2-(2-oxo-2,3-dihydrobenzo[d]oxazole-6-sulfonamido)acetic acid | 650603-24-0

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 苯并恶唑类
• 英文名称: 2-(2-oxo-2,3-dihydrobenzo[d]oxazole-6-sulfonamido)acetic acid
• 英文别名: 2-[(2-oxo-3H-1,3-benzoxazol-6-yl)sulfonylamino]acetic acid
• CAS: 650603-24-0
• 化学式: C₉H₈N₂O₆S
• 分子量: 272.238
• InChiKey: NPUMZYDAABFWRG-UHFFFAOYSA-N

物化性质

• 密度：
  1.661±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -0.52
• 重原子数：
  18.0
• 可旋转键数：
  4.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.11
• 拓扑面积：
  129.47
• 氢给体数：
  3.0
• 氢受体数：
  5.0

反应信息

• 作为反应物：
  描述：

  2-(2-oxo-2,3-dihydrobenzo[d]oxazole-6-sulfonamido)acetic acid 、 对氨基苯腈 在 N-甲基吗啉 、 1-羟基苯并三唑 、 盐酸-N-乙基-Nˊ-(3-二甲氨基丙基)碳二亚胺 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 0.5h， 生成 N-(4-Cyanophenyl)-2-[(2-oxo-3H-1,3-benzoxazol-6-yl)sulfonylamino]acetamide
  参考文献：
  名称：

  Identification of a selective inhibitor of murine intestinal alkaline phosphatase (ML260) by concurrent ultra-high throughput screening against human and mouse isozymes

  摘要：

  Alkaline phosphatase (AP) isozymes are present in a wide range of species from bacteria to man and are capable of dephosphorylation and transphosphorylation of a wide spectrum of substrates in vitro. In humans, four AP isozymes have been identified-one tissue-nonspecific (TNAP) and three tissue-specific-named according to the tissue of their predominant expression: intestinal (IAP), placental (PLAP) and germ cell (GCAP) APs. Modulation of activity of the different AP isozymes may have therapeutic implications in distinct diseases and cellular processes. For instance, changes in the level of IAP activity can affect gut mucosa tolerance to microbial invasion due to the ability of IAP to detoxify bacterial endo-toxins, alter the absorption of fatty acids and affect ectopurinergic regulation of duodenal bicarbonate secretion. To identify isozyme selective modulators of the human and mouse IAPs, we developed a series of murine duodenal IAP (Akp3-encoded dIAP isozyme), human IAP (hIAP), PLAP, and TNAP assays. High throughput screening and subsequent SAR efforts generated a potent inhibitor of dIAP, ML260, with specificity for the Akp3-, compared to the Akp5- and Akp6-encoded mouse isozymes. (C) 2013 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2013.12.043
• 作为产物：
  描述：

  2-氧代-2,3-二氢苯并恶唑-6-磺酰氯 在 三乙胺 、 三氟乙酸 作用下， 以 二氯甲烷 为溶剂， 反应 0.3h， 生成 2-(2-oxo-2,3-dihydrobenzo[d]oxazole-6-sulfonamido)acetic acid
  参考文献：
  名称：

  Identification of a selective inhibitor of murine intestinal alkaline phosphatase (ML260) by concurrent ultra-high throughput screening against human and mouse isozymes

  摘要：

  Alkaline phosphatase (AP) isozymes are present in a wide range of species from bacteria to man and are capable of dephosphorylation and transphosphorylation of a wide spectrum of substrates in vitro. In humans, four AP isozymes have been identified-one tissue-nonspecific (TNAP) and three tissue-specific-named according to the tissue of their predominant expression: intestinal (IAP), placental (PLAP) and germ cell (GCAP) APs. Modulation of activity of the different AP isozymes may have therapeutic implications in distinct diseases and cellular processes. For instance, changes in the level of IAP activity can affect gut mucosa tolerance to microbial invasion due to the ability of IAP to detoxify bacterial endo-toxins, alter the absorption of fatty acids and affect ectopurinergic regulation of duodenal bicarbonate secretion. To identify isozyme selective modulators of the human and mouse IAPs, we developed a series of murine duodenal IAP (Akp3-encoded dIAP isozyme), human IAP (hIAP), PLAP, and TNAP assays. High throughput screening and subsequent SAR efforts generated a potent inhibitor of dIAP, ML260, with specificity for the Akp3-, compared to the Akp5- and Akp6-encoded mouse isozymes. (C) 2013 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2013.12.043

文献信息

• Identification of a selective inhibitor of murine intestinal alkaline phosphatase (ML260) by concurrent ultra-high throughput screening against human and mouse isozymes
  作者：Robert J. Ardecky、Ekaterina V. Bobkova、Tina Kiffer-Moreira、Brock Brown、Santhi Ganji、Jiwen Zou、Ian Pass、Sonoko Narisawa、Flávia Godoy Iano、Craig Rosenstein、Anton Cheltsov、Justin Rascon、Michael Hedrick、Carlton Gasior、Anita Forster、Shenghua Shi、Russell Dahl、Stefan Vasile、Ying Su、Eduard Sergienko、Thomas D.Y. Chung、Jonathan Kaunitz、Marc F. Hoylaerts、Anthony B. Pinkerton、José Luis Millán

  DOI：10.1016/j.bmcl.2013.12.043

  日期：2014.2

  Alkaline phosphatase (AP) isozymes are present in a wide range of species from bacteria to man and are capable of dephosphorylation and transphosphorylation of a wide spectrum of substrates in vitro. In humans, four AP isozymes have been identified-one tissue-nonspecific (TNAP) and three tissue-specific-named according to the tissue of their predominant expression: intestinal (IAP), placental (PLAP) and germ cell (GCAP) APs. Modulation of activity of the different AP isozymes may have therapeutic implications in distinct diseases and cellular processes. For instance, changes in the level of IAP activity can affect gut mucosa tolerance to microbial invasion due to the ability of IAP to detoxify bacterial endo-toxins, alter the absorption of fatty acids and affect ectopurinergic regulation of duodenal bicarbonate secretion. To identify isozyme selective modulators of the human and mouse IAPs, we developed a series of murine duodenal IAP (Akp3-encoded dIAP isozyme), human IAP (hIAP), PLAP, and TNAP assays. High throughput screening and subsequent SAR efforts generated a potent inhibitor of dIAP, ML260, with specificity for the Akp3-, compared to the Akp5- and Akp6-encoded mouse isozymes. (C) 2013 Elsevier Ltd. All rights reserved.