2-(tert-butyldimethylsilyloxy)-N-(p-(tert-butyldimethylsilyloxy)phenyl)thioacetamide | 1033617-40-1

• 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: 2-(tert-butyldimethylsilyloxy)-N-(p-(tert-butyldimethylsilyloxy)phenyl)thioacetamide
• CAS: 1033617-40-1
• 化学式: C₂₀H₃₇NO₂SSi₂
• 分子量: 411.756
• InChiKey: YGPJNJJHDOJJTA-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  6.83
• 重原子数：
  26.0
• 可旋转键数：
  6.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.65
• 拓扑面积：
  30.49
• 氢给体数：
  1.0
• 氢受体数：
  3.0

反应信息

• 作为反应物：
  描述：

  2,3,4,6-tetra-O-acetyl-D-glucosyl-1-amine 、 2-(tert-butyldimethylsilyloxy)-N-(p-(tert-butyldimethylsilyloxy)phenyl)thioacetamide 在 trimethoxonium tetrafluoroborate 、 4 A molecular sieve 、 N-溴代丁二酰亚胺(NBS) 作用下， 以 二氯甲烷 为溶剂， 反应 16.25h， 以89%的产率得到N-(p-(tert-butyldimethylsilyloxy)phenyl)-N'-(2,3,4,6-tetraacetyl-1-β-D-glucopyranosyl)-(tert-butyldimethylsilyloxy)methylamidine
  参考文献：
  名称：

  Affinity purification and characterization of a key enzyme responsible for circadian rhythmic control of nyctinasty in Lespedeza cuneata L

  摘要：

  The synthesis of an affinity gel aimed at leaf-opening factor beta-glucosidase (LOFG) and affinity purification of LOFG is presented. A gluconamidine-based beta-glucosidase inhibitor was used as the ligand of the affinity gel. beta-Glucosidase exhibiting an activity shift throughout the day was selectively purified from Lespedeza cuneata Don by the affinity gel. The resulting LOFG exhibited high substrate specificity toward the leaf-opening factor. (c) 2008 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2008.02.035
• 作为产物：
  描述：

  2-(tert-butyldimethylsilyloxy)-N-(p-(tert-butyldimethylsilyloxy)phenyl)acetamide 在 劳森试剂 作用下， 以 甲苯 为溶剂， 反应 2.0h， 以87%的产率得到2-(tert-butyldimethylsilyloxy)-N-(p-(tert-butyldimethylsilyloxy)phenyl)thioacetamide
  参考文献：
  名称：

  Affinity purification and characterization of a key enzyme responsible for circadian rhythmic control of nyctinasty in Lespedeza cuneata L

  摘要：

  The synthesis of an affinity gel aimed at leaf-opening factor beta-glucosidase (LOFG) and affinity purification of LOFG is presented. A gluconamidine-based beta-glucosidase inhibitor was used as the ligand of the affinity gel. beta-Glucosidase exhibiting an activity shift throughout the day was selectively purified from Lespedeza cuneata Don by the affinity gel. The resulting LOFG exhibited high substrate specificity toward the leaf-opening factor. (c) 2008 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2008.02.035