(5Z,7E)-9,10-seco-2α-chloro-cholesta-5,7,10(19)-trien-1β,3β,25-triol

• 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
• 英文名称: (5Z,7E)-9,10-seco-2α-chloro-cholesta-5,7,10(19)-trien-1β,3β,25-triol
• 英文别名: 2alpha-chloro-1beta,25-dihydroxyvitamin D3/2alpha-chloro-1beta,25-dihydroxycholecalciferol；(1R,2S,3S,5Z)-5-[(2E)-2-[(1R,3aS,7aR)-1-[(2R)-6-hydroxy-6-methylheptan-2-yl]-7a-methyl-2,3,3a,5,6,7-hexahydro-1H-inden-4-ylidene]ethylidene]-2-chloro-4-methylidenecyclohexane-1,3-diol
• 化学式: C₂₇H₄₃ClO₃
• 分子量: 451.09
• InChiKey: YBTPGKMEEDFQBI-CHGYUPLRSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.4
• 重原子数：
  31
• 可旋转键数：
  6
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.78
• 拓扑面积：
  60.7
• 氢给体数：
  3
• 氢受体数：
  3

反应信息

• 作为产物：
  描述：

  在 盐酸 、 联苯 、 2,7-dimethyl-3,6-diaza-cyclohepta-1,6-diene tetrafluoroborate 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 9.33h， 生成 (5Z,7E)-9,10-seco-2α-chloro-cholesta-5,7,10(19)-trien-1β,3β,25-triol
  参考文献：
  名称：

  Synthesis and biological activities of 2α-chloro-1-epicalcitriol and 1-epicalcitriol 11Dedicated to Prof. Dr. P. Welzel on the occasion of his 60th birthday.

  摘要：

  Anomalous diequatorial epoxide ring opening of 1 beta,2 beta-oxido-cholesta-5,7-diene-3 beta,25-diol 1 produces the 1 beta-hydroxy-2 alpha-chloro-provitamin 2 and its corresponding 1 beta-hydroxy-provitamin 3. The provitamins 2 and 3 are transformed by irradiation and thermal isomerization to 2 alpha-chloro-1-epicalcitriol NS3 (4) and 1-epicalcitriol NS8 (5), respectively. These two A-ring derivatives were tested for their in vitro biological activity in the mesenchymal, murine cell line C3H10T1/2, and their effects were compared with those of the native vitamin D-3 derivatives 25(OH)D-3 and 1,25(OH)(2)D-3. NS3 and NS8 showed marked differences in their nffinitYfor the vitamin D binding protein (DBP) and in their ability to inhibit cell proliferation. NS8 has the ability to bind to a high-affinity DBP-binding site for which 25(OH)D-3 has none affinity. The 2 alpha-chloro-substitution (NS3) prevents binding to the postulated noncompetitive, NS8-specific DBP-binding site and diminishes the affinity to the vitamin D receptor (VDR) and therefore diminishing NS3's biological abilities. The elucidation of the structure-function relationships at the DBP-binding-sites could have major impact on the development of new vitamin D, derivatives with extended serum half-life. (C) 1998 by Elsevier Science Inc.

  DOI：

  10.1016/s0039-128x(97)00106-2