O-(tert-butyl) S-[2-(hydroxymethyl)phenyl] thiocarbonate | 396725-76-1

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: O-(tert-butyl) S-[2-(hydroxymethyl)phenyl] thiocarbonate
• 英文别名: 2-S-(t-butoxycarbonyl)mercaptobenzyl alcohol；Tert-butyl [2-(hydroxymethyl)phenyl]sulfanylformate
• CAS: 396725-76-1
• 化学式: C₁₂H₁₆O₃S
• 分子量: 240.323
• InChiKey: MBNHTKGIRIGKOW-UHFFFAOYSA-N

物化性质

• 沸点：
  356.8±44.0 °C(Predicted)
• 密度：
  1.18±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  2.7
• 重原子数：
  16
• 可旋转键数：
  5
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.42
• 拓扑面积：
  71.8
• 氢给体数：
  1
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  O-(tert-butyl) S-[2-(hydroxymethyl)phenyl] thiocarbonate 在 sodium tetrahydroborate 、 草酰氯 、 溶剂黄146 、 二甲基亚砜 、 三乙胺 、 三氟乙酸 作用下， 以 二氯甲烷 为溶剂， 反应 3.5h， 生成 FTI-2315
  参考文献：
  名称：

  Design and Synthesis of Potent Nonpeptidic Farnesyltransferase Inhibitors Based on a Terphenyl Scaffold

  摘要：

  By modification of key carboxylate, hydrophobic, and zinc-binding groups projected from a sterically restricted terphenyl scaffold, a series of simple and nonpeptide mimetics of the Cys-Val-Ile-Met tetrapeptide substrate of protein farnesyltransferase (FTase) have been designed and synthesized. A crystal structure of 4-nitro-2-phenyl-3'-methoxycarbonylbiphenyl shows that the triphenyl fragment provides a large hydrophobic surface that potentially mimics the hydrophobic side chains of the three terminal residues in the tetrapeptide. 2-Phenyl-3-(N-(1-(4-eyanobenzyl)-1H-imidazol-5-yl)methyl)amino-3'carboxylbiphenyl, in which the free thiol group was replaced with a 1-(4-cyanobenzyl)imidazole group, shows submicromolar inhibition activity against FTase in vitro and inhibits H-Ras processing in whole cells.

  DOI：

  10.1021/jm0103099
• 作为产物：
  描述：

  2-(S-t-butoxycarbonyl)mercaptobenzoic acid 在 sodium tetrahydroborate 、 三乙胺 作用下， 以 四氢呋喃 为溶剂， 反应 1.5h， 生成 O-(tert-butyl) S-[2-(hydroxymethyl)phenyl] thiocarbonate
  参考文献：
  名称：

  Design and Synthesis of Potent Nonpeptidic Farnesyltransferase Inhibitors Based on a Terphenyl Scaffold

  摘要：

  By modification of key carboxylate, hydrophobic, and zinc-binding groups projected from a sterically restricted terphenyl scaffold, a series of simple and nonpeptide mimetics of the Cys-Val-Ile-Met tetrapeptide substrate of protein farnesyltransferase (FTase) have been designed and synthesized. A crystal structure of 4-nitro-2-phenyl-3'-methoxycarbonylbiphenyl shows that the triphenyl fragment provides a large hydrophobic surface that potentially mimics the hydrophobic side chains of the three terminal residues in the tetrapeptide. 2-Phenyl-3-(N-(1-(4-eyanobenzyl)-1H-imidazol-5-yl)methyl)amino-3'carboxylbiphenyl, in which the free thiol group was replaced with a 1-(4-cyanobenzyl)imidazole group, shows submicromolar inhibition activity against FTase in vitro and inhibits H-Ras processing in whole cells.

  DOI：

  10.1021/jm0103099

文献信息

• A simple acylation of thiols with anhydrides
  作者：Andrea Temperini、Diego Annesi、Lorenzo Testaferri、Marcello Tiecco

  DOI：10.1016/j.tetlet.2010.07.126

  日期：2010.10

  Different thiols were efficiently acylated at room temperature with different anhydrides in the presence of potassium carbonate. Chemoselective protection of thiol in the presence of hydroxy group was achieved using di-tert-butyl dicarbonate and isatoic anhydride.

  在碳酸钾存在下，在室温下用不同的酸酐将不同的硫醇有效地酰化。使用二-达到在羟基基团存在的硫醇化学选择性保护叔丁基酯和靛红酸酐。
• Design and Synthesis of Potent Nonpeptidic Farnesyltransferase Inhibitors Based on a Terphenyl Scaffold
  作者：Junko Ohkanda、Jeffrey W. Lockman、Mohit A. Kothare、Yimin Qian、Michelle A. Blaskovich、Said M. Sebti、Andrew D. Hamilton

  DOI：10.1021/jm0103099

  日期：2002.1.1

  By modification of key carboxylate, hydrophobic, and zinc-binding groups projected from a sterically restricted terphenyl scaffold, a series of simple and nonpeptide mimetics of the Cys-Val-Ile-Met tetrapeptide substrate of protein farnesyltransferase (FTase) have been designed and synthesized. A crystal structure of 4-nitro-2-phenyl-3'-methoxycarbonylbiphenyl shows that the triphenyl fragment provides a large hydrophobic surface that potentially mimics the hydrophobic side chains of the three terminal residues in the tetrapeptide. 2-Phenyl-3-(N-(1-(4-eyanobenzyl)-1H-imidazol-5-yl)methyl)amino-3'carboxylbiphenyl, in which the free thiol group was replaced with a 1-(4-cyanobenzyl)imidazole group, shows submicromolar inhibition activity against FTase in vitro and inhibits H-Ras processing in whole cells.