ilicicolin C | 22562-67-0

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: ilicicolin C
• 英文别名: LL-Z 1272δ；5-chloro-2,4-dihydroxy-6-methyl-3-[(E)-3-methyl-5-[(1S,2R,6R)-1,2,6-trimethyl-3-oxocyclohexyl]pent-2-enyl]benzaldehyde
• CAS: 22562-67-0
• 化学式: C₂₃H₃₁ClO₄
• 分子量: 406.95
• InChiKey: IJEHYEVNWOYGMS-WGUBEYSISA-N

物化性质

• 沸点：
  544.8±29.0 °C(Predicted)
• 密度：
  1.143±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  6.4
• 重原子数：
  28
• 可旋转键数：
  6
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.57
• 拓扑面积：
  74.6
• 氢给体数：
  2
• 氢受体数：
  4

安全信息

• WGK Germany：
  3

反应信息

• 作为产物：
  描述：

  LL-Z 1272ε 在 sodium chlorate 、 sodium dihydrogenphosphate 、 双氧水 作用下， 以 水 、 乙腈 为溶剂， 生成 ilicicolin C
  参考文献：
  名称：

  Chemistry and Biology of Cylindrols:  Novel Inhibitors of Ras Farnesyl-Protein Transferase from Cylindrocarpon lucidum

  摘要：

  Farnesyl-protein transferase (FPTase) is an enzyme responsible for the farnesylation of Ras protein. Farnesylation is required for cell-transforming activity in several tumor-types, and therefore, inhibition of FPTase activity may be a potential target for anticancer drugs. Our continued search for novel inhibitors led to the isolation of a number of bicyclic resorcinaldehyde cyclohexanone derivatives named here cylindrols A(1) to A(4), cylindrols B and B-1, and a number of known compounds, from Cylindrocarpon Lucidum. The compounds were isolated by bioassay-guided separation using Sephadex LH-20, silica gel, and reverse phase HPLC. Structures were elucidated by extensive application of 2D NMR and X-ray crystallography. The determination of absolute stereochemistry was accomplished by CD measurements. Chemical transformations of the most abundant compound resulted in a number of key derivatives which were critical for the evaluation of structure activity relationship. These compounds are members of ascochlorin family and showed a wide range of inhibitory activity (0.7 mu M to > 140 mu M) against FPTase. The FPTase activity was noncompetitive with respect to both substrates. Isolation, structures, chemical transformations, and FPTase activity are discussed in detail.

  DOI：

  10.1021/jo961074p

文献信息

• MEROTERPENOID COMPOUNDS FOR USE IN THE PREVENTION AND TREATMENT OF A NEUROLOGICAL DISORDER
  申请人：SOCIETE DES PRODUITS NESTLE S.A.

  公开号：US20200405676A1

  公开（公告）日：2020-12-31

  The present invention relates to a compound, in particular a meroterpenoid compound, or salt thereof, for use in the prevention and/or treatment of a neurological disorder in an individual. The compound of the invention can promote lactate secretion. A composition comprising the compound of the invention, and a food or food extract enriched with said compound or composition is also provided.
• Chemistry and Biology of Cylindrols:  Novel Inhibitors of Ras Farnesyl-Protein Transferase from <i>Cylindrocarpon lucidum</i>
  作者：Sheo B. Singh、Richard G. Ball、Gerald F. Bills、Carmen Cascales、Jackson B. Gibbs、Michael A. Goetz、Karst Hoogsteen、Rosalind G. Jenkins、Jerrold M. Liesch、Russell B. Lingham、Keith C. Silverman、Deborah L. Zink

  DOI：10.1021/jo961074p

  日期：1996.1.1

  Farnesyl-protein transferase (FPTase) is an enzyme responsible for the farnesylation of Ras protein. Farnesylation is required for cell-transforming activity in several tumor-types, and therefore, inhibition of FPTase activity may be a potential target for anticancer drugs. Our continued search for novel inhibitors led to the isolation of a number of bicyclic resorcinaldehyde cyclohexanone derivatives named here cylindrols A(1) to A(4), cylindrols B and B-1, and a number of known compounds, from Cylindrocarpon Lucidum. The compounds were isolated by bioassay-guided separation using Sephadex LH-20, silica gel, and reverse phase HPLC. Structures were elucidated by extensive application of 2D NMR and X-ray crystallography. The determination of absolute stereochemistry was accomplished by CD measurements. Chemical transformations of the most abundant compound resulted in a number of key derivatives which were critical for the evaluation of structure activity relationship. These compounds are members of ascochlorin family and showed a wide range of inhibitory activity (0.7 mu M to > 140 mu M) against FPTase. The FPTase activity was noncompetitive with respect to both substrates. Isolation, structures, chemical transformations, and FPTase activity are discussed in detail.