[(3S,3aR,4S,6S,6aR,7S,8S,9bS)-3,4,6-tri(butanoyloxy)-3a-hydroxy-3,6,9-trimethyl-8-[(Z)-2-methylbut-2-enoyl]oxy-2-oxo-4,5,6a,7,8,9b-hexahydroazuleno[4,5-b]furan-7-yl] octanoate | 1246196-66-6

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: [(3S,3aR,4S,6S,6aR,7S,8S,9bS)-3,4,6-tri(butanoyloxy)-3a-hydroxy-3,6,9-trimethyl-8-[(Z)-2-methylbut-2-enoyl]oxy-2-oxo-4,5,6a,7,8,9b-hexahydroazuleno[4,5-b]furan-7-yl] octanoate
• CAS: 1246196-66-6
• 化学式: C₄₀H₆₀O₁₃
• 分子量: 748.909
• InChiKey: HNPKZMPFTORRQD-NGBXUZPPSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.8
• 重原子数：
  53
• 可旋转键数：
  23
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.75
• 拓扑面积：
  178
• 氢给体数：
  1
• 氢受体数：
  13

反应信息

• 作为产物：
  描述：

  isopropenyl butyrate 、 [(1S,4S,5S,6R,7S,9S,13S,16R)-7-butanoyloxy-16-hydroxy-3,7,11,11,13-pentamethyl-4-[(Z)-2-methylbut-2-enoyl]oxy-14-oxo-10,12,15-trioxatetracyclo[7.6.1.02,6.013,16]hexadec-2-en-5-yl] octanoate 在 对甲苯磺酸 作用下， 反应 1.75h， 以16%的产率得到(3S,3aR,4S,6S,6aR,7S,8S,9bS)-6-(butyryloxy)-3,3a,4-trihydroxy-3,6,9-trimethyl-8-(((Z)-2-methylbut-2-enoyl)oxy)-2-oxo-2,3,3a,4,5,6,6a,7,8,9b-decahydroazuleno[4,5-b]furan-7-yl octanoate
  参考文献：
  名称：

  Elucidation of the topography of the thapsigargin binding site in the sarco-endoplasmic calcium ATPase

  摘要：

  Removal of each of the acyl groups of thapsigargin at O-3, O-8 and O-10 significant reduces the affinity of the inhibitors to the SERCA1a pump. Replacement of the acyl groups at O-3 and O-10 with flexible residues could be performed with only a minor decrease of the affinity, whereas introduction of voluminous stiff residues caused dramatic reduction of the affinity. The results can be rationalized on the basis of the interactions of thapsigargin with the SERCA1a pump as revealed from 3D X-ray structural models of thapsigargin bound to the SERCA1a. In conclusion the results confirm and elaborate the previously suggested pharmocophore model of thapsigargin. (C) 2010 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2010.06.032

文献信息

• Elucidation of the topography of the thapsigargin binding site in the sarco-endoplasmic calcium ATPase
  作者：Dorthe Mondrup Skytte、Jesper Vuust Møller、Huizhen Liu、Helle Østergren Nielsen、Louise Elsa Svenningsen、Christina Mernøe Jensen、Carl Erik Olsen、Søren Brøgger Christensen

  DOI：10.1016/j.bmc.2010.06.032

  日期：2010.8

  Removal of each of the acyl groups of thapsigargin at O-3, O-8 and O-10 significant reduces the affinity of the inhibitors to the SERCA1a pump. Replacement of the acyl groups at O-3 and O-10 with flexible residues could be performed with only a minor decrease of the affinity, whereas introduction of voluminous stiff residues caused dramatic reduction of the affinity. The results can be rationalized on the basis of the interactions of thapsigargin with the SERCA1a pump as revealed from 3D X-ray structural models of thapsigargin bound to the SERCA1a. In conclusion the results confirm and elaborate the previously suggested pharmocophore model of thapsigargin. (C) 2010 Elsevier Ltd. All rights reserved.