(R)-2-(6-methoxybenzo[d]thiazol-2-yl)-5,5-dimethyl-4,5-dihydrothiazole-4-carboxylic acid

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: (R)-2-(6-methoxybenzo[d]thiazol-2-yl)-5,5-dimethyl-4,5-dihydrothiazole-4-carboxylic acid
• 英文别名: (4R)-2-(6-methoxy-1,3-benzothiazol-2-yl)-5,5-dimethyl-4H-1,3-thiazole-4-carboxylic acid
• 化学式: C₁₄H₁₄N₂O₃S₂
• 分子量: 322.409
• InChiKey: CJHATKORAPBBQD-SNVBAGLBSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.2
• 重原子数：
  21
• 可旋转键数：
  3
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.36
• 拓扑面积：
  125
• 氢给体数：
  1
• 氢受体数：
  7

反应信息

• 作为产物：
  描述：

  L-青霉胺 、 2-氰基-6-甲氧基苯并噻唑 在 sodium carbonate 作用下， 以 水 为溶剂， 反应 3.0h， 生成 (R)-2-(6-methoxybenzo[d]thiazol-2-yl)-5,5-dimethyl-4,5-dihydrothiazole-4-carboxylic acid
  参考文献：
  名称：

  Luciferin and derivatives as a DYRK selective scaffold for the design of protein kinase inhibitors

  摘要：

  D-Luciferin is widely used as a substrate in luciferase catalysed bioluminescence assays for in vitro studies. However, little is known about cross reactivity and potential interference of D-luciferin with other enzymes. We serendipitously found that firefly luciferin inhibited the CDK2/Cyclin A protein kinase. Inhibition profiling of D-luciferin over a 103-protein kinase panel showed significant inhibition of a small set of protein kinases, in particular the DYRK-family, but also other members of the CMGC-group, including ERK8 and CK2. Inhibition profiling on a 16-member focused library derived from D-luciferin confirms that D-luciferin represents a DYRK-selective chemotype of fragment-like molecular weight. Thus, observation of its inhibitory activity and the initial SAR information reported here promise to be useful for further design of protein kinase inhibitors with related scaffolds. (C) 2015 Elsevier Masson SAS. All rights reserved.

  DOI：

  10.1016/j.ejmech.2015.02.035

文献信息

• Luciferin and derivatives as a DYRK selective scaffold for the design of protein kinase inhibitors
  作者：Ulli Rothweiler、Jonas Eriksson、Wenche Stensen、Frederick Leeson、Richard A. Engh、John S. Svendsen

  DOI：10.1016/j.ejmech.2015.02.035

  日期：2015.4

  D-Luciferin is widely used as a substrate in luciferase catalysed bioluminescence assays for in vitro studies. However, little is known about cross reactivity and potential interference of D-luciferin with other enzymes. We serendipitously found that firefly luciferin inhibited the CDK2/Cyclin A protein kinase. Inhibition profiling of D-luciferin over a 103-protein kinase panel showed significant inhibition of a small set of protein kinases, in particular the DYRK-family, but also other members of the CMGC-group, including ERK8 and CK2. Inhibition profiling on a 16-member focused library derived from D-luciferin confirms that D-luciferin represents a DYRK-selective chemotype of fragment-like molecular weight. Thus, observation of its inhibitory activity and the initial SAR information reported here promise to be useful for further design of protein kinase inhibitors with related scaffolds. (C) 2015 Elsevier Masson SAS. All rights reserved.