(R,E)-2-acetamido-3-((3-methyl-4-(naphthalen-2-yloxy)but-2-en-1-yl)thio)propanoic acid | 1333080-97-9

• 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: (R,E)-2-acetamido-3-((3-methyl-4-(naphthalen-2-yloxy)but-2-en-1-yl)thio)propanoic acid
• 英文别名: (2R)-2-acetamido-3-[(E)-3-methyl-4-naphthalen-2-yloxybut-2-enyl]sulfanylpropanoic acid
• CAS: 1333080-97-9
• 化学式: C₂₀H₂₃NO₄S
• 分子量: 373.473
• InChiKey: FVNDRYXZEYGDDJ-JNMQVBFRSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.7
• 重原子数：
  26
• 可旋转键数：
  9
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.3
• 拓扑面积：
  101
• 氢给体数：
  2
• 氢受体数：
  5

反应信息

• 作为产物：
  描述：

  (E)-[(4-bromo-3-methylbut-2-en-1-yl)oxy](tert-butyl)dimethylsilane 在 N-氯代丁二酰亚胺 、 二甲基硫 、 四丁基氟化铵 、 sodium hydride 作用下， 生成 (R,E)-2-acetamido-3-((3-methyl-4-(naphthalen-2-yloxy)but-2-en-1-yl)thio)propanoic acid
  参考文献：
  名称：

  Lipid and sulfur substituted prenylcysteine analogs as human Icmt inhibitors

  摘要：

  Inhibition of isoprenylcysteine carboxyl methyltransferase (Icmt) offers a promising strategy for K-Ras driven cancers. We describe the synthesis and inhibitory activity of substrate-based analogs derived from several novel scaffolds. Modifications of both the prenyl group and thioether of N-acetyl-S-farnesyl-L-cysteine (AFC), a substrate for human Icmt (hIcmt), have resulted in low micromolar inhibitors of Icmt and have given insights into the nature of the prenyl binding site of hIcmt. (C) 2011 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2011.06.053

文献信息

• Lipid and sulfur substituted prenylcysteine analogs as human Icmt inhibitors
  作者：Joel A. Bergman、Kalub Hahne、Christine A. Hrycyna、Richard A. Gibbs

  DOI：10.1016/j.bmcl.2011.06.053

  日期：2011.9

  Inhibition of isoprenylcysteine carboxyl methyltransferase (Icmt) offers a promising strategy for K-Ras driven cancers. We describe the synthesis and inhibitory activity of substrate-based analogs derived from several novel scaffolds. Modifications of both the prenyl group and thioether of N-acetyl-S-farnesyl-L-cysteine (AFC), a substrate for human Icmt (hIcmt), have resulted in low micromolar inhibitors of Icmt and have given insights into the nature of the prenyl binding site of hIcmt. (C) 2011 Elsevier Ltd. All rights reserved.