5-(aminooxy)-5-(3-chlorophenyl)-N-phenylpentanamide

• 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: 5-(aminooxy)-5-(3-chlorophenyl)-N-phenylpentanamide
• 英文别名: 5-aminooxy-5-(3-chlorophenyl)-N-phenylpentanamide
• 化学式: C₁₇H₁₉ClN₂O₂
• 分子量: 318.803
• InChiKey: MQZXPUVUSFHKGT-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3
• 重原子数：
  22
• 可旋转键数：
  7
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.24
• 拓扑面积：
  64.4
• 氢给体数：
  2
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  5-(aminooxy)-5-(3-chlorophenyl)-N-phenylpentanamide 在 盐酸 作用下， 以 乙醚 、 水 为溶剂， 以62%的产率得到5-(aminooxy)-5-(3-chlorophenyl)-N-phenylpentanamide hydrochloride
  参考文献：
  名称：

  Diaryl hydroxylamines as pan or dual inhibitors of indoleamine 2,3-dioxygenase-1, indoleamine 2,3-dioxygenase-2 and tryptophan dioxygenase

  摘要：

  Tryptophan (Trp) catabolizing enzymes play an important and complex role in the development of cancer. Significant evidence implicates them in a range of inflammatory and immunosuppressive activities. Whereas inhibitors of indoleamine 2,3-dioxygenase-1 (IDO1) have been reported and analyzed in the clinic, fewer inhibitors have been described for tryptophan dioxygenase (TDO) and indoleamine 2,3-dioxygenase-2 (IDO2) which also have been implicated more recently in cancer, inflammation and immune control. Consequently the development of dual or pan inhibitors of these Trp catabolizing enzymes may represent a therapeutically important area of research. This is the first report to describe the development of dual and pan inhibitors of IDO1, TDO and IDO2. (C) 2018 Elsevier Masson SAS. All rights reserved.

  DOI：

  10.1016/j.ejmech.2018.11.010
• 作为产物：
  描述：

  (3-chlorophenyl)magnesium bromide 在 sodium tetrahydroborate 、 N-羟基邻苯二甲酰亚胺 、 双二甲胺基乙基醚 、 偶氮二甲酸二异丙酯 、 (1-cyano-2-ethoxy-2-oxoethylidenaminooxy)dimethylaminomorpholinocarbenium hexafluorophosphate 、 N,N-二异丙基乙胺 、 三苯基膦 作用下， 以 四氢呋喃 、 甲醇 、 二氯甲烷 为溶剂， 反应 6.92h， 生成 5-(aminooxy)-5-(3-chlorophenyl)-N-phenylpentanamide
  参考文献：
  名称：

  Diaryl hydroxylamines as pan or dual inhibitors of indoleamine 2,3-dioxygenase-1, indoleamine 2,3-dioxygenase-2 and tryptophan dioxygenase

  摘要：

  Tryptophan (Trp) catabolizing enzymes play an important and complex role in the development of cancer. Significant evidence implicates them in a range of inflammatory and immunosuppressive activities. Whereas inhibitors of indoleamine 2,3-dioxygenase-1 (IDO1) have been reported and analyzed in the clinic, fewer inhibitors have been described for tryptophan dioxygenase (TDO) and indoleamine 2,3-dioxygenase-2 (IDO2) which also have been implicated more recently in cancer, inflammation and immune control. Consequently the development of dual or pan inhibitors of these Trp catabolizing enzymes may represent a therapeutically important area of research. This is the first report to describe the development of dual and pan inhibitors of IDO1, TDO and IDO2. (C) 2018 Elsevier Masson SAS. All rights reserved.

  DOI：

  10.1016/j.ejmech.2018.11.010

文献信息

• Diaryl hydroxylamines as pan or dual inhibitors of indoleamine 2,3-dioxygenase-1, indoleamine 2,3-dioxygenase-2 and tryptophan dioxygenase
  作者：Maria Winters、James B. DuHadaway、Khoa N. Pham、Ariel Lewis-Ballester、Shorouk Badir、Jenny Wai、Eesha Sheikh、Syun-Ru Yeh、George C. Prendergast、Alexander J. Muller、William P. Malachowski

  DOI：10.1016/j.ejmech.2018.11.010

  日期：2019.1

  Tryptophan (Trp) catabolizing enzymes play an important and complex role in the development of cancer. Significant evidence implicates them in a range of inflammatory and immunosuppressive activities. Whereas inhibitors of indoleamine 2,3-dioxygenase-1 (IDO1) have been reported and analyzed in the clinic, fewer inhibitors have been described for tryptophan dioxygenase (TDO) and indoleamine 2,3-dioxygenase-2 (IDO2) which also have been implicated more recently in cancer, inflammation and immune control. Consequently the development of dual or pan inhibitors of these Trp catabolizing enzymes may represent a therapeutically important area of research. This is the first report to describe the development of dual and pan inhibitors of IDO1, TDO and IDO2. (C) 2018 Elsevier Masson SAS. All rights reserved.