tert-butyl N-(thiophene-3-carbonylamino)carbamate | 1017126-83-8

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 噻吩类
• 英文名称: tert-butyl N-(thiophene-3-carbonylamino)carbamate
• CAS: 1017126-83-8
• 化学式: C₁₀H₁₄N₂O₃S
• 分子量: 242.299
• InChiKey: NLMDZPOUUBOAOV-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.8
• 重原子数：
  16
• 可旋转键数：
  3
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.4
• 拓扑面积：
  95.7
• 氢给体数：
  2
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  tert-butyl N-(thiophene-3-carbonylamino)carbamate 在 盐酸 作用下， 以 1,4-二氧六环 为溶剂， 生成 3-三噻吩羧酸肼
  参考文献：
  名称：

  Triazole derivatives as non-nucleoside inhibitors of HIV-1 reverse transcriptase—Structure–activity relationships and crystallographic analysis

  摘要：

  A series of 3,4,5-trisubstituted 1,2,4-4H triazole derivatives was synthesized and investigated for HIV-1 reverse transcriptase inhibition. An X-ray structure with HIV-1 RT secured the binding mode and allowed the key interactions with the enzyme to be identified.

  DOI：

  10.1016/j.bmcl.2007.11.127
• 作为产物：
  描述：

  3-噻吩甲酰氯 、 肼基甲酸叔丁酯 在 TEA 作用下， 以 四氢呋喃 为溶剂， 生成 tert-butyl N-(thiophene-3-carbonylamino)carbamate
  参考文献：
  名称：

  Triazole derivatives as non-nucleoside inhibitors of HIV-1 reverse transcriptase—Structure–activity relationships and crystallographic analysis

  摘要：

  A series of 3,4,5-trisubstituted 1,2,4-4H triazole derivatives was synthesized and investigated for HIV-1 reverse transcriptase inhibition. An X-ray structure with HIV-1 RT secured the binding mode and allowed the key interactions with the enzyme to be identified.

  DOI：

  10.1016/j.bmcl.2007.11.127

文献信息

• Triazole derivatives as non-nucleoside inhibitors of HIV-1 reverse transcriptase—Structure–activity relationships and crystallographic analysis
  作者：Thorsten A. Kirschberg、Mini Balakrishnan、Wei Huang、Rebecca Hluhanich、Nilima Kutty、Albert C. Liclican、Damian J. McColl、Neil H. Squires、Eric B. Lansdon

  DOI：10.1016/j.bmcl.2007.11.127

  日期：2008.2

  A series of 3,4,5-trisubstituted 1,2,4-4H triazole derivatives was synthesized and investigated for HIV-1 reverse transcriptase inhibition. An X-ray structure with HIV-1 RT secured the binding mode and allowed the key interactions with the enzyme to be identified.