重楼皂苷 VII | 68124-04-9

• 物质功能分类: 天然产物 - 甾体化合物
• 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 VII
• 中文别名: 重楼皂苷VII
• 英文名称: paris saponin VII
• 英文别名: polyphyllin VII；pennogenin 3-O-α-L-rhamnopyranosyl-(1-> 4)-α-L-rhamnopyranosyl-(1-> 4)-[α-L-rhamnopyranosyl-(1-> 2)]-β-D-glucopyranoside；pennogenin 3-O-α-L-rhamnopyranosyl-(1→4)-α-L-rhamnopyranosyl-(1→4)-[α-L-rhamnopyranosyl-(1→2)]-β-D-glucopyranoside；pennogenin tetraglycoside；chonglou saponin VII；(2S,3R,4R,5R,6S)-2-[(2S,3R,4S,5R,6S)-4,5-dihydroxy-6-[(2R,3S,4S,5R,6R)-4-hydroxy-2-(hydroxymethyl)-6-[(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]oxy-5-[(2S,3R,4R,5R,6S)-3,4,5-trihydroxy-6-methyloxan-2-yl]oxyoxan-3-yl]oxy-2-methyloxan-3-yl]oxy-6-methyloxane-3,4,5-triol
• CAS: 68124-04-9
• 化学式: C₅₁H₈₂O₂₁
• 分子量: 1031.2
• InChiKey: FBFJAXUYHGSVFN-IYUYFXHASA-N

物化性质

• 熔点：
  243-245 °C (decomp)
• 密度：
  1.45±0.1 g/cm3(Predicted)
• 溶解度：
  溶于甲醇；

计算性质

• 辛醇/水分配系数(LogP)：
  -1
• 重原子数：
  72
• 可旋转键数：
  9
• 环数：
  10.0
• sp3杂化的碳原子比例：
  0.96
• 拓扑面积：
  315
• 氢给体数：
  11
• 氢受体数：
  21

安全信息

• 海关编码：
  29329990
• WGK Germany：
  3

制备方法与用途

生物活性

Paris saponin VII (Chonglou Saponin VII) 是从延龄草（Trillium tschonoskii Maxim）的根和根茎中分离出的一种甾体皂苷。研究表明，它通过抑制 Akt/p38 MAPK 和 P-gp 诱导 K562/ADR 细胞凋亡。Paris saponin VII 能够降低线粒体膜电位、上调 Bax 和细胞色素 c 的表达，并下调 Bcl-2、caspase-9、caspase-3、PARP-1 和 p-Akt 的蛋白水平，从而在 K562/ADR 细胞中诱导强烈的自噬，有助于白血病的研究。

目标
Akt
p38
Bcl-2
Caspase-9
Caspase-3
PARP-1

体外研究

Paris saponin VII (Chonglou Saponin VII) 对多柔比星耐药的人类白血病细胞株 K562/ADR 的生长表现出剂量依赖性的抑制作用。它通过 G0/G1 期的细胞周期阻滞显著抑制细胞增殖。

体内研究

Paris saponin VII (Chonglou Saponin VII) （静脉注射）在裸鼠 MCF-7/ADR 异种移植模型中显著增强了多柔比星的抗癌效果。

化学性质

白色结晶粉末，可溶于甲醇、乙醇、DMSO 等有机溶剂，来源于重楼。

用途

重楼皂苷Ⅶ具有抗炎、抗肿瘤、抗病毒和降低胆固醇、降血压等多种作用。可用于含量测定/鉴定/药理实验等。其药理药效包括止血、祛痰和抑菌、镇静镇痛、抗早孕杀灭精子、抗细胞毒等，临床上用于治疗功能性子宫出血、神经性皮炎、外科炎症及肿瘤等，均显示出显著疗效。

反应信息

• 作为反应物：
  描述：

  重楼皂苷 VII 在 Curvularia lunata 3.4381 1,4-α-D-glucan glucohydrolase 作用下， 以 phosphate buffer 为溶剂， 反应 6.0h， 生成 pennogenin 3-O-α-L-rhamnopyranosyl(1→4)-α-L-rhamnopyranosyl(1→4)-β-D-glucopyranoside
  参考文献：
  名称：

  The substrate specificity of a glucoamylase with steroidal saponin-rhamnosidase activity from Curvularia lunata

  摘要：

  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.

  DOI：

  10.1016/j.tet.2007.04.076

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.