons, and the number of glycon of sugar chain of steroidal saponin. The end- rhamnosyl of ginsenosides and p-nitrophenyl-a-L-rhamnopyranoside (pNPR) could not be hydrolyzed by the enzyme from C. lunata. (c) 2007 Elsevier Ltd. All rights reserved.